concanavalin-a and Adenocarcinoma

Lung cancer is one of the most important avoidable causes of death around the world, the most widespread carcinoma, with a very poor prognosis, and is the leading cause of cancer death in both developed and developing countries. We report morphological and biological behavior characteristics of a tumor that arose in only one BALB/c mouse of an experimental group treated with urethane, a chemical lung-tumorigenic agent. Morphological and immunochemical analysis indicated phenotypic compatibility with a lung adenocarcinoma. The tumor was named LAC1 (lung adenocarcinoma 1). Implant success in eight LAC1-bearing mice generations was 100%, with a fast evolution (58 survival days) and good metastatic capacity (41% of animals with metastases). The tumor induced a paraneoplastic syndrome characterized by anemia, neutrophilia, cachexia, splenomegaly and thymic atrophy. The lymphoproliferation to Con A was altered in tumor-bearing mice. This lung adenocarcinoma may be a useful experimental model for studying tumor progression, paraneoplastic syndromes and immunology in carcinogenic studies.

Topics: Adenocarcinoma; Animals; Cell Proliferation; Cells, Cultured; Concanavalin A; Erythrocyte Count; Hematocrit; Immunohistochemistry; Leukocytes, Mononuclear; Lung Neoplasms; Mice; Mice, Inbred BALB C; Models, Animal; Neoplasm Transplantation; Neutropenia; Organ Size; Splenomegaly; Thymus Gland; Urethane

The prognostic value of histologic classifications of gastric adenocarcinoma is controversial, although they have been commonly used. The clinical significance of the mucin phenotype has not been clarified. This study was conducted to determine the clinical significance of mucin phenotype as a possible prognostic factor. Mucin histochemistry by paradoxical concanavalin A (Con A) staining and immunostaining for 45M1, MUC2 glycoprotein and CD10 of mucin was performed in surgically obtained paraffin-embedded specimens from 106 gastric adenocarcinomas. We determined their mucin phenotypes and analyzed their relationships with clinical and histopathologic variables and survival rates. Among 106 gastric adenocarcinomas, 37 (34.9%), 35 (33.0%), 22 (20.8%) and 12 (11.3%) expressed the intestinal (I-), the gastric (G-), mixed (M-), and undetermined (U-) phenotypes, respectively. Although the mucin phenotype correlated well with histologic differentiation (p=0.000) and Lauren's classification of a tumor (p=0.003), it did not accord completely with them. There was no relationship between mucin phenotype and other patient clinicopathologic variables. No statistically significant difference in survival was observed among mucin phenotypes on univariate (p=0.089) and multivariate (p=0.088) analyses. However, the patients with I-phenotype tumor had a significantly better outcome than those with non-I-phenotype tumor on univariate (p=0.023) and multivariate (p=0.049) analyses. In conclusion, the mucin phenotype did not accord completely with histologic differentiation and Lauren's classification of gastric adenocarcinoma, despite a well-defined correlation between them. I-phenotypic expression, but not the histologic differentiation and Lauren's classification, was found to be an independent good prognostic factor of gastric cancers.

Topics: Adenocarcinoma; Adult; Aged; Biomarkers, Tumor; Concanavalin A; Female; Humans; Immunohistochemistry; Kaplan-Meier Estimate; Male; Middle Aged; Mucin-2; Mucins; Neoplasm Staging; Neprilysin; Phenotype; Prognosis; Stomach Neoplasms

Combinations of cellular immune-based therapies with chemotherapy and other antitumour agents may be of significant clinical benefit in the treatment of many forms of cancer. Gamma delta (gammadelta) T cells are of particular interest for use in such combined therapies due to their potent antitumour cytotoxicity and relative ease of generation in vitro. Here, we demonstrate high levels of cytotoxicity against solid tumour-derived cell lines with combination treatment utilizing Vgamma9Vdelta2 T cells, chemotherapeutic agents and the bisphosphonate, zoledronate. Pre-treatment with low concentrations of chemotherapeutic agents or zoledronate sensitized tumour cells to rapid killing by Vgamma9Vdelta2 T cells with levels of cytotoxicity approaching 90%. In addition, zoledronate enhanced the chemotherapy-induced sensitization of tumour cells to Vgamma9Vdelta2 T cell cytotoxicity resulting in almost 100% lysis of tumour targets in some cases. Vgamma9Vdelta2 T cell cytotoxicity was mediated by perforin following TCR-dependent and isoprenoid-mediated recognition of tumour cells. Production of IFN-gamma by Vgamma9Vdelta2 T cells was also induced after exposure to sensitized targets. We conclude that administration of Vgamma9Vdelta2 T cells at suitable intervals after chemotherapy and zoledronate may substantially increase antitumour activities in a range of malignancies.

Topics: Adenocarcinoma; Antineoplastic Agents; Apoptosis; Breast Neoplasms; Burkitt Lymphoma; Carcinoma; Cell Line, Tumor; Cisplatin; Colorectal Neoplasms; Concanavalin A; Cytotoxicity, Immunologic; Diphosphonates; Doxorubicin; Drug Screening Assays, Antitumor; Drug Synergism; Etoposide; Female; Genes, T-Cell Receptor delta; Genes, T-Cell Receptor gamma; Humans; Imidazoles; Interferon-gamma; Lovastatin; Lung Neoplasms; Male; Membrane Glycoproteins; Neoplasms; Perforin; Pore Forming Cytotoxic Proteins; Prostatic Neoplasms; Receptors, Antigen, T-Cell, gamma-delta; T-Lymphocyte Subsets; Urinary Bladder Neoplasms; Vincristine; Zoledronic Acid

It has been proved that some differentiated-type gastric carcinomas have a gastric phenotype. Similarly, it can be conjectured that some undifferentiated-type gastric carcinomas have an intestinal phenotype and that there are biological differences between undifferentiated-type gastric carcinomas with a gastric phenotype and those with an intestinal phenotype. We classified the phenotypes of early undifferentiated-type gastric carcinomas and investigated the relationship between their biological behavior and the phenotypes.. Sixty lesions of intramucosal undifferentiated-type gastric carcinoma were classified into four phenotypes; gastric type, incomplete-intestinal type, complete-intestinal type, and unclassified type, according to the expression of CD10, MUC2, small-intestinal mucinous antigen (SIMA), human gastric mucin (HGM), or concanavalin A (ConA).. The incidence of gastric-type carcinoma, incomplete-intestinal-type carcinoma, and complete-intestinal-type carcinoma was 33% (20 cases), 65% (39 cases), and 2% (1 case), respectively. There was no significant difference in any of the clinicopathological factors examined between the 20 gastric-type carcinomas and the 40 intestinal-type carcinomas, but there were significant differences in the morphological findings. Intestinal-type carcinomas had a glandular structure more frequently than the gastric-type carcinomas. The spreading pattern of gastric-type carcinomas showed a middle-layer type more frequently than the intestinal-type carcinomas.. Undifferentiated-type gastric carcinomas frequently expressed an intestinal phenotype. There were differences in the growth patterns between undifferentiated-type gastric carcinomas with a gastric phenotype and those with the intestinal phenotype.

Topics: Adenocarcinoma; Antigens, Neoplasm; Biomarkers, Tumor; Cell Differentiation; Concanavalin A; Female; Gastric Mucins; Humans; Immunoenzyme Techniques; Male; Middle Aged; Mucin-2; Mucins; Neprilysin; Phenotype; Stomach Neoplasms

Expression of decay-accelerating factor (DAF, CD55), a complement-regulatory glycoprotein, is enhanced in colorectal-cancer (CC) cells and colonic epithelium in ulcerative colitis (UC), and stools from these patients contain increased amounts of DAF. Carbohydrate chains of glycoproteins are often altered during malignant transformation or inflammation. In this study, we investigated whether DAF molecules in patients with CC and those with UC differ with respect to oligosaccharide side chains. We analyzed DAF in stools and homogenates of colonic-tissue specimens obtained from patients with CC or UC using solid-phase enzyme-linked assay and Western blotting for reactivity with the lectins Ulex europaeus agglutinin I (UEA-I), wheat-germ agglutinin, peanut agglutinin, and concanavalin A. UEA-I bound to DAF in stools from patients with UC but not in that from the stools of CC patients, as demonstrated on the solid-phase enzyme-linked assay (P <.05, Mann-Whitney U test) and Western blotting. Binding of UEA-I was specifically inhibited by the addition of fucose. The difference in UEA-I reactivity with DAF was observed also in colonic-tissue homogenates from patients with UC and those with CC. DAF expressed in the mucosa and excreted into the stools of UC patients is different from that expressed in CC with regard to UEA-I reactivity. Future studies should be directed toward determining whether a qualitatively unique isoform of DAF is present, of which sugar chains are specific to CC in UC patients.

Topics: Adenocarcinoma; Adult; Aged; CD55 Antigens; Colitis, Ulcerative; Colon; Colonic Neoplasms; Colorectal Neoplasms; Concanavalin A; Feces; Female; Humans; Intestinal Mucosa; Kinetics; Lectins; Male; Middle Aged; Neoplasm Staging; Plant Lectins; Rectal Neoplasms

We have shown that the sera of lung cancer patients affect the response of ConA-stimulated normal peripheral blood mononuclear cells by decreasing the expression of IL-2Ralpha and inhibiting the release of IL-1beta and IL-2. A tendency to enhance the release of IL-6 was also observed. We conclude that an imbalance in the Th1/Th2 cytokine response, typical for cancer patients, may at least partly be related to soluble factors circulating in the patients' blood. We discuss a putative role of serum IL-10, IL-1ra, and soluble IL-2Ralpha in the effects observed.

Topics: Adenocarcinoma; Adult; Aged; Carcinoma, Large Cell; Carcinoma, Non-Small-Cell Lung; Carcinoma, Squamous Cell; Concanavalin A; Cytokines; Female; Humans; Interleukin-2 Receptor alpha Subunit; Lung Neoplasms; Male; Middle Aged; Monocytes; Receptors, Interleukin; Receptors, Interleukin-2; Serum

A method to improve the reactivity to specific lectins of N-glycoproteins isolated from human colorectal mucosa and from adenocarcinoma biopsies was developed using a combination of techniques. Total protein extracts were subjected to affinity chromatography, using the immobilised lectin Concanavalin A coupled to Sepharose, by fast performance liquid chromatography (FPLC). N-glycoprotein enriched fractions were resolved by SDS-PAGE, transferred to PVDF membranes and incubated with various lectins. Digoxigenin-conjugated SNA I and MAA lectins were used to detect sialic acid residues. Biotin-conjugated UEA I lectin was used to detect L-fucose residues. By this method, lectin-binding N-glycoproteins were found in a broad relative molecular mass (Mr) range (from 47 to 205 kDa). No tissue-specific N-glycoproteins were observed when human colorectal mucosa and adenocarcinoma samples were compared.

Topics: Adenocarcinoma; Biomarkers, Tumor; Biopsy; Chromatography, Affinity; Chromatography, High Pressure Liquid; Colorectal Neoplasms; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Fucose; Glycoproteins; Humans; Intestinal Mucosa; Lectins; Membranes, Artificial; Molecular Weight; N-Acetylneuraminic Acid; Organ Specificity

Although the major histologic type in small gastric cancers, less than 10 mm in diameter, is differentiated-type adenocarcinoma (D.Ca), the incidence of D.Ca and that of undifferentiated-type adenocarcinoma (UD.Ca) is almost the same in all early gastric cancers. Histologic conversion from D.Ca to UD.Ca has been speculated, however, a detailed examination of this phenomenon has not yet been performed. Three-hundred and 51 early gastric cancers (D.Ca, 150 (42.7%) lesions; UD.Ca, 93 (26.4%) lesions; and mixed differentiated and undifferentiated type (D&UD.Ca), 108 (30.8%) lesions; tumor size less than 10 mm in diameter; 64 lesions, more than 10 mm, 287 lesions) were examined histochemically with paradoxical concanavalin A type III and high-iron diamine-Alcian blue (pH 2.5), and immunohistochemically with antigastric mucin antibody. The associations between tumor size, tumor differentiation and phenotypic expression of mucin were examined. Regardless of the tumor size, mucin phenotypic expression in the mucosal lesions examined was preserved. Of 47 cancers with a gastrointestinal mucin phenotype (GIM type) or a gastric mucin phenotype (GM type) measuring less than 10 mm, 35 (74.5%) consisted of D.Ca and 12 (25.5%) of both D&UD.Ca and UD.Ca, while of 224 GIM or GM type cancers measuring more than 10 mm, 64 (28.6%) consisted of D.Ca and 160 (71.4%) of both D&UD.Ca and UD.Ca. Differences between these two groups were statistically significant (P < 0.001). Of 15 cancers with an intestinal mucin phenotype (IM type) measuring less than 10 mm, 12 (80.0%) consisted of D.Ca and three (20.0%) of both D&UD.Ca and UD.Ca, and of 50 IM type cancers measuring more than 10 mm, 35 (70.0%) consisted of D.Ca and 15 (30.0%) of both D&UD.Ca and UD.Ca. Differences between these two groups were not statistically significant. These findings suggest that small D.Ca showing gastric mucin expression may transform into UD.Ca during the progression of early gastric cancer.

Topics: Adenocarcinoma; Alcian Blue; Concanavalin A; Gastric Mucins; Horseradish Peroxidase; Humans; Immunohistochemistry; Phenotype; Stomach Neoplasms

Natural killer (NK) cells are non-T, non-B cell lymphocytes that lyse a variety of tumor and virus-infected cells. In this study, we demonstrated that phytohemagglutinin (PHA) rendered resistant autologous T cells extremely sensitive to natural-killer(NK)-cell-mediated lysis. The sensitization was very rapid and concentration-dependent (0.01-1 microg/ml); 62% and 95% of autologous T cells were lysed by interleukin-2-activated NK cells 5 min and 18 h respectively after treatment with PHA (1 microg/ml). The maximal decrease in the level of MHC class I molecules observed on T cells was 22%. Induction of susceptibility to NK-mediated lysis was correlated with the expression of activation markers on T cells treated for relatively long intervals (more than 18 h) with high concentrations of PHA (more than 0.1 microg/ml). Sensitization of T cells required RNA and protein synthesis, although DNA synthesis was not essential. We propose that this unique system is suitable for studying the mechanisms involved in recognition and killing of target cells by NK cells.

Topics: Adenocarcinoma; Colonic Neoplasms; Concanavalin A; Cycloheximide; Cytotoxicity, Immunologic; Dactinomycin; DNA Replication; Humans; Interleukin-2; K562 Cells; Killer Cells, Natural; Lymphocyte Activation; Mitomycin; Nucleic Acid Synthesis Inhibitors; Phytohemagglutinins; Protein Biosynthesis; Protein Synthesis Inhibitors; RNA; T-Lymphocyte Subsets; Tumor Cells, Cultured

Endocervical and endometrial tissues were stained with four lectins to determine the difference in staining pattern between non-neoplastic and neoplastic conditions of these tissues.. The lectins used were Ulex europaeus agglutinin (UEA), Dolicho biflorus agglutinin (DBA). Concanavalin A (Con A), and Phaseolus vulgaris agglutinin (PHA). Endocervical tissues included normal endocervical glands, microglandular hyperplasia, minimal deviation adenocarcinoma and endocervical adenocarcinoma, well to poorly differentiated types. Endometrial tissues were collected from normal endometrium, simple glandular hyperplasia, complex hyperplasia, atypical hyperplasia and adenocarcinoma grades 1-3. Non-neoplastic and neoplastic endocervical and endometrial glandular epithelium showed positive reaction for UEA, Con A and PHA. Non-neoplastic glands showed mild to moderate intensity and apical and/polar type of staining pattern for all lectins. Endocervical adenocarcinoma including minimal deviation adenocarcinoma (MDC) and adenocarcinoma well to moderately differentiated type showed diffuse cytoplasmic type of staining pattern for all lectins, but poorly differentiated adenocarcinoma of endocervix showed only a stromal pattern for all lectins. Endometrial hyperplasia and adenocarcinoma grades 1-3 showed positive reaction for all lectins except for DBA. The staining pattern of endometrial hyperplasia was variable, but adenocarcinoma grades 1-3 showed diffuse type.. Intensity and staining patterns of lectins are helpful in distinguishing between endocervical and endometrial non-neoplastic and neoplastic lesions. Intense positive reaction of MDC, especially for Con A and PHA, can differentiate this lesion from normal endocervical glands. The stromal type of staining pattern of poorly differentiated endocervical adenocarcinoma can also have diagnostic significance. Negative reactions of DBA lectin for endometrial adenocarcinoma can be used for differentiating it from endocervical adenocarcinoma.

Topics: Adenocarcinoma; Adult; Aged; Cervix Uteri; Concanavalin A; Diagnosis, Differential; Endometrium; Epithelium; Female; Humans; Hyperplasia; Lectins; Middle Aged; Phytohemagglutinins; Plant Lectins; Staining and Labeling; Uterine Cervical Neoplasms; Uterine Neoplasms

Differences between human prostate carcinoma (PCA, five cases) and benign prostatic hyperplasia (BPH, five cases) in asparagine-linked (Asn) sugar-chain structure of prostatic acid phosphatase (PAP) were investigated using lectin affinity chromatography with concanavalin A (Con A) and wheat germ agglutinin (WGA). PAP activities were significantly decreased in PCA-derived PAP, while no significant differences between the two PAP preparations were observed in the enzymatic properties (Michaelis-Menten value, optimal pH, thermal stability, and inhibition study). In these PAP preparations, all activities were found only in the fractions which bound strongly to the Con A column and were undetectable in the Con A unbound fractions and in the fractions which bound weakly to the Con A column. The relative amounts of PAP which bound strongly to the Con A column but passed through the WGA column, were significantly greater in BPH-derived PAP than in PCA-derived PAP. In contrast, the relative amounts of PAP which bound strongly to the Con A column and bound to the WGA column, were significantly greater in PCA-derived PAP than in BPH-derived PAP. The findings suggest that Asn-linked sugar-chain structures are altered during oncogenesis in human prostate and also suggest that studies of qualitative differences of sugar-chain structures of PAP might lead to a useful diagnostic tool for PCA.

Topics: Acid Phosphatase; Adenocarcinoma; Aged; Chromatography, Affinity; Concanavalin A; Humans; Male; Middle Aged; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms; Wheat Germ Agglutinins

We investigated the expression of differential lambda light chains in human B cell lines secreting immunoglobulin (Ig). When these cell lines were cultured with concanavalin A for a long period of time, a subpopulation of some but not all of these cell lines was induced to express new lambda light chains replacing the original lambda chain (light chain shifting). Production of the new lambda chain, which replaces the original lambda chain, results from a VJ rearrangement at a previously excluded allele and a dramatic reduction of the original lambda chain transcript, although no difference was found in the level of heavy chain transcript. Recombination activating genes RAG-1 and RAG-2, which are normally expressed during specific early stages of lymphocyte development, were expressed in not only the light chain shifting-inducible lines but also in the non-inducible cells. Treatment of these Ig secreting cell lines with dibutyryl cAMP, which is known to enhance expression of the RAG genes, could not induce the creation of new lambda light chain-producing cells from the inducible lines, suggesting that the expression of the two RAG genes is not sufficient for inducing new lambda light chain production. Concanavalin A induced a gradual but significant production lost of the original lambda chain in a subpopulation of the light chain shifting-inducible cells but not in the non-inducible cells. Association of new lambda light chain production with loss of original lambda chain raises the possibility that, when the RAG genes are expressed, concanavalin A may act on a novel intracellular mechanism controlling lambda light chain allelic exclusion in these plasma cell lines.

Topics: Adenocarcinoma; Alleles; B-Lymphocytes; Base Sequence; Burkitt Lymphoma; Cell Line; Concanavalin A; DNA Primers; DNA-Binding Proteins; Flow Cytometry; Gene Rearrangement; Genes, Immunoglobulin; Homeodomain Proteins; Humans; Hybridomas; Immunoglobulin lambda-Chains; Lung Neoplasms; Molecular Sequence Data; Nuclear Proteins; Polymerase Chain Reaction; Protein Biosynthesis; Transcription, Genetic

An in vitro cytotoxic screening of extracts of Rhaphidophora korthalsii indicated cytotoxicity in the ether fraction. ED50 values of the extract against P388, Molt 4, KB and SW 620 were 12, 14, 8 and 13 micrograms/ml, respectively. The extract was relatively more toxic on P388 and Molt 4 cell lines at concentrations of 50 micrograms/ml and 100 micrograms/ml. Screening with mouse splenocytes showed that the hot water extract had splenocytes stimulating activity.

Topics: Adenocarcinoma; Adjuvants, Immunologic; Animals; Antineoplastic Agents, Phytogenic; Carcinoma, Squamous Cell; Cell Division; Colonic Neoplasms; Coloring Agents; Concanavalin A; Dose-Response Relationship, Drug; Female; Humans; Leukemia; Leukemia P388; Lymphocyte Activation; Mice; Mice, Inbred BALB C; Nasopharyngeal Neoplasms; Plant Extracts; Plant Lectins; Plants, Medicinal; Spleen; Tetrazolium Salts; Thiazoles; Tumor Cells, Cultured; Water

The authors report two cases of adenocarcinoma arising from Brünner's glands. The diagnosis was made on histological, histochemical and lectin-histochemical grounds. Brünner's glands carcinoma cells were alike and located very close to normal Brünner's glands. Brünner's glands carcinoma cells contained neutral glycoproteins and were positive for Concanavalin A.

Topics: Adenocarcinoma; Aged; Brunner Glands; Concanavalin A; Duodenal Neoplasms; Glycoproteins; Histocytochemistry; Humans; Male

The characteristics, including metastatic potential, of 5 xenografts of alpha-fetoprotein (AFP)-producing gastric carcinomas in nude mice, designated TSG1, TSG3, TSG11, TSG17 and TSG20, were examined. Of these xenografts, TSG1, TSG11 and TSG20 were regarded as hepatoid adenocarcinomas based on their morphological resemblance to hepatocellular carcinoma, frequent immunoreactivity for liver-cell markers, and excessive production of AFP with a high concanavalin A (Con-A)-binding property of hepatic type. On the other hand, TSG3 and TSG17 tumors showed the features of poorly differentiated medullary adenocarcinoma with scattered AFP-positive cells consistent with low AFP levels in mouse sera, and negative immunoreactivity for other liver-cell markers. Ultrastructurally, these tumors were composed of undifferentiated cells with a little adenocarcinomatous differentiation. Moreover, the AFP produced by TSG3 and TSG17 tumors had an extremely high Con-A nonbound fraction (80% to 90%), which was different from that of the hepatic or yolk-sac types. Therefore, both TSG3 and TSG17 tumors were regarded as non-hepatoid, poorly differentiated adenocarcinomas which could be differentiated from any types of AFP-producing gastric carcinoma. Furthermore, cells from hepatoid adenocarcinoma strains (TSG1, TSG11 and TSG20) injected into the spleens of nude mice produced liver metastases in all the mice examined, whereas cells from non-hepatoid carcinoma strains (TSG3 and TSG17) produced few or no liver metastases. Our data show that some non-hepatoid AFP-producing gastric carcinomas have lower liver-metastasizing potential than hepatoid AFP-producing gastric carcinomas.

Topics: Adenocarcinoma; alpha-Fetoproteins; Animals; Concanavalin A; Humans; Immunohistochemistry; Liver Neoplasms, Experimental; Male; Mice; Mice, Inbred BALB C; Mice, Nude; Microscopy, Electron; Neoplasm Transplantation; Stomach Neoplasms; Transplantation, Heterologous

The case is presented of a 46 year old woman who had a gastric tumor with components of choriocarcinoma, hepatoid adenocarcinoma and common types of adenocarcinoma. Although two histologic types of tumor producing carcinoplacental or carcinofetal proteins were contained within the tumor, immunohistochemical analyses, especially of placental alkaline phosphatase, clearly showed that each component was present separately within the same tumor. It was only hepatoid adenocarcinoma cells that permeated the lymph and blood vessels. After the recurrence, the serum level of alpha-fetoprotein (AFP) markedly elevated, but that of human chorionic gonadotropic beta-subunit (hCG-beta) was always within normal range. These findings indicate that in the present case the hepatoid adenocarcinoma component was more aggressive in growth than the choriocarcinoma component.

Topics: Adenocarcinoma; alpha-Fetoproteins; Choriocarcinoma; Concanavalin A; Female; Humans; Immunoenzyme Techniques; Middle Aged; Neoplasms, Multiple Primary; Stomach Neoplasms

Topics: Adenocarcinoma; Biomarkers, Tumor; Concanavalin A; Humans; Immunoelectrophoresis; Orosomucoid; Stomach Neoplasms

A molecular form of CEA non-binding Con A (CEAnC) was isolated from colon adenocarcinoma metastases in liver as a fraction of CEA having no affinity to Con-A-Sepharose. CEAnC was shown to be immunochemically identical to CEA, but to differ substantially with regard to the amino acid and sugar composition, and structure of the sugar moiety, possibly containing non only N-, but also O-glycosyl carbohydrate chains. The antigens studied were also found to possess different spatial structures. The differences between CEA and CEAnC suggest CEAnC to be a new molecular form of CEA.

Topics: Adenocarcinoma; Amino Acids; Carbohydrate Sequence; Carcinoembryonic Antigen; Chromatography, Gel; Chromatography, Ion Exchange; Circular Dichroism; Colonic Neoplasms; Concanavalin A; Humans; Immunochemistry; Immunodiffusion; Liver Neoplasms; Molecular Sequence Data

Phenotypic expression of tumor cells was investigated in 33 early gastric carcinomas by mucin histochemistry using paradoxical concanavalin A staining. This staining method had been developed to differentiate 3 classes of mucins located at various sites of the alimentary tract. Twenty-five (76%) tumors contained mixtures of neutral or acid class II mucin and class III mucin, suggesting the origin of multipotential stem cells. The surface mucous cell expression was more dominant than the pyloric gland or intestinal phenotypes in the well-and poorly differentiated adenocarcinomas. The intestinal properties of the tumor cells were noted not only in the well-differentiated but also in the poorly differentiated or signet ring cell carcinomas, not closely being related to the presence of background intestinal metaplasia. Signet ring cell carcinomas revealed a distinct pattern of mucin histochemistry compared with the other types.

Topics: Adenocarcinoma; Adenocarcinoma, Mucinous; Cell Differentiation; Concanavalin A; Histocytochemistry; Humans; Intestines; Metaplasia; Mucins; Staining and Labeling; Stem Cells; Stomach Neoplasms

Glycoproteins from normal and malignant human cervix were studied using an organ culture system and compared by gel electrophoresis and autoradiography. Five glycoproteins of 178 kDa, 95 kDa, 93 kDa, 82 kDa and 38 kDa and 1 glycolipid (46 kDa) were detected more frequently in squamous carcinomas. Certain glycoproteins were shown to be oncofoetal and some had affinity for Concanavalin A (Con A). The 82 kDa glycoprotein was present in 16/17 squamous carcinomas but in only 1/13 normal cervices. This band represented a glycoprotein containing glucosamine, mannose, small quantities of methionine and no fucose. These preliminary results suggest that these glycoproteins and in particular the 82-kDa glycoprotein are worthy of further investigation and characterisation.

Topics: Adenocarcinoma; Adult; Aged; Biopsy; Blotting, Western; Carcinoma, Squamous Cell; Chromatography; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Female; Glycoproteins; Humans; Lectins; Middle Aged; Tumor Cells, Cultured; Uterine Cervical Neoplasms

A case of adenocarcinoma of the cervical oesophagus was examined by employing a battery of histochemical techniques and was demonstrated to arise from ectopic gastric mucosa. The patient was a 66-year-old Japanese male. Endoscopy revealed an ulcerated tumour on the right anterior wall of the cervical oesophagus, approximately 16 cm from the incisor teeth. Pathological examination of surgically removed specimens showed well-differentiated tubular adenocarcinoma. Ectopic gastric mucosa was found in the oesophageal mucosa adjoining the carcinoma. Histochemical stains for characterizing mucosubstances and immunostains for various antigens were used. In addition to this carcinoma, ectopic gastric mucosa in the oesophagus and normal oesophageal, cardiac, tracheal and bronchial mucosa were also examined. The results showed that the carcinoma contained mucins, which showed reactivities characteristic of the gastric surface mucous cell (galactose oxidase-cold thionin Schiff reactive) and gland mucous cell (paradoxical concanavalin A staining reactive). Ectopic gastric mucosa consistently contained these mucins, but other tissue sites lacked them.

Topics: Adenocarcinoma; Aged; Antigens; Choristoma; Concanavalin A; Esophageal Neoplasms; Gastric Mucosa; Humans; Male; Mucins

[14C]Glucosamine metabolic labeling and concanavalin A blots were used to identify four major glycoprotein species associated with ascites tumor cell microvillar microfilament cores and with a transmembrane complex containing actin. Phalloidin shift analysis of glucosamine-labeled microvilli showed that glycoproteins of 110-120, 80, 65, and 55 kDa are stably associated with the microfilament cores. Analysis of large (greater than 10(6) kDa) transmembrane complexes from microvillar membranes made under microfilament-depolymerizing conditions (Carraway, C. A. C., Jung, G., and Carraway, K. L. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 430-434) revealed glycoproteins of the same Mr values, showing the same relative staining or labeling patterns as those observed with the microfilament cores. Gel filtration of high salt, high pH extracts of intact microvilli, microfilament cores, or transmembrane complexes showed that in all of these fractions the glycoproteins are associated in a very large, stable complex. The glycoprotein multimer was isolated essentially free of actin and other components by Sephacryl S-1000 chromatography of microvilli, microvillar membranes prepared at pH 11, microfilament cores, or transmembrane complex fractions in Triton X-100, 1 M KCl, glycine, pH 9.5. Purified glycoprotein complex bound actin when incubated under polymerizing conditions. The presence of the glycoprotein heteromultimer in both microfilament cores and transmembrane complex from isolated membranes and the association of the purified glycoprotein complex with actin are consistent with our hypothesis that the glycoprotein-containing transmembrane complex is an association site for microfilaments at the plasma membrane.

Topics: Actins; Adenocarcinoma; Animals; Ascites; Blotting, Western; Chromatography, Gel; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Glucosamine; Membrane Glycoproteins; Microfilament Proteins; Microvilli; Phalloidine; Rats; Tumor Cells, Cultured

Biochemical and immunohistochemical analyses were done on five cases of gastric carcinoma with excessive production of alpha-fetoprotein (AFP). Histologic and ultrastructural examination of these cases showed conventional poorly differentiated adenocarcinoma of cuboidal or polygonal tumor cells in the medullary area with scattered AFP-positive cancer cells. Comparative studies on serum AFP between these cases and in hepatocellular carcinoma (HCC) or in testicular yolk sac tumor cases using concanavalin A (ConA)-affinity and lens culinalis agglutinin A (LCA)-affinity sepharose columns revealed that the AFP derived from four cases had a high ConA nonadsorping rate and high LCA-reactive fraction similar to that of yolk sac tumor. The AFP from one case had a small LCA-reactive fraction similar to that of HCC. Further immunohistochemical study using several markers for liver cells or germ cell tumor did not show additional evidence of these tumor cells to differentiate into liver cells or yolk sac tumor cells. Thus, this study indicates that AFP-producing gastric carcinomas are not always derived from hepatoid differentiation of the foregut. These gastric carcinomas might be categorized into medullary tumor with gastrointestinal tract-specific AFP.

Topics: Adenocarcinoma; Aged; alpha-Fetoproteins; Biomarkers, Tumor; Carcinoma; Chromatography, Affinity; Chromatography, Agarose; Concanavalin A; Cytoplasm; Female; Humans; Immunoenzyme Techniques; Lectins; Male; Microscopy, Electron; Middle Aged; Stomach Neoplasms

Helix pomatia agglutinin (HPA)- and Concanavalin A (Con A)-binding carbohydrate expression were studied on 32 tumour samples from primary adenocarcinoma of the breast and 12 samples from lymph node metastases. Live cells were spilled from each of the fresh samples and the extent of fluorescent-labelled HPA and Con A-binding was assessed by flow cytometry. The extent of brightness was expressed in a defined quantitative fashion and the percentage of positive cells was accurately determined from a sample of 10,000 cells per tumour. Correlation of binding with clinicopathological features showed that HPA but not Con A related to lymph node involvement (P = 0.001) in tumours of higher grade (II and III). Spilled tumour cells (non-lymphocytes) were selected from the lymph nodes and the presence of HPA binding cells in the involved lymph nodes was found to relate to positive HPA binding in autologous primary tumours (P = 0.002). Dual-label analysis of HPA and Con A binding showed characteristic features for each tumour. The study demonstrates the use of flow cytometry as a simple and effective technique in detecting differences in lectin binding in live spilled cells from fresh breast cancer tissues. This method may prove to be particularly useful if performed preoperatively on cells in fine-needle aspirates.

Topics: Adenocarcinoma; Adult; Breast Neoplasms; Carbohydrate Metabolism; Carcinoma, Intraductal, Noninfiltrating; Cell Membrane; Concanavalin A; Female; Flow Cytometry; Fluorescence; Humans; Lectins; Lymph Nodes; Middle Aged

Cloned muscarinic acetylcholine m1 and m2 receptors were expressed in stably transfected mouse Y1 adrenal cells and in a variant Y1 line, Kin-8, which is deficient in cAMP-dependent protein kinase activity (PKA-). m1 and m2 receptors were rapidly internalized following exposure of transfected PKA+ or PKA- cells to the muscarinic agonist carbachol. Thus, agonist-dependent internalization of m1 and m2 did not require PKA activity. A differential effect of PKA on regulation by agonist of the m2 receptor, but not the m1 receptor, was unmasked in PKA- cells. The m2 receptor was more sensitive to agonist-dependent internalization, and its rate of internalization was faster in PKA- cells than it was in PKA+ cells. Treatment of PKA+ cells with 8-(4-chlorophenylthio)-cAMP or forskolin did not result in internalization of either m1 or m2 receptors and did not alter the extent of agonist-dependent internalization of m2. These data indicate that the basal activity of PKA may modulate the agonist-dependent internalization of the m2 receptor, but not the m1 receptor. The internalization of the m1 and m2 receptors in both PKA+ and PKA- cells was accompanied by desensitization of functional responses. Exposure of PKA+ cells to 10(-7) M phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C, resulted in a 30 +/- 9% decrease in the number of m1 receptors on the cell surface. However, treatment of PKA- cells expressing the m1 receptor did not result in internalization, suggesting that PKA was required for some aspect of PMA-dependent internalization.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Adenocarcinoma; Adrenal Gland Neoplasms; Animals; Colforsin; Concanavalin A; Cyclic AMP; Endocytosis; Mice; N-Methylscopolamine; Phorbol Esters; Pilocarpine; Protein Kinases; Quinuclidinyl Benzilate; Receptors, Muscarinic; Recombinant Fusion Proteins; Scopolamine Derivatives; Second Messenger Systems; Thionucleotides; Tumor Cells, Cultured

Human ovarian clear cell carcinoma cell line (transferrin (Tf)-non-producer), HAC 2, cells were adapted to grow in chemically defined synthetic medium when the cells were cultured with medium containing 10 micrograms/ml of insulin at least for 6 months. They synthesized and secreted constantly the 80 kDa protein immunologically similar to human serum Tf (15 +/- 12 ng/ml/10(7) cells/3 days). By sensitive lectin-affinity electrophoresis followed by antibody-affinity blotting technique, a concanavalin A weakly bound or unbound, lentil lectin, a strongly reactive abnormal band, which was rarely found in human serum Tf, was detectable in the Tf synthesized by HAC 2 cells (HACTf). These findings suggest that the HACTf may act as one of the autocrine growth factors and that this heterogeneity of HACTf for lectin affinity is ascribed to differences in the carbohydrate moiety of the Tf.

Topics: Adenocarcinoma; Chromatography, Affinity; Concanavalin A; Female; Humans; Immunoelectrophoresis; Lectins; Molecular Weight; Neoplasm Proteins; Ovarian Neoplasms; Plant Lectins; Precipitin Tests; Transferrin; Tumor Cells, Cultured

118 surgical specimens were obtained from patients with lung cancer treated in our hospital during the period of 1977-1983 and tested with carcinoembryonic antigen (CEA), ABO (H) isoantigen and Concanavalin A (ConA). The results showed that the CEA assessment, which give no prognostic significance for long-term survival (P greater than 0.05), would be useful in predicting short-term (6 month) out come (P less than 0.05). All patients with positive ABO (H) test for squamous cell lung carcinoma survived at the end of five years. As for ConA, no definite link has been found with the prognosis.

Topics: ABO Blood-Group System; Adenocarcinoma; Carcinoembryonic Antigen; Carcinoma, Squamous Cell; Concanavalin A; Humans; Isoantigens; Lung Neoplasms; Prognosis

The freshly separated indicator cells (suspension of leukocytes) used in humoral leukocyte adherence inhibition test were labeled either with 14C-amino acid mixture or 3H-concanavalin A (3H-ConA). Instead of counting the adherent cells, the amount of 'adherent' radioactivity was measured by a liquid scintillation spectrometer. By the modified method, sera from 25 lung-carcinoma-bearing patients as well as serum samples from 21 healthy persons were examined in the presence of crude antigens prepared from 'normal' lung tissue or lung tumors of various histologic types. Although the results demonstrated high specificity and reproducibility of both methods, the binding of 3H-ConA to the surface of adherent cells is more expressed and assures higher levels of radioactivity.

Topics: Adenocarcinoma; Adult; Aged; Amino Acids; Carcinoma; Carcinoma, Small Cell; Carcinoma, Squamous Cell; Concanavalin A; Female; Humans; Immunologic Techniques; Indicators and Reagents; Leukocyte Adherence Inhibition Test; Lung Neoplasms; Male; Middle Aged

We studied mucin histochemistry in 25 rectosigmoid adenocarcinomas and in the transitional mucosa adjacent to these tumors using standard techniques for the detection of neutral and acid sialomucins and sulfomucins and the paradoxical concanavalin A (Con A) stain. This histochemical procedure selectively detects residues of mannose in glycoproteins exposed to brief steps of oxidation and reduction. Those techniques were also used to study histologically normal mucosa of specimens with carcinoma, normal rectosigmoid mucosa of patients without inflammatory or neoplastic bowel disease, hyperplastic rectal polyps, and rectosigmoid mucosa of human fetuses. Normal mucosa and hyperplastic polyps mainly contained sulfomucins and did not display Con A binding activity with any of the variants of the stain. In contrast, fetal, transitional, and malignant mucosa predominantly showed sialomucins and although not reactive with the standard Con A sequence, displayed binding activity for the lectin after short oxidative-reductive steps. These results provide further evidence that transitional and malignant mucosa produce markedly abnormal mucins whose histochemical patterns represent a re-emergence of the fetal type found during development. The principles of the paradoxic Con A reaction may be applied to unmask lectin binding activity in apparently unreactive sites.

Topics: Adenocarcinoma; Aged; Binding Sites; Concanavalin A; Female; Fetus; Humans; Male; Middle Aged; Mucous Membrane; Pregnancy; Rectal Neoplasms; Rectum; Sigmoid Neoplasms

An alpha-fetoprotein (AFP)-producing human gallbladder carcinoma showing direct invasion into the liver was transplanted into BALB/c-nu/nu nude mice. Although patient serum levels of AFP and carcinoembryonic antigen (CEA) were within normal limits, they were elevated to 1,040 ng/ml and 22.1 ng/ml, respectively, after cholecystectomy. Prominent liver metastasis was demonstrated by diagnostic imaging techniques shortly after the operation. Pathologically, the resected tumor consisted of papillotubular adenocarcinoma and the part which had invaded the liver showed a solid growth pattern with no papillo-tubular structure. The transplanted tumor showed both papillo-tubular and solid growth patterns, in which positive reactions for AFP, CEA, ferritin (FER), carbohydrate antigen 19-9 (CA 19-9), albumin (ALB) and fibrinogen (FIB) were confirmed by the avidin-biotin-peroxidase complex method. Serum levels of AFP, CEA, CA 19-9, beta 2-microglobulin (BMG) and FER were elevated in the nude mice bearing tumor transplants. Twenty-five percent of the serum AFP from nude mice with tumor transplants bound with concanavalin A (Con A), suggesting that the tumor was of gastrointestinal rather than hepatic origin.

Topics: Adenocarcinoma; Adult; alpha-Fetoproteins; Animals; Biomarkers, Tumor; Carcinoembryonic Antigen; Concanavalin A; Female; Gallbladder Neoplasms; Humans; Immunohistochemistry; Mice; Mice, Nude; Neoplasm Transplantation; Transplantation, Heterologous

A 67-year-old man presented with a pulmonary atypical carcinoid tumor with marked elevation of the serum alpha-fetoprotein (AFP) level to 181,000 ng/ml and no hepatic metastases. Immunohistochemistry revealed AFP-positive fine granules, sparsely distributed in some cells. The proportion of the concanavalin A nonbinding subfraction was 33.7%. Light microscopy revealed hyaline globules within or outside the clear and reticular cytoplasm of a few cells. These were ultrastructurally electron-dense materials similar to the hyaline bodies observed in yolk sac tumors. The Grimelius silver method stained only a few cells and very few cells showed a positive Masson-Fontana reaction. Electron microscopy revealed secretory granules measuring 220 nm on the average in scattered cells. Immunohistochemical studies showed 5-hydroxytryptophan in many cells and 5-hydroxytriptamine or serotonin in only a few cells. As for polypeptide hormones, gastrin was detected and in autopsy specimens carcinoembryonic antigen (CEA) immunoreactive cells were observed. Past case reports on the coexistence of carcinoid tumors and adenocarcinomas in the digestive tract suggest that the tumor cells in our case are also derived from primitive or stem cells of endodermal origin and expressed unusual differentiation in the course of treatment.

Topics: Adenocarcinoma; Aged; alpha-Fetoproteins; Carcinoembryonic Antigen; Carcinoid Tumor; Concanavalin A; Cytoplasmic Granules; Humans; Immunoelectrophoresis, Two-Dimensional; Immunohistochemistry; Lung Neoplasms; Male; Microscopy, Electron

Topics: Adenocarcinoma; Animals; Colonic Neoplasms; Concanavalin A; Cyclic AMP; Heat-Shock Proteins; Humans; Hyperthermia, Induced; Lysine; Membrane Glycoproteins; Neoplasm Proteins; Predictive Value of Tests; Protein Biosynthesis

The effect of surgery on peripheral blood mononuclear cell responsiveness to mitogens and suppressor cell (SC) activity assessed in a concanavalin A (ConA) assay were studied in patients with stage 0 and stage III-IV cancer. Patients were exposed to a similar surgical trauma the same type of anaesthesia, and to no pre- and early postoperative radio- or chemotherapy. A more pronounced postoperative decrease in the lymphocyte count, responsiveness to phytohemagglutinin (PHA) and ConA, and in the SC activity was found in the nonadvanced than advanced cancer group. These findings point to an impaired mobilization and distribution capacity of circulating lymphocytes in patients with advanced neoplastic disease.

Topics: Adenocarcinoma; Adult; Aged; Aged, 80 and over; Carcinoma in Situ; Cells, Cultured; Colonic Neoplasms; Concanavalin A; Female; Humans; Leukocyte Count; Leukocytes, Mononuclear; Lymphatic Metastasis; Lymphocytes; Middle Aged; Neoplasm Metastasis; Phytohemagglutinins; Stomach Neoplasms; T-Lymphocytes, Regulatory; Uterine Neoplasms

Microfilament-associated proteins and membrane-microfilament interactions are being investigated in microvilli isolated from 13,762 rat mammary ascites tumor cells. "Phalloidin shift" analyses on velocity sedimentation gradients of Triton X-100 extracts of [3H]-glucosamine-labeled microvilli identified a 120-kDa cell-surface glycoprotein associated with the microvillar microfilament core. The identification was verified by concanavalin A (Con A) blots of one- and two-dimensional (2D) electrophoresis gels of sedimented microfilament cores. By 2D-electrophoresis and lectin analyses the 120-kDa protein appeared to be a fraction of ASGP-2, the major Con A-binding glycoprotein of the sialomucin complex of the 13,762 cells. This identity was confirmed by immunoblot analyses using immunoblot-purified anti-ASGP-2 from anti-membrane serum prepared against microvillar membranes. Proteolysis of the microvilli with subtilisin or trypsin resulted in an increase in the amount of ASGP-2 associated with the microfilament cores. An increase was also observed with sialidase treatment of the microvilli, suggesting that negative charges, probably present on the highly sialated sialomucin ASGP-1 of the ASGP-1/ASGP-2 sialomucin complex, reduce ASGP-2 association with the microfilament core. Proteolysis of isolated microvillar membranes, which contain actin but not microfilaments, also increased the association of ASGP-2 with a Triton-insoluble, actin-containing membrane fraction. Purified ASGP-2 does not bind to microfilaments in sedimentation assays. Since the Triton-insoluble membrane residue is enriched in an actin-containing transmembrane complex, which contains a different glycoprotein, we suggest that the ASGP-2 is binding indirectly via this complex to the microfilament core in the intact microvilli.

Topics: Actin Cytoskeleton; Adenocarcinoma; Animals; Centrifugation, Density Gradient; Concanavalin A; Cytoskeleton; Electrophoresis, Polyacrylamide Gel; Immunoblotting; Isoelectric Focusing; Mammary Neoplasms, Experimental; Microvilli; Mucin-4; Phalloidine; Rats; Sialoglycoproteins; Subtilisins; Tumor Cells, Cultured

The expression of six lectins (Arachis hypogaea, B. simplicifolia I, concanavalin A, Dolichus biflorus, Triticum vulgaris, Lotus tetragonolobus) was studied in 24 adenocarcinomas, 24 adenomas, 20 metaplastic polyps, 17 specimens of mucosal prolapse (solitary ulcer syndrome) and 10 of normal mucosa, all taken from the rectum. Qualitative, quantitative and distributive differences in lectin expression were observed between adenocarcinoma and normal mucosa. These cancer-associated glycoprotein alterations were also observed, though to a lesser extent, in benign neoplastic and non-neoplastic lesions of the rectum. It appears therefore that the glycoprotein modifications associated with malignant transformation are not specific indicators of malignancy. It is suggested that the common denominator is a disturbance in the activities of enzymes, particularly the glycosyl-transferases and glycosidases, involved in the biosynthesis of glycoprotein. This disturbance can occur in situations where cells are less differentiated either through developmental immaturity, rapid cellular division or neoplastic de-differentiation. These changes are therefore more likely to reflect the state of differentiation rather than the malignant nature of the cells. It is shown that the greater the deviation of the lesion from normal the greater the glycoprotein alterations. The potential usefulness of lectin expressions as predictive indicators of biological behaviour of adenocarcinomas of the large bowel needs further studies.

Topics: Adenocarcinoma; Adenoma; Arachis; Concanavalin A; Histocytochemistry; Humans; Intestinal Mucosa; Lectins; Plant Lectins; Polyps; Rectal Neoplasms; Rectum; Triticum

The binding of different lectins (concanavalin A [Con A], triticum vulgaris [WGA], glycine maximum [SBA], dolichos bilflorus [DBA], ulex europaeus [UEA I], arachis hypogaea [PNA], and ricinus communis [RCA I]) to cells of normal prostate glands, hyperplastic glands and adenocarcinoma was studied. The Con A, WGA, DBA, PNA and RCA I bound to both normal and hyperplastic glands. The binding in the malignant glands differed from that of the benign conditions. The SBA, which was not bound by benign cells, was bound to the malignant glandular cells. Also, UEA I was bound to a part of the carcinoma cells. In addition, the binding pattern of Con A and WGA in the cells differed between the malignant and benign conditions. Based on the results of this study, it is suggested that lectin histochemical study might be useful in routine pathologic examination to detect malignant cells in cases which are doubtful with regard to malignancy by routine methods.

Topics: Adenocarcinoma; Biomarkers, Tumor; Concanavalin A; Fluorescein-5-isothiocyanate; Fluoresceins; Histocytochemistry; Humans; Lectins; Male; Peanut Agglutinin; Plant Lectins; Prostatic Hyperplasia; Prostatic Neoplasms; Soybean Proteins; Thiocyanates; Wheat Germ Agglutinins

Topics: 1,2-Dimethylhydrazine; Adenocarcinoma; Animals; Colonic Neoplasms; Concanavalin A; Dimethylhydrazines; Female; Glycoproteins; Lectins; Mice; Mice, Inbred ICR

Serum concentrations of serum amyloid A protein (SAA), peripheral blood lymphocytes (PBL) mitogenic response to phytohemagglutinin (PHA) and Concanavalin A (Con A), numbers of circulating T- and B-lymphocytes and length of survival after diagnosis were measured in 50 patients with cancer of the lung. SAA levels were significantly elevated when compared to 50 control subjects (P less than 0.001), but did not correlate with state of tumor spread at the time of diagnosis. Mitogenic responses of PBL from the cancer patients to PHA and Con A were significantly depressed (P less than 0.001), but also did not predict state of metastatic spread. The percentage of circulating T-lymphocytes was also significantly depressed in cancer patients when compared to controls. In six patients who survived tumor-free for greater than 2.5 years, SAA serum concentrations returned to normal. Statistical analysis showed a significant correlation between SAA serum concentrations and PBL mitogenic response to Con A. In addition, both high SAA concentrations and depressed PBL responses to Con A correlated with shortened survival. Therefore, these parameters may be of value in evaluating prognosis in patients with lung cancer. In addition, serial monitoring of SAA concentrations may be of value in evaluating recurrence or cure of lung cancer.

Topics: Adenocarcinoma; Adult; Aged; Amyloid; Carcinoma; Carcinoma, Small Cell; Carcinoma, Squamous Cell; Cells, Cultured; Concanavalin A; Humans; Leukocyte Count; Lung Neoplasms; Lymphocytes; Male; Middle Aged; Phytohemagglutinins; Prognosis; Prospective Studies; Serum Amyloid A Protein

The tissue responds in culture differently to each of the tested hormones. Insulin, but not prolactin or hydrocortisone, was mitogenic to the culture, but did not alter the overall transcriptional activity pattern displayed by the insulin-free cultures. Prolactin stimulated transcriptional activity above control levels between days 2 and 6 of culture, but hydrocortisone was inhibitory to both DNA-synthetic and transcriptional activity of the culture. Upon initial 24-hr treatment with 50 micrograms/ml monovalent concanavalin A, the tissue altered its hormonal sensitivity in the examined activities, but the presence of any one of the hormones in the culture medium abolished the individual effect of concanavalin A. With hydrocortisone, however, the individual effects of the lectin and the hormone interacted in cultures treated with both compounds, suggesting a type of intracellular communication with the membrane, operative in this mammary cell line, that may involve channels of biochemical changes energized by a hydrocortisone stimulus.

Topics: Adenocarcinoma; Animals; Concanavalin A; Culture Techniques; DNA, Neoplasm; Hormones; Hydrocortisone; Insulin; Male; Mammary Neoplasms, Experimental; Mice; Mice, Inbred BALB C; Neoplasm Transplantation; Prolactin; RNA, Messenger; Transcription, Genetic

Formalin-fixed, paraffin-embedded tissue sections of normal skin, sebaceous hyperplasia, nevus sebaceus, sebaceous adenoma, and sebaceous carcinoma were studied by means of biotinylated and FITC conjugated concanavalin A (Con A) and Lens culinaris agglutinin (LCA). At relatively high concentrations of these lectins, all cutaneous epithelial cells were stained. As the concentration of LCA was lowered, there was a corresponding decrease in the intensity of staining of all epithelial cells. With lowered concentrations of Con A, staining of sebaceous epithelium remained strongly positive, while staining of other epithelia decreased in a manner similar to that seen for LCA. These staining patterns were seen in normal and neoplastic tissues. Both Con A and LCA are known to bind to alpha-D-mannopyranosyl and alpha-D-glucopyranosyl residues of glycoproteins and glycolipids. The difference in staining of sebaceous epithelial cells by Con A and LCA suggests that the binding of these lectins is not determined strictly by the presence of alpha-D-mannopyranosyl or alpha-D-glucopyranosyl residues, but is modified by side-chain substitution on the monosaccharides and/or by the oligosaccharide which contains the particular monosaccharide. Whichever event is operative, a saccharide moiety is present on the surface of mature sebaceous cells which has a strong affinity for Con A.

Topics: Adenocarcinoma; Adenoma; Concanavalin A; Epithelium; Histocytochemistry; Humans; Hyperplasia; Lectins; Nevus; Plant Lectins; Sebaceous Gland Neoplasms; Sebaceous Glands

To evaluate the efficacies of various administration routes of the streptococcal preparation, OK-432, we studied the lymphocyte proliferation responses to lectins in patients with malignancies. OK-432 was administered intravenously (I.V.), intramuscularly (I. M.) or intradermally (I.D.) for 2 weeks. Lymphocyte proliferation responses to concanavalin A, PHA and SuM (crude extract of OK-432) were studied before and after OK-432 administration. Enhanced responses were observed in 7 out of 9 patients (77.8%) in the I.V. group compared with 3 out of 7 (44.2%) in the I.M. group and 4 out of 9 (44.4%) in the I.D. group. Ratios of stimulation index (S.I.) after administration over S.I. before administration were highest in the I.V. group. These results suggest that I.V. administration of OK-432 is most effective for stimulating host immune systems.

Topics: Adenocarcinoma; Adult; Aged; Biological Products; Carcinoma, Squamous Cell; Concanavalin A; Female; Humans; Infusions, Parenteral; Lung Neoplasms; Lymphocyte Activation; Male; Middle Aged; Phytohemagglutinins; Picibanil

A patient with primary gastric adenocarcinoma with extremely high serum alpha-fetoprotein (AFP) levels (12,000 ng/ml) is described. Histologically, foci strongly resembling hepatocellular carcinoma with hyaline globules were noted. Within tumor cells, AFP was identified with both light and electron microscopy, showing the production of AFP by tumor cells themselves. Furthermore, 88% of serum AFP combined with Concanavalin A (ConA), revealing that it was hepatic-type AFP and not germ-cell-type. Localization of alpha-1-antitrypsin within tumor cells was also noted. Ultrastructural study showed that there were two types of structures corresponding to periodic acid-Schiff (PAS)-positive globules, one of which, the proteinaceous material in intracytoplasmic lumina, was found to contain AFP. Among gastric adenocarcinomas with a high serum AFP level (several thousand or more ng/ml of AFP), foci resembling hepatocellular carcinomas have been reported by several investigators. Those gastric carcinomas, together with the current case, may constitute a clinicopathologic entity, hepatoid adenocarcinoma of the stomach.

Topics: Adenocarcinoma; alpha-Fetoproteins; Cell Differentiation; Concanavalin A; Humans; Immunoenzyme Techniques; Male; Microscopy, Electron; Middle Aged; Stomach Neoplasms

Insulin induced in organ culture of a mouse mammary adenocarcinoma the expression of two cytoplasmic proteins of molecular size 72 and 49 kD. In freshly excised tumor both proteins are present in relatively large amounts, but their concentration became greatly diminished during culture in insulin-free media, indicating sensitivity to post-transcriptional modification which was activated in vitro in the absence of insulin. In insulin cultures the two proteins reappeared after two culture days, their concentration becoming increased thereafter with time of culture, but their expression could not be correlated with the biphasic pattern of transcriptional activity fluctuation recorded during culture similarly to insulin-free cultures. Insulin on the other hand stimulated two waves of doubling of DNA synthesis during 6 culture days. The results demonstrate insulin responsiveness in culture of a proliferative fraction of the tumorous cell population in this adenocarcinoma line in the synthesis of two sensitive proliferation-derived cytoplasmic proteins. The possible biological significance of these proteins is discussed.

Topics: Adenocarcinoma; Animals; Concanavalin A; Cytoplasm; DNA, Neoplasm; Insulin; Male; Mammary Neoplasms, Experimental; Mice; Mice, Inbred BALB C; Neoplasm Proteins; Organ Culture Techniques; Particle Size; RNA; Time Factors; Transcription, Genetic

The inhibition of the cell surface enzyme 5'-nucleotidase by concanavalin A is being studied as a model for understanding transmembrane modulation of cell surface functions. Nucleotidase of 13762 MAT-C1 ascites rat mammary adenocarcinoma cells is inhibited by concanavalin A in a noncooperative process. When cells are treated with the cytoplasmic effectors cytochalasins, colchicine, energy poisons, calcium plus ionophore or hypotonic buffers, the concanavalin A inhibition of the enzyme becomes cooperative. 5'-Nucleotidase of isolated MAT-C1 microvilli is also inhibited by concanavalin A in a noncooperative process; however, treatment of the microvilli with the same cytoplasmic effectors does not induce cooperativity. Since previous studies in several systems have suggested an association of nucleotidase with actin-containing microfilaments or the cell cytoskeleton, one explanation for the cooperativity changes is that they result from a change in the association of the enzyme with the cytoskeleton. However, Triton X-100 extractability of nucleotidase is the same for MAT-C1 cells exhibiting cooperative or noncooperative concanavalin A inhibition. Moreover, enzyme from cells exhibiting cooperative inhibition can be extracted into the zwitterionic detergent Zwittergent in a cooperative form, while enzyme exhibiting noncooperative behavior can be extracted into Zwittergent in a noncooperative form. Gel filtration and rate-zonal sucrose density gradient centrifugation showed little discernible size or sedimentation difference between enzyme samples exhibiting noncooperative and cooperative inhibition. These results indicate that changes in the cooperativity of the concanavalin A inhibition of nucleotidase are not a result of changes in the association of the enzyme with the cytoskeleton. These studies emphasize the caution which must be exercised in interpreting the effects of cytoskeletal perturbants on cell surface functions.

Topics: 5'-Nucleotidase; Adenocarcinoma; Animals; Cell Membrane; Concanavalin A; Cytoskeleton; Mammary Neoplasms, Experimental; Microvilli; Nucleotidases; Rats

The capacity of inbred W/Fu rats bearing syngeneic colon carcinomas to generate interleukin(s) (IL) was studied during primary tumor growth, after tumor resection, and during postresection immunotherapy. During local tumor growth, there was a significant decrease in the capacity of the host's adherent mononuclear cells to generate IL-1 and of peripheral blood mononuclear cells to generate IL-2 (16.6 and 23%, respectively, when compared to control animals; P less than .01). The presence of regional metastases or large primary tumor burden resulted in a further sharp fall in IL generation (0.9 and 10% for IL-1 and IL-2, respectively, when compared to control animals; P less than .01). With the use of three different doses of tumor inoculum, inhibition of IL generation was shown to occur when tumors were barely palpable. Decrease in IL correlated with tumor growth and not with the initial number of tumor cells injected. Tumor resection resulted in a rise in IL-2 generation from 36 to 64% of control animals' levels. Postresection immunotherapy with the use of an active specific immunization protocol successfully modulated IL-2 production to normal in animals protected from tumor recurrence. Animals that developed recurrent tumors despite immunization exhibited a continued inability to generate IL (mean values of IL-2 production compared to controls: 184% in animals free of recurrence after immunotherapy, 1% in animals developing recurrent tumors after immunotherapy; P less than .01). These results suggested that alterations in IL generation may lead to immune unresponsiveness during tumor growth. Active specific immunotherapy protecting animals from recurrence after primary tumor resection may be predicated on the successful modulation of IL level generation by host immunocytes.

Topics: Adenocarcinoma; Animals; Cell Division; Cells, Cultured; Colonic Neoplasms; Concanavalin A; Immunotherapy; Interleukin-1; Interleukin-2; Male; Monocytes; Neoplasm Metastasis; Neoplasm Recurrence, Local; Neoplasm Transplantation; Rats; Rats, Inbred Strains

In the adenocarcinoma cell line HT-29 receptor-bound insulin is substrate for a proteolytic process leading to the release of about half of the cell-associated [125I]monoiodoinsulin in the form of [125I]iodide and [125I]monoiodotyrosine. Classical lysosomal inhibitors (NH+4, methylamine, leupeptin) did not inhibit this proteolysis. Inhibitors of membrane traffic (chloroquine and monensin) and of metabolism (CN-) inhibited the fractional receptor-mediated degradation. The former led to an increased cell-associated 125I activity whereas the latter reduced the uptake. Sulphydryl reagents inhibited the receptor-mediated degradation. The data are not compatible with a quantitatively major role of lysosomes in the receptor-mediated insulin degradation. However, since the process requires energy it is suggested that the receptor-mediated degradation takes place in vesicles other than secondary lysosomes. The responsible enzyme(s) may belong to the thiol group of proteases. Both insulin and the insulin receptor are internalized as a consequence of incubation of HT-29 cells with insulin.

Topics: Adenocarcinoma; Adipose Tissue; Animals; Cell Line; Colonic Neoplasms; Concanavalin A; Fibroblasts; Humans; Hydrogen-Ion Concentration; Insulin; Iodine Radioisotopes; Lymphocytes; Rats; Receptor, Insulin; Sulfhydryl Reagents; Temperature

The immunological properties of thyroglobulins (Tg) of individual patients, obtained from a thyroid tumor and its adjacent tissue were compared, using conventional or monoclonal antibodies against human Tg. The thyroid tumors studied were non-functioning thyroid carcinomas and functioning thyroid adenomas. In contrast to non-functioning tumors, Tg from the functioning tumors was generally iodinated at a level close to that of normal tissue, and Tg from the tissue adjacent to the tumors had a very low iodine content. The conventional antiserum and monoclonal antibodies, B2F, seemed to recognize the conformation of Tg, while C6G showed a high affinity to Tg even when unfolded or denatured. In most cases, Tg isolated from the tissue adjacent to a tumor showed a higher affinity to antibodies than Tgs of the tumor tissue, as determined by the inhibitional effect of these Tgs against the binding of standard Tg and antibody. Furthermore, the Tg of the adjacent tissue was immunologically different in nature from the standard Tg obtained from a normal thyroid gland. From these results, Tgs of tumor and the adjacent tissue in individual patients were heterogeneous in immunological property, regardless of iodine content.

Topics: Adenocarcinoma; Adenoma; Antibodies, Monoclonal; Carcinoma, Papillary; Concanavalin A; Humans; Thyroglobulin; Thyroid Gland; Thyroid Neoplasms

Topics: Adenocarcinoma; alpha-Fetoproteins; Animals; Carcinoma, Hepatocellular; Concanavalin A; Diagnosis, Differential; Humans; Isoenzymes; L-Lactate Dehydrogenase; Liver Neoplasms; Lung Neoplasms; Mediastinal Neoplasms; Mesonephroma; Mice; Protein Binding

Concanavalin A (Con A)-induced anchorage of the major cell surface sialoglycoprotein component complex (ASGP-1/ASGP-2) was studied in 13762 rat mammary adenocarcinoma sublines with mobile (MAT-B1 subline) and immobile (MAT-C1 subline) cell surface Con A receptors. Treatment of cells, isolated microvilli, or microvillar membranes with Con A resulted in marked retention of ASGP-1 and ASGP-2, a Con A-binding protein, in cytoskeletal residues of both sublines obtained by extraction with Triton X-100 in PBS. When Con A-treated microvillar membranes were extracted with a buffer containing Triton X-100, the sialoglycoprotein complex was found associated in the residues with a transmembrane complex composed of actin, a 58,000-dalton polypeptide, and a cytoskeleton-associated glycoprotein (CAG), also a Con A-binding protein, in MAT-C1 membranes, and of actin and CAG in MAT-B1 membranes. Untreated membrane Triton residues retained very little ASGP-1/ASGP-2 complex. Association of the sialoglycomembrane complex and the transmembrane complex was also demonstrated in Con A-treated, but not untreated, microvilli by their comigration on CsCl gradients. Association of both complexes with the cytoskeleton of microvilli was shown by sucrose density gradient centrifugation. A fraction of the polymerized actin comigrated with the transmembrane complex alone in the absence of Con A and with both the transmembrane complex and the sialoglycoprotein complex in the presence of Con A. From these results we propose that anchorage of the sialoglycoprotein complex to the cytoskeleton on Con A treatment occurs by cross-linking ASGP-2, the major cell surface Con A-binding component, to CAG of the transmembrane complex, which is natively linked to the cytoskeleton via its actin component. Since Con A-induced anchorage occurs in sublines with mobile and immobile receptors, the anchorage process cannot be responsible for the differences in receptor mobility between the sublines.

Topics: Actins; Adenocarcinoma; Animals; Cell Adhesion; Cells, Cultured; Concanavalin A; Cytoskeleton; Detergents; Female; Glycoproteins; Mammary Neoplasms, Experimental; Membrane Proteins; Microvilli; Protein Binding; Rats; Receptors, Concanavalin A

The lectin (PHA and Con A) induced agglutination of a human tumour cell line (lung adenocarcinoma and osteosarcoma) was estimated by the spectrophotometric method. A decrease in the optic density for 1 min (delta D) of cell suspension and the time (t0) necessary for a complete sedimentation of cells (at delta D = 0) were used as quantitative indicators of agglutination. An increase in the concentration of tumour cells and lectins resulted in an increase of delta D and a decrease of t0. The results of spectrophotometry were correlated with the microscopic study data for tumour cells agglutination.

Topics: Adenocarcinoma; Agglutination; Cell Aggregation; Cell Count; Cells, Cultured; Concanavalin A; Humans; Lectins; Lung Neoplasms; Neoplasms; Osteosarcoma; Phytohemagglutinins; Spectrophotometry

The suppressor activity induced by Concanavalin A (Con A) was evaluated in peripheral lymphocytes from 20 patients with solid malignant tumors of different origin, that is: 9 lung epidermoid carcinomas; 6 breast adenocarcinomas and 5 melanomas. Simultaneously 10 normal control subjects were studied. No significant differences in the percentage of suppression were found in patients bearing breast adenocarcinoma and lung epidermoid carcinoma as compared to normal subjects. Melanoma patients, on the contrary, showed significant differences on the same test. On the other hand, the Con A lymphoproliferative response was found to be only significantly increased in the melanoma patients compared to normal controls. No differences were found in the percentage of peripheral blood lymphocytes between patients and controls.

Topics: Adenocarcinoma; Adult; Aged; Breast Neoplasms; Carcinoma, Squamous Cell; Concanavalin A; Humans; In Vitro Techniques; Lung Neoplasms; Lymphocyte Activation; Lymphocytes; Melanoma; Middle Aged; T-Lymphocytes, Regulatory

Tumor pairs, selected on the basis of their different capacities to metastasize in vivo (SP73/AS and ASML from the rat, Eb/ESb from the mouse), have been assayed for their membrane associated actin through the DNase inhibition assay. It is found that, provided inhibitions per cell are corrected for the influence of gross heterogeneities in size distributions, the more metastatic tumor cells have significantly higher DNase I inhibitions than their less invasive counterparts. This observation, which extends our previous study of normal recirculating lymphocytes, is rationalized by postulating a participation of these actin pools to a property critical for both normal recirculation and metastatic spreading, arguments are presented which favor cell surface deformability as a possible candidate.

Topics: Actins; Adenocarcinoma; Animals; Concanavalin A; Deoxyribonuclease I; Endodeoxyribonucleases; Female; Fibrosarcoma; Lymphoma; Male; Neoplasm Metastasis; Neoplasms; Rats

In the present study we have evaluated monocyte phagocytosis and T lymphocyte in vitro reactivity to mitogens in peripheral blood samples from 14 colorectal cancer patients, from 21 nonneoplastic control patients, and from 22 normal donors. Monocyte and lymphocyte functions were tested before and 1 and 6 months after surgery. Our results indicate the existence of increased monocyte phagocytosis and decreased mitogen reactivity in untreated patients with advanced tumors. These abnormal responses persisted and were even more pronounced after surgery and chemotherapy.

Topics: Adenocarcinoma; Adult; Aged; Colonic Neoplasms; Concanavalin A; Female; Humans; Lymphocyte Activation; Lymphocytes; Male; Middle Aged; Monocytes; Phagocytosis; Phytohemagglutinins; Rectal Neoplasms; Rosette Formation

Rat 13762NF mammary adenocarcinoma cell surface glycoproteins from s.c. tumor- or lung metastases-derived cell clones of differing spontaneous metastatic potentials were examined for their relationship to metastasis. After treatment with neuraminidase, lectin-binding assays showed that highly metastatic clone MTLn3 cells express approximately twice the quantity of peanut agglutinin (PNA) binding sites (approximately 2.3 X 10(8) sites/cell) than clones of lower metastatic potential. However, the number of wheat germ agglutinin (WGA)-binding sites on the various cell clones decreased slightly as the metastatic potential of the clones increased. The quantities of concanavalin A (conA)-binding sites were similar (approximately 1.7 X 10(8) sites/cell) in all cell clones and growth conditions. Glycoprotein analysis was performed by electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate (SDS-PAGE) and subsequent staining with 125I-labeled lectins. SDS-PAGE gels stained with 125I-labeled conA revealed mainly one glycoprotein (Mr approximately 150 kD), and the amounts of this glycoprotein did not correlate with metastasis. Differences in WGA-binding glycoproteins were detected between s.c. tumor- and lung metastases-derived cell clones. Several desialylated glycoproteins were detected with 125I-labeled PNA after SDS-PAGE, and the labeling intensity of one (Mr approximately 580 kD) correlated with the metastatic potentials of the various cell clones. This high Mr galactoprotein was further analyzed by [3H]glucosamine metabolic labeling, solubilization, sequential gel filtration, and chondroitinase ABC treatment prior to SDS-PAGE. The 580 kD galactoprotein was expressed in increased amounts on the more highly metastatic clones. Chemical labeling of cell surface sialic acid residues using periodate treatment followed by [3H]borohydride reduction showed an additional change in a major sialoglycoprotein (Mr approximately 80 kD), which decreased in labeling intensity on clones of increasing metastatic potential. The results suggest quantitative changes in cell surface glycoproteins rather than major qualitative alterations are associated with differences in the metastatic behavior of 13762NF tumor cell clones.

Topics: Adenocarcinoma; Animals; Arachis; Binding Sites; Clone Cells; Concanavalin A; Glycoproteins; Lectins; Mammary Neoplasms, Experimental; Membrane Proteins; Mice; Neoplasm Metastasis; Neoplasm Proteins; Peanut Agglutinin; Plant Lectins; Sialoglycoproteins; Surface Properties; Wheat Germ Agglutinins

Cell suspensions from the R 3230 AC rat mammary adenocarcinoma, when injected intravenously into F344 rats, invariably produce multiple lung foci within 10 days. We compared the colonization potential of cultures obtained from these foci and from cell populations exposed to 100 micrograms/ml medium of both concanavalin A and wheat germ agglutinin for 5 passages with the original cell line. Plasminogen activator activity (PAA) was determined in all three cell subpopulations, using S2251 (KABI) as chromogenic substrate. All cell lines retained their ability to grow after subcutaneous implant. The lectin resistant variant was found to have lost its capacity to nidate in the lung completely and also had the lowest PAA. In contrast, the cell population derived from the lung foci ranked highest in PAA.

Topics: Adenocarcinoma; Animals; Cell Line; Concanavalin A; Female; Lectins; Mammary Neoplasms, Experimental; Neoplasm Metastasis; Neoplasm Transplantation; Plasminogen Activators; Rats; Rats, Inbred F344; Wheat Germ Agglutinins

Effects of trypsin treatment on insulin and concanavalin A binding to, and glucose and proline transport in, dissociated R3230AC mammary adenocarcinoma cells were examined. Reduction of binding of 125I-labelled insulin was dependent on the amount of trypsin used, the temperature and the time of the incubation period. Under conditions that reduced insulin binding by greater than 75%, transport of glucose and proline was reduced by less than 15%. Scatchard analysis of insulin binding after trypsin treatment yielded slopes similar to those from cells not exposed to trypsin, assuming either two classes of receptors or an average affinity, Ke. Dissociation of bound insulin from untreated or trypsin-treated cells was enhanced by addition of excess unlabelled ligand. Insulin added in vitro, which decreased glucose transport in untreated cells, produced a decrease in glucose transport in cells treated with trypsin for 5 min (insulin binding was decreased 35%), but not in cells treated for 45 min (insulin binding was decreased 90%). Binding of the plant lectin concanavalin A was also reduced by trypsin treatment, but to a lesser extent and with a different time-course than for insulin. Scatchard analysis of the binding of concanavalin A in untreated and trypsin-treated cells yielded comparable values for Kd. The insulinomimetic actions of concanavalin A on glucose transport were abolished after brief exposure to trypsin. Pre-treatment of cells with concanavalin A reduced insulin binding and partially protected insulin receptors from trypsin digestion, but the inability to remove all of the concanavalin A precluded its use as a method to protect insulin receptors. Thus, in this rat mammary tumor, the number, but not the affinity or functional activity, of insulin receptors can be reduced by trypsin treatment without significant effects on glucose or A system amino acid transport.

Topics: Adenocarcinoma; Animals; Concanavalin A; Female; Glucose; Insulin; Kinetics; Mammary Neoplasms, Experimental; Proline; Rats; Rats, Inbred F344; Receptor, Insulin; Receptors, Concanavalin A; Trypsin

Binding of insulin and Concanavalin A to primary cell cultures of the R3230AC rat mammary adenocarcinoma was studied as a function of time in culture. As the culture became confluent, the amount of insulin binding per cell increased with culture time and reached a plateau, whereas the binding of Con A to surface glycoproteins decreased to 50% of the initial value. Exposure of confluent cultures to insulin at 37 C resulted in down-regulation of the cell surface insulin receptors. The decrease in insulin binding was related to the ambient insulin concentration and the decreased numbers of receptors per cell with no apparent alteration in their affinity. The maximal decrease in receptor number was 60-70%. Cell cultures degraded significant amounts of insulin at 37 C, but the addition of bacitracin to the culture medium decreased the amount of degradation and increased the extent of down-regulation at each insulin concentration. Porcine proinsulin was less effective than insulin in competing with 125I-labeled insulin and inducing receptor down-regulation. Down-regulation of insulin receptors did not require protein synthesis. The rate of insulin-induced receptor loss was much faster than the decrease in insulin binding due to inhibition of protein synthesis by cyclohexamide. The estimated half-life of the insulin receptor was 10.5 h. Down-regulation of insulin receptors was reversible; regeneration of receptors to 50% of control levels occurred approximately 9.6 h after the removal of insulin and required protein synthesis. These results indicate that these mammary tumor cells retain the ability to regulate their insulin receptors.

Topics: Adenocarcinoma; Animals; Bacitracin; Cells, Cultured; Concanavalin A; Female; Insulin; Kinetics; Mammary Neoplasms, Experimental; Neoplasm Transplantation; Proinsulin; Rats; Receptor, Insulin

The activation of pure populations of cloned peritoneal macrophages for tumor cell cytotoxicity by Con A was demonstrated using a recently developed tumor cell clonogenic assay. Cloned macrophages were rendered cytotoxic by Con A at concentrations above 20 micrograms/ml. The tumor cell cytotoxicity was caused mainly by the tumoricidal activity of the Con A-activated cloned macrophages. Increasing The Con A-activation time from 24 hours to 48 hours and 72 hours heightened the cytotoxic activity of cloned macrophages. Cloned macrophages incubated with con A for only 2 hours possessed no cytotoxic effect. Culture fluid from cultures of activated macrophages exerted no tumor cell cytotoxicity. Alpha-methyl-D-mannoside, a specific receptor-binding inhibitor for Con A, was capable of blocking the activation of macrophages for cytotoxicity at 0.01 M concentration.

Topics: Adenocarcinoma; Animals; Cell Adhesion; Cell Survival; Cells, Cultured; Clone Cells; Concanavalin A; Female; Kinetics; Macrophages; Mammary Neoplasms, Experimental; Mice; Mice, Inbred C3H

To clarify immune response of regional lymph nodes in 30 patients with lung cancer, the T cell population, phytohemagglutinin (PHA) and Concanavalin A (ConA) stimulation and the T cell subpopulation bearing Ig-G Fc receptors (Tg cells) were tested concerning the clinical stage, histology and the lymph nodes locations. The T cell population, and PHA and ConA response rates in lymph nodes of stage I patients were grossly the same as those of benign lung diseases, but were statistically higher than those of stage III patients (p less than 0.025, p less than 0.005). Among the three histological types of lung cancer, regional lymph nodes of adenocarcinoma had the greatest T cell populations, and PHA and ConA responses. Concerning the location of lymph nodes, the closer the lymph nodes was to the tumor, the greater was its T cell population, and vice versa. However there was no difference in PHA and ConA responses. All lung cancer patients revealed a significant increase of Tg cells in regional lymph nodes and in their peripheral blood lymphocytes compared with peripheral blood lymphocytes in normal subjects (p less than 0.005).

Topics: Adenocarcinoma; Concanavalin A; Humans; Leukocyte Count; Lung Neoplasms; Lymph Nodes; Lymphocyte Activation; Phytohemagglutinins; T-Lymphocytes

To investigate the effects of concanavalin A on insulin binding to R3230AC mammary carcinomas, initial experiments were performed to characterize binding of concanavalin A. Concanavalin A binding was found to be specific and saturable. Equilibrium binding experiments demonstrated that addition of low concentrations of concanavalin A enhanced the binding of [3H]concanavalin A, suggestive of positively cooperative interactions. Binding of concanavalin A was responsive to hormonal alterations; tumor cells from diabetic rats showed enhanced binding of concanavalin A and insulin compared to cells from intact rats and administration of insulin to diabetic rats returned concanavalin A and insulin binding to levels seen in controls. Incubation of tumor cells with concanavalin A prior to addition of 125I-labelled insulin resulted in a reduction of insulin-binding capacity; succinyl-concanavalin A did not affect binding of insulin. The present inhibition of insulin binding by concanavalin A was highest at the lower insulin concentrations, providing a linearized Scatchard plot that yielded a calculated Kd value comparable to the low-affinity portion of the curvilinear Scatchard plot for insulin binding. The dissociation rate of bound insulin depended on receptor occupancy. Addition of concanavalin A after insulin binding reached equilibrium resulted in increased insulin binding at higher hormone concentrations, decreased rates of dissociation of insulin and a loss of the correlation between receptor occupancy and dissociation rates. Concanavalin A alone demonstrated an insulin-like effect on glucose transport, which in these tumor cells represents a decrease in transport of 3-O-methylglucose. These results suggest that binding of both concanavalin A and insulin to cells from this hormonally responsive neoplasm is under insulin regulation and demonstrates similar characteristics to those reported for a variety of normal cells. Furthermore, the interaction between concanavalin A and te cell membranes affects the affinity of the insulin receptor for insulin and appears to decrease the observed negative cooperativity.

Topics: 3-O-Methylglucose; Adenocarcinoma; Animals; Biological Transport; Concanavalin A; Diabetes Mellitus, Experimental; Female; Insulin; Kinetics; Mammary Neoplasms, Experimental; Methylglucosides; Rats; Receptor, Insulin

Topics: 4-Nitroquinoline-1-oxide; Adenocarcinoma; Animals; Concanavalin A; Gastric Mucosa; Intestinal Mucosa; Male; Methylnitronitrosoguanidine; Mucins; Rats; Staining and Labeling; Stomach Neoplasms

Concanavalin A (Con A)-inducible suppressor cell activity in peripheral blood lymphocytes (PBL) of urologic cancer patients and of appropriate controls with benign urologic disorders was measured concurrently. Although the proliferative responses to Con A of the cancer patients were significantly lower than those of controls, no difference in Con A-induced suppressor cell activity was demonstrated between cancer patients and controls when tested under a variety of conditions. Moreover, regression analysis revealed no correlation between the proliferative response to Con A and suppressor cell activity in either cancer patients or controls. The results indicated that Con A-inducible suppressor cell activity was unaltered in urologic cancer patients and suggested that suppressor cells of the type that can be activated by Con A were not involved in the general immunologic impairment frequently associated with urologic cancer.

Topics: Adenocarcinoma; Concanavalin A; Female; Humans; Kidney Calculi; Kidney Neoplasms; Lymphocyte Activation; Male; Middle Aged; Prostatic Hyperplasia; Prostatic Neoplasms; Prostatitis; T-Lymphocytes, Regulatory; Urethral Stricture; Urinary Bladder Neoplasms; Urinary Tract Infections; Urogenital Neoplasms

The human hepatoma cell line SK-HEP-1 has been shown by radioimmunoelectrophoresis to synthesize and secrete a protein which coprecipitates with human alpha 1-antitrypsin. This protein was indistinguishable from serum alpha 1-antitrypsin in terms of electrophoretic mobility, apparent subunit molecular weight (47,000), and binding to concanavalin-A. The protein identified as alpha 1-antitrypsin (alpha 1 AT) was secreted by seven clones derived from SK-HEP-1 and by twelve out of eighteen hybrid clones derived from the fusion of SK-HEP-1 with mouse RAG cells. There was no correlation between the expression of alpha 1 AT and that of human enzymes assigned to sixteen different autosomes. There was an imperfect correlation between the expression of alpha 1 AT and of the two chromosome 9 marker enzymes AK1 and AK3 (two discordant clones).

Topics: Adenocarcinoma; alpha 1-Antitrypsin; Animals; Carcinoma, Hepatocellular; Cell Line; Clone Cells; Concanavalin A; Humans; Hybrid Cells; Karyotyping; Liver Neoplasms; Mice; Molecular Weight

Intact viable 13762 mammary-adenocarcinoma ascites cells hydrolyse added ATP. The localization of hydrolysis product and inactivation by the slowly penetrating chemical reagent diazotized sulphanilic acid indicate that this ATPase is at the external surface of the cell. A number of features differentiate this enzyme from mitochondrial, myosin and cation-transport ATPases. It is stimulated by either Ca2+ or Mg2+ and has little or no activity in their absence. It is insensitive to ouabain, oligomycin and azide. It is the major ATPase activity found in homogenates of gently disrupted 13762 cels. The ATPase activity is inhibited at high substrate concentrations and shows an apparent stimulation by concanavalin A in isolated membranes, but not in intact cells. The stimulation by concanavalin A results predominantly from a release from substrate inhibition.

Topics: Adenocarcinoma; Adenosine Triphosphatases; Animals; Calcium; Cell Membrane; Concanavalin A; Female; In Vitro Techniques; Kinetics; Magnesium; Mammary Neoplasms, Experimental; Phosphoric Monoester Hydrolases; Rats

Topics: Adenocarcinoma; Aged; Cell Adhesion; Colonic Neoplasms; Concanavalin A; Cytotoxicity, Immunologic; Female; Humans; Male; Middle Aged; Phytohemagglutinins; Rectal Neoplasms; T-Lymphocytes

Topics: Adenocarcinoma; Adolescent; Adult; Aged; Concanavalin A; Female; Humans; Immunity, Cellular; Kidney Neoplasms; Lymphocyte Activation; Male; Middle Aged; Phytohemagglutinins; Tuberculin Test

A methotrexate/concanavalin-A conjugate (MTX/Con-A) was prepared by covalent cross-linking. The extent of substitution was approximately 5 moles methotrexate (MTX) per mole concanavalin A (Con-A). Inhibition of dihydrofolate reductase by the conjugate was only marginal when compared to MTX. However, MTX/Con-A showed a 7- to 116 times higher cytocidal activity than MTX against cultured KB cells and various established cell lines from mouse colon adenocarcinomas 26 and 38, and Lewis lung carcinoma. The effect of MTX/Con-A was diminished when the conjugate was preincubated with alpha-methyl-D-mannoside, a specific binding sugar to Con-A. MTX/Con-A efficiently incorporated into cells and retained in them for longer periods of time than was MTX. The strong cytocidal action of the conjugate could be explained by the higher incorporation rate and the longer retention time of the conjugate in the cells.

Topics: Adenocarcinoma; Animals; Cell Line; Colonic Neoplasms; Concanavalin A; Methotrexate; Mice; Neoplasms, Experimental

Alveolar macrophages (AM) obtained from F344 rats were rendered tumoricidal by incubation in vitro with cellfree culture supernatant fluids rich in macrophage-activating factor (MAF) activity harvested from mitogen-stimulated F344 rat lymphocytes. AM activated by this procedure destroyed syngeneic, allogeneic, and xenogeneic tumor cells but were not cytotoxic for nonneoplastic cells. MAF was encapsulated in multilamellar lipid vesicles (liposomes) and its ability to render AM tumoricidal was compared with that of free (unencapsulated) MAF. Liposome-encapsulated MAF rendered AM cytotoxic at concentrations up to 16,000 times lower than free MAF. These data demonstrate that AM can respond in vitro to lymphokines and that MAF encapsulated within liposomes is far more efficient in rendering AM tumoridical than free MAF.

Topics: Adenocarcinoma; Animals; Binding Sites; Cells, Cultured; Concanavalin A; Cytotoxicity, Immunologic; Lipopolysaccharides; Liposomes; Lymphokines; Macrophages; Male; Mammary Neoplasms, Experimental; Rats; Rats, Inbred F344

The ultrastructural organization of the cells of the transplantable prostatic adenocarcinoma of the rat, R3327H, has been studied on a cytochemical level. The techniques used were those to localize lipids, peroxidase, and carbohydrate-like substances. This study has clearly shown that there are, in the tumor cells and not in normal prostatic epithelial cells, both lipid compartments with an intense peroxidase membrane. Within the lipid "droplet" we find it to be compartmentalized by conconavalan A-positive material. These observations suggest that this tumor cell may be a "degenerating" or old cell. It may well be that this cancer is a disease of dying cells--the degrading consequence of cell growth.

Topics: Adenocarcinoma; Animals; Carbohydrates; Cell Survival; Concanavalin A; Histocytochemistry; Intracellular Membranes; Lipids; Male; Neoplasms, Experimental; Peroxidases; Prostatic Neoplasms; Rats

Topics: Adenocarcinoma; Animals; Cell Membrane; Concanavalin A; Female; Glucosamine; Glycoproteins; Mammary Neoplasms, Experimental; Membrane Proteins; Mice; Molecular Weight

We have recently described the presence of a guanylate cyclase [GTP pyrophosphate-lyase (cyclizing), EC 4.6.1.2] inhibitor (GCI) in an aqueous extract of the balsam pear (Momordica charantia abbreviata). Because the guanylate cyclase-cyclic GMP system is though to be involved in cell growth, DNA and RNA synthesis, and possible malignant transformation, we examined the effect of the aqueous extract containing GCI on an undifferentiated adenocarcinoma of the rat prostate and concanavalin-A-stimulated [3H]thymidine incorporation into cultured splenic lymphocytes, a process thought to be mediated by cyclic GMP. The results demonstrate that the extract of the balsam pear blocks both the growth of the rat prostatic adencarcinoma in vitro and [3H]thymidine incorporation into DNA. DNA histograms from flow cytometry indicated that the extract containing GCI inhibited in the G2 + M phase of the cell cycle, a presumed locus of cyclic GMP effects. In addition, guanylate cyclase activity was significantly greater in the tumor than normal prostate tissue and was decreased by the extract containing GCI. Cyclic GMP levels in the tumor in culture wer also decreased by addition of the extract. It remains to be determined whether or not the anti-tumor agent and GCI are the same substance.

Topics: Adenocarcinoma; Animals; Cell Cycle; Concanavalin A; Cyclic GMP; Guanylate Cyclase; In Vitro Techniques; Male; Neoplasms, Experimental; Plant Extracts; Prostatic Neoplasms; Thymidine

Con A-Sepharose affinity chromatography was utilized to examine the glycoproteins in phosphosaline extracts of normal and breast tumor tissues and breast patient sera. In extracts of normal breast tissue, normal sera and patient sera, all glycoproteins were eluted from the Con A-Sepharose with a linear gradient of 0.0-0.5 M alpha-methylmannose. Using breast tumor extracts, a glycoprotein peak which could not be eluted as with normal tissue extracts was observed. This tightly-binding peak could be eluted from the Con A-Sepharose with acetate buffer containing 1.0 M KCl. Polyacrylamide electrophoresis of this tightly-binding glycoprotein peak revealed one major glycoprotein and four minor glycoproteins. The major glycoprotein obtained from electrophoresis represented about 60% of the Con A-Sepharose tightly-binding protein and reacted with antiserum to human orosomucoid (alpha 1-acid glycoprotein). All glycoproteins isolated from tumor tissue extracts appeared to represent normal serum constituents as they were retained on an immunoadsorbent containing antibodies to normal serum proteins. The possible significance of the isolated tumor-associated orosomucoid is discussed.

Topics: Adenocarcinoma; Breast Neoplasms; Chromatography, Affinity; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Female; Humans; Immunodiffusion; Orosomucoid

Topics: Adenocarcinoma; Animals; Cell Survival; Cell-Free System; Concanavalin A; Cytopathogenic Effect, Viral; Lymphocyte Activation; Lymphocyte Culture Test, Mixed; Lymphocytes; Lymphoma; Mammary Neoplasms, Experimental; Rats; Rats, Inbred BN; Rats, Inbred F344; Rats, Inbred WF; Spleen; Thymidine; Ultracentrifugation; Ultrasonics; Ultraviolet Rays

Topics: Adenocarcinoma; Agglutination; Animals; Antigens, Neoplasm; Anura; Ascites; Cell Line; Cell Membrane; Cell Nucleus; Concanavalin A; Inclusion Bodies; Kidney Neoplasms; Rana pipiens

Topics: Adenocarcinoma; Animals; Cell Line; Cell Survival; Concanavalin A; Guinea Pigs; Immune Sera; Lymphocyte Activation; Lymphocytes; Mammary Neoplasms, Experimental; Neoplasm Transplantation; Neutralization Tests; Oncogenic Viruses; Rats; Rats, Inbred WF; Tumor Virus Infections

Macrophage-activating factor (MAF) was obtained from cultures of normal F344 rat lymphocytes incubated with insoluble concanavalin A. The MAF rendered macrophages from normal C57BL/6 mice cytotoxic against the syngeneic B16 melanoma and the allogeneic AC 15091. At the same time, normal syngeneic or allogeneic embryo cells were unharmed, even in the presence of susceptible tumor cells. Optimal MAF levels followed incubation of lymphocytes for 48 hr with Sepharose-bound concanavalin A. A 2-hr incubation of macrophages with MAF was sufficient to initiate activation, providing that 46 hr were allowed to elapse before tumor cells were added. The MAF activity was enhanced after heating the supernatant to 199 degrees. Control experiments largely excluded the possibility that residual unbound concanavalin A caused the observed macrophage-mediated tumoricidal effects.

Topics: Adenocarcinoma; Animals; Cells, Cultured; Concanavalin A; Cytotoxicity Tests, Immunologic; Lymphocytes; Macrophages; Melanoma; Mice; Mice, Inbred C57BL; Neoplasms, Experimental; Rats; Rats, Inbred F344; Time Factors

The properties of the amylase produced by carcinoma of the lung were studied. The abnormal amylase recognized in the serum of a patient with carcinoma of the lung had a mobility with beta-position and showed reduced migration to the cathodic side after neuraminidase digestion. This abnormal amylase had a close affinity for Concanavalin A and this affinity was not retarded by the neuraminidase digestion. However, the purified, tumor-extracted, amylase from the same patient had the same electrophoretic migration as normal human salivary amylase and was not affected by neuraminidase treatment. The abnormal affinity for Concanavalin A was not observed in this purified tumor-extracted amylase. It is suggested that some transglycosidation steps are needed for the appearance of the abnormal amylase in the patient's serum, and that the terminal sialic acid is independent of the affinity for Concanavalin A. The dissociation constants of the tumor amylase for several substrates were smaller than those of normal pancreatic or salivary amylases. Moreover, maltotriose had no affinity for the tumor-extracted amylase and it was not digested to maltose and glucose by the purified tumor extracted amylase. These differences in the kinetic properties and in the mode of digestion were of interest in the study of tumor-produced amylases.

Topics: Adenocarcinoma; Adult; Amylases; Chromatography, Affinity; Concanavalin A; Humans; Kinetics; Lung Neoplasms; Male; Organ Specificity; Protein Binding; Saliva; Starch

The in vivo tumorigenicity of malignant mouse-nonmalignant human somatic cell hybrids was correlated with the in vitro characteristics. The renal adenocarcinoma mouse cell line RAG and the normal, diploid human cell line Wl-38 were used as the fusion parents. Five independent RAG Wl 38 hybrid clones were tested for concanavalin A (Con A) agglutination patterns, in vitro invasiveness, and tumor formation in immunosuppressed mice. Tests on the parental lines showed that RAG cells agglutinated at much lower levels of Con A than the Wl-38 cells. RAG cells overgrew Wl-38 cells in the in vitro invasiveness assay. RAG cells readily formed tumors in untreated adult or young immunosuppressed mice, whereas the Wl-38 cells did not. The five hybrid clones were all similar, since they had Con A agglutination levels intermediate to those of both parents, though patterns were more "tumor-like", overgrew the Wl-38 cells in the invasiveness assay, and formed tumors in immunosuppressed mice.

Topics: Adenocarcinoma; Agglutination; Animals; Cell Division; Chromosomes; Concanavalin A; Humans; Hybrid Cells; Immunosuppression Therapy; Kidney Neoplasms; Male; Mice; Neoplasms, Experimental

The mitogens concanavalin A (Con A) and bacterial lipopolysaccharide (LPS) stimulated normal spleen cells of DBA/2J, CBA/J, and BALB/c mice about equally in the presence of either isologous or homologous serum. This system revealed that sera from mice with five different methylcholanthrene-induced rhabdomyosarcomas inhibited mitogen stimulation of normal spleen cells. Sera from mice with a mammaryadenocarcinoma and spontaneous rhabdomyosarcoma were similarly suppressive. In contrast, sera from mice with melanoma were not inhibitory and often enhanced stimulation. Sera from tumor-bearing animals had the same effects both qualitatively and quantitatively on cells from the strain carrying the tumor and on cells from the other two strains. The mixed lymphocyte response of CBA/J times BALB/c spleen cells was affected exactly as were the responses to mitogen by the various sera. Stimulation by mitogen of mouse lymph-node cells and spleen cells with macrophages removed, as well as that of guinea pig spleen cells, was also inhibited by sera from mice with rhabdomyosarcoma and mammary adenocarcinoma.

Topics: Adenocarcinoma; Animals; Blood; Concanavalin A; Guinea Pigs; Lipopolysaccharides; Lymph Nodes; Lymphocyte Activation; Lymphocyte Culture Test, Mixed; Lymphocytes; Mammary Neoplasms, Experimental; Melanoma; Methylcholanthrene; Mice; Mice, Inbred BALB C; Mice, Inbred CBA; Mice, Inbred DBA; Mitogens; Neoplasms, Experimental; Polysaccharides, Bacterial; Rhabdomyosarcoma; Sarcoma, Experimental; Spleen

Topics: Adenocarcinoma; Carcinoembryonic Antigen; Carcinoma, Hepatocellular; Chromatography, Affinity; Colonic Neoplasms; Concanavalin A; Freeze Drying; Glutaral; Humans; Liver Neoplasms; Neoplasm Metastasis

The rat mammary adenocarcinoma 13762A is weakly immunogenic in syngeneic hosts. Transplantation immunity is not developed after injection of irradiated tumor cells. Two cell types were isolated from the tumor: one grew slowly forming solid implants; the second grew rapidly in ascites form, even in allogeneic hosts. Spleen cells cytotoxic for a tissue culture derivative of the tumor were produced in animals after injection of either cell type indicating a common antigen. The kinetics of tumor growth and production of cytotoxic spleen cells were compared in syngeneic and allogeneic animals. In vivo rejection of the tumor in allogeneic hosts did not correlate with the in vitro assay of spleen lymphocyte cytotoxicity. Futhermore, the cytotoxic response of spleen cells from syngeneic tumor-bearing hosts parallels that found in allogeneic hosts.

Topics: Adenocarcinoma; Agglutination Tests; Animals; Ascitic Fluid; Concanavalin A; Cytotoxicity Tests, Immunologic; Female; Kinetics; Mammary Neoplasms, Experimental; Rats; Rats, Inbred F344; Rats, Inbred Lew; Spleen; Transplantation, Homologous; Transplantation, Isogeneic

Cell surface structures of two mouse ascites tumors were studied using lectins. The tumors are sublines of the spontaneous mammary adenocarcinoma TA3 in strain A, differing in two main characteristics. Subline TA3-St grows only in syngeneic mice and has high expression of H-2 antigens. Subline TA3-Ha, in contrast, proliferates in all mouse strains, and has low amounts of exposed H-2 antigens. Concanavalin A (Con A), phytohemagglutinin (PHA) and Helix pomatia anti A hemagglutinin (HP) were used in agglutination tests, in binding experiments with 125I-labelled lectins and also in fluorescence studies with FITC-labelled lectins. Con A and PHA agglutinated the TA3-St cells but not the TA3-Ha cells. However, fluorescein-labelled Con A and PHA were bound to all cells (greater than 90%) of both sublines. Moreover both cell types contained an identical number of Con A receptors. The same result was obtained when the number of PHA receptors on the two sublines was compared. HP agglutinated TA3-Ha cells but not TA3-St cells. However, in this case, the difference in agglutinability between the lines was due to the presence or absence of HP receptors. All TA3-Ha cells contained large numbers of HP receptors. In contrast the majority (greater than 90%) of the TA3-St cells lacked HP receptors. (See article.) Trypsin released the HP receptors from TA3-Ha cells, at the same time making these cells agglutinable by both Con A and PHA. We conclude that the Ta3-Ha cells have a trypsin sensitive surface glycoprotein (or glycoproteins) detectable by HP, which is absent on most TA3-St cells. It is possible that this glycoprotein interferes with the agglutinability of TA3-Ha cells by Con A and PHA; whether it is also responsible for the low expression of H-2 alloantigen on this cell remains to be seen.

Topics: Adenocarcinoma; Animals; Cell Aggregation; Cell Line; Cells, Cultured; Concanavalin A; Fluorescent Antibody Technique; Hemagglutinins; Iodine Radioisotopes; Lectins; Mammary Neoplasms, Experimental; Mice; Mice, Inbred Strains

The carcinoembryonic antigen (CEA) of normal and pathological tissue extracts was separated into two variants, Concanavalin A reactive (CEAr) and non-reactive CEA (CEAn) by affinity chromatography on Con A Sepharose columns. CEAr was the quantitatively predominant variant. CEAn varied in concentration between 0.2 and 6 percent of the total CEA activity. The affinity of CEAn for anti-CEA antibodies was significantly lower than that of CEAr. Pooled extracts of primary adenocarcinomas of the colon contained CEAn in the lowest concentration and with the least affinity for antibodies. It is suggested that a deficiency and/or steric blocking of alpha-D-mannopyranosyl residues in CEAn reduce the affinities for both antibodies and Con A.

Topics: Adenocarcinoma; Carcinoembryonic Antigen; Chromatography, Affinity; Colonic Neoplasms; Concanavalin A; Fetus; Genetic Variation; Humans; Liver; Liver Cirrhosis; Liver Neoplasms; Lung; Neoplasm Metastasis; Organ Specificity; Radioimmunoassay; Spleen

Topics: Adenocarcinoma; Animals; Concanavalin A; Female; Fibrosarcoma; Immunotherapy; Mammary Neoplasms, Experimental; Methylcholanthrene; Mice; Mice, Inbred C3H; Mice, Inbred C57BL; Mitomycins; Neoplasm Transplantation; Neoplasms, Experimental; Neuraminidase; Sarcoma, Experimental; Transplantation, Homologous; Vibrio cholerae

Topics: Adenocarcinoma; Animals; Antigens, Neoplasm; Cell Membrane; Concanavalin A; Epitopes; Female; Fibrosarcoma; Immunotherapy; Mammary Neoplasms, Experimental; Melanoma; Mice; Mice, Inbred C3H; Mice, Inbred C57BL; Neoplasm Transplantation; Neoplasms, Experimental; Neuraminidase; Sarcoma, Experimental; Transplantation, Homologous; Vibrio cholerae

Topics: Adenocarcinoma; Concanavalin A; Humans; Hypersensitivity, Delayed; Immunologic Memory; Lectins; Lymphocyte Activation; Lymphocyte Culture Test, Mixed; Melanoma; Neoplasms; Nitrobenzenes; Sarcoma; Skin Tests

Topics: Acetamides; Adenocarcinoma; Agglutination; Animals; Carcinogens; Cell Differentiation; Cell Membrane; Colonic Neoplasms; Concanavalin A; Epithelium; Galactose; Glucosamine; Glucosyltransferases; Hydrazines; Intestinal Neoplasms; Intestines; Lectins; Neoplasms, Experimental; Rats; Rats, Inbred Strains; Transferases

Topics: Adenocarcinoma; Animals; Antigens, Neoplasm; Concanavalin A; Female; Fibrosarcoma; Immunotherapy; Mammary Neoplasms, Experimental; Melanoma; Methylcholanthrene; Mice; Mice, Inbred Strains; Mitomycins; Neoplasm Transplantation; Neuraminidase; Sarcoma, Experimental; Vibrio cholerae

Topics: Adenocarcinoma; Agglutination; Animals; Antigens, Neoplasm; Cell Count; Cell Line; Chromosomes; Concanavalin A; Electrophoresis; Female; Immunity, Cellular; Male; Mammary Neoplasms, Experimental; Mice; Mice, Inbred Strains; Microscopy, Electron, Scanning; Neoplasm Transplantation; Species Specificity