alpha-chymotrypsin and Adenocarcinoma

Bowman-Birk inhibitors (BBI) from soybean and related proteins are naturally occurring protease inhibitors with potential health-promoting properties within the gastrointestinal tract. In this work, we have investigated the effects of soybean BBI proteins on HT29 colon adenocarcinoma cells, compared with non-malignant colonic fibroblast CCD-18Co cells. Two major soybean isoinhibitors, IBB1 and IBBD2, showing considerable amino acid sequence divergence within their inhibitory domains, were purified in order to examine their functional properties, including their individual effects on the proliferation of HT29 colon cancer cells. IBB1 inhibited both trypsin and chymotrypsin whereas IBBD2 inhibited trypsin only. Despite showing significant differences in their enzyme inhibitory properties, the median inhibitory concentration values determined for IBB1 and IBBD2 on HT29 cell growth were not significantly different (39.9+/-2.3 and 48.3+/-3.5 microM, respectively). The cell cycle distribution pattern of HT29 colon cancer cells was affected by BBI treatment in a dose-dependent manner, with cells becoming blocked in the G0-G1 phase. Chemically inactive soybean BBI had a weak but non-significant effect on the proliferation of HT29 cells. The anti-proliferative properties of BBI isoinhibitors from soybean reveal that both trypsin- and chymotrypsin-like proteases involved in carcinogenesis should be considered as potential targets of BBI-like proteins.

Topics: Adenocarcinoma; Alkylation; Anticarcinogenic Agents; Cell Proliferation; Cell Survival; Chymotrypsin; Colorectal Neoplasms; Dose-Response Relationship, Drug; HT29 Cells; Humans; Inhibitory Concentration 50; Peptide Mapping; Protein Interaction Domains and Motifs; Protein Isoforms; Resting Phase, Cell Cycle; Sequence Alignment; Serine Proteinase Inhibitors; Time Factors; Trypsin Inhibitor, Bowman-Birk Soybean; Trypsin Inhibitors

The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. However, its other pathophysiological functions are still not very well understood. This can be attributed mainly to a lack of appropriate molecular probes that can selectively modulate the immunoproteasome catalytic subunits. Herein, we report the development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome. We show that these compounds irreversibly modify the LMP2 subunit with high specificity. Importantly, LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.

Topics: Adenocarcinoma; Animals; Catalytic Domain; Cell Line, Tumor; Chymotrypsin; Cysteine Endopeptidases; Humans; Male; Mice; Molecular Probes; Neovascularization, Pathologic; Prostatic Neoplasms; Proteasome Endopeptidase Complex; Serine

Dimethylbenzanthracene (DMBA) induces pancreatic adenocarcinomas in rats 9 months after carcinogen exposure, with precursor lesions (tubular complexes) developing 1 month after initiation of treatment. Because previous studies have suggested an acinar cell of origin for these tumors, we investigated the expression pattern of ductal, acinar, and islet cell markers in these cancers to gain insight into their phenotype and cell of origin. Pancreatic neoplasms were induced in rats by implantation of DMBA into the head of the pancreas. Lesions studied included 10 early tubular complexes (DMBA for 2 weeks), 8 tubular complexes (DMBA for 1 month), and 10 adenocarcinomas (DMBA for 9 months). Normal rat pancreas served as a control. For comparison, 5 human ductal adenocarcinomas were also evaluated. Immunohistochemistry with ductal (keratin, cytokeratin 19, cytokeratin 20), acinar (chymotrypsin), and islet (chromogranin A) cell markers was performed to analyze the tissues. Rat tubular complexes and adenocarcinomas revealed strong expression of keratin, cytokeratin 19, and cytokeratin 20 in the cytoplasm of all neoplastic cells, absence of chymotrypsin, and rare immunoreactivity to chromogranin A. Human adenocarcinomas showed strong expression of keratin and cytokeratin 19 in all neoplastic cells, expression of cytokeratin 20 in 5-20% of cells, and absence of chymotrypsin and chromogranin A. Pancreatic adenocarcinomas induced by DMBA in rats express markers consistent with a ductal phenotype, as observed in human tumors. Ductal marker expression in early tumor stages suggests a ductal cell of origin.

Topics: 9,10-Dimethyl-1,2-benzanthracene; Adenocarcinoma; Aged; Animals; Biomarkers, Tumor; Chromogranin A; Chromogranins; Chymotrypsin; Female; Humans; Immunohistochemistry; Intermediate Filament Proteins; Keratin-20; Keratins; Male; Pancreas; Pancreatic Neoplasms; Precancerous Conditions; Rats; Rats, Sprague-Dawley

Using specific substrates, benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide, benzyloxycarbonyl-Gly-Gly-Arg-2-naphthylamide and benzyloxycarbonyl-Leu-Leu-Glu-2-naphthylamide, cytosolic chymotrypsin-like, trypsin-like and cucumsin-like activities were determined, respectively, in rat epithelial tissues and differentiated human Caco-2 cells. The cytosolic fractions of rat colonic, rectal, nasal, and alveolar epithelial cells and differentiated human Caco-2 cells contained these three distinct enzyme activities. However, effects of enzyme inhibitors revealed that these three distinctive activities were not extensively involved in cytosolic or homogenate degradation of insulin and insulin-like growth factor I (IGF-I). It is concluded that proteasome-like activities may not significantly limit nonparenteral absorption of peptide and protein drugs such as insulin and IGF-I.

Topics: Adenocarcinoma; Animals; Cell Differentiation; Chromatography, High Pressure Liquid; Chymotrypsin; Colonic Neoplasms; Cytosol; Epithelial Cells; Epithelium; Humans; Insulin; Insulin-Like Growth Factor I; Male; Rats; Rats, Sprague-Dawley; Trypsin

The ability of tumor cells to express elevated levels of proteinases capable of degrading tissue matrix and basement membrane components in vitro has been correlated to their invasive and metastatic potential. Many in vitro invasion assays have been performed either in the presence of serum or with tumor cells that had been previously grown in serum. Since serum contains large amounts of active proteinase inhibitors, their presence could complicate interpretations. We have, therefore, attempted to measure the amounts of serine proteinase inhibitors released into culture medium by two rat mammary adenocarcinoma metastatic variants selected in vitro for serum-independent growth and differing in their in vivo metastatic behavior. Concentrated spent media (CSM) derived from cultures of poorly metastatic MTLn2(T42D) and highly metastatic MTLn3(T17D) tumor cells, grown in the presence and absence of fetal bovine serum (FBS) for 20-24 h, were compared for the presence of serine proteinase inhibitors capable of inactivating alpha-chymotrypsin. Our results show that when MTLn2(T42D) and MTLn3(T17D) tumor cells were exposed to FBS, the CSM of MTLn2(T42D) exhibited nearly 5-fold greater amounts of active proteinase inhibitors than that of MTLn3(T17D). The amount of proteinase inhibitory activity detected in the CSM of tumor cells not exposed to FBS was not eliminated but declined by 82% and 37% for MTLn2(T42D) and MTLn3(T17D), respectively. Analysis for enzyme-inhibitor (E-I) complex formation by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography confirmed the kinetic results and revealed that the major inhibitor present in CSM/FBS of both variants forms a heat- and sodium dodecyl sulfate-stable E-I complex with an apparent molecular weight of approximately 79,000, identical to that formed when FBS or purified alpha 1-proteinase inhibitor is incubated with [alpha-125I]chymotrypsin. E-I complexes with apparent molecular weights of 44,000 and 50,000 were formed from CSM/bovine serum albumin of MTLn3(T17D) and MTLn2(T42D), respectively, that were not detected when [alpha-125I]chymotrypsin was incubated with bovine serum albumin. We infer from these observations that, in culture, poorly metastatic MTLn2(T42D) tumor cells, as compared to their highly metastatic MTLn3(T17D) counterparts, exhibit an increased capacity to retain and subsequently release significantly greater amounts of serum-derived active proteinase inhibitors

Topics: Adenocarcinoma; Animals; Chymotrypsin; Electrophoresis, Polyacrylamide Gel; Female; Lung Neoplasms; Mammary Neoplasms, Experimental; Neoplasm Invasiveness; Neoplasm Metastasis; Rats; Rats, Inbred F344; Serine Proteinase Inhibitors

Incubation of monolayers of HT29-D4 cells (a clone of the human colonic adenocarcinoma cell line HT29) in the presence of 17.5 microM cycloheximide resulted in an increase in the number of vasoactive intestinal peptide (VIP) binding sites at the cell surface without any change in the affinity of receptor for its ligand. The increase in 125I-VIP-binding capacity was dose-dependent between 0.35 microM and 17.5 microM cycloheximide and was correlated with the inhibition of protein biosynthesis. At higher concentrations of drug (17.5-100 microM) a plateau corresponding to a twofold increase in VIP-binding capacity was reached independently of the extent of protein synthesis inhibition. We found that VIP receptors of HT29-D4 cells with such an enhanced binding capacity behaved like those of control cells with respect to receptor internalization and recycling (i.e. the cycle of occupied receptors was insensitive to cycloheximide). After inactivation of 90% of cell-surface VIP receptors by alpha-chymotrypsin, we observed a biphasic kinetic of reappearance of VIP-binding sites. 40% of VIP-binding sites reappeared very quickly (less than 5 min) and 100% within 17 h. The fast recovery of VIP receptors was probably due to the deployment of new binding sites from an intracellular pool. The rate and extent of recovery of these receptors were similar in control cells and in cycloheximide-treated cells. However, the slow recovery was inhibited in cycloheximide-treated cells probably because a pool of immature receptors was depleted by the drug before the alpha-chymotrypsin treatment. Our data are consistent with the existence of two different intracellular pathways of occupied and unoccupied VIP receptors.

Topics: Adenocarcinoma; Binding Sites; Cell Line; Chymotrypsin; Colonic Neoplasms; Cycloheximide; Dose-Response Relationship, Drug; Humans; Kinetics; Methionine; Receptors, Gastrointestinal Hormone; Receptors, Vasoactive Intestinal Peptide; Vasoactive Intestinal Peptide

Hepatoid adenocarcinomas of the stomach are gastric carcinomas with both adenocarcinomatous and hepatocellular differentiations. They usually produce large amounts of alpha-fetoprotein (AFP) with a Concanavalin A-binding property of hepatic type. In this study, these carcinomas occurred in older persons, with the antrum being a common site. Observed grossly, growth of the tumors was nodular and massive. Prognosis was poor because of frequent liver metastases. In the cytoplasms of tumor cells, various serum proteins were identified, including AFP, alpha-1 antitrypsin (AAT), alpha-1 antichymotrypsin (ACT), albumin, and prealbumin. Localizations of ferritin, prothrombin, and transferrin were demonstrated with less frequency. Adenocarcinomatous foci were composed of well-differentiated, intestinal-type epithelial cells and often contained carcinoembryonic antigen. These adenocarcinomatous and hepatoid areas were often intermingled with each other. There were extensive venous involvements by tumor cells. The poor prognosis of the tumors may be attributed to these involvements as well as to production of AFP and presence of AAT/ACT, which have immunosuppressive and protease-inhibitory properties, respectively.

Topics: Adenocarcinoma; Adult; Aged; Albumins; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; alpha-Fetoproteins; Carcinoembryonic Antigen; Carcinoma, Hepatocellular; Cell Differentiation; Cell Nucleus; Chymotrypsin; Cytoplasm; Female; Histocytochemistry; Humans; Immunoenzyme Techniques; Liver Neoplasms; Male; Middle Aged; Prealbumin; Prognosis; Staining and Labeling; Stomach Neoplasms

Human stomach adenocarcinomas containing alpha-1-antichymotrypsin (ACT) in their cell nuclei were transplanted into nude mice. The presence of ACT was monitored using an immunohistochemical technique with horseradish peroxidase-labeled rabbit anti-ACT Fab' as well as single radial immunodiffusion. Two weeks after transplantation, ACT could be found neither in transplanted carcinoma cells nor in the sera of carcinoma-bearing nude mice. However, if human ACT was injected i.v., it could be detected in the transplanted carcinoma cell nuclei 2 h after injection. The ACT was detected immunohistochemically and was confirmed by biochemical fractionation using 125I-labeled ACT. On the other hand, the amount of ACT production was not sufficient to indicate biosynthesis. These results demonstrated that ACT detected in stomach carcinoma cell nuclei was not synthesized in carcinoma cells but was incorporated from the blood circulation.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; Animals; Biological Transport; Cell Nucleus; Chymotrypsin; Humans; Mice; Mice, Nude; Neoplasm Transplantation; Stomach Neoplasms

Presence of lysozyme, lactoferrin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and ferritin was examined by the immunoperoxidase method in 15 consecutive parotid gland tumors as well as in normal parotid gland tissue. Lysozyme and lactoferrin were detected in intercalated duct cells of normal tissue and in the epithelial component of pleomorphic adenomas. alpha 1-antitrypsin, alpha 1-antichymotrypsin and ferritin were found in both epithelial and mesenchymal components of pleomorphic adenomas but not in normal parotid tissue. In the epithelial component of adenolymphoma only alpha 1-antichymotrypsin and lactoferrin were observed. The results would support a tentative histogenetic link between the intercalated duct cell and the epithelial component of the pleomorphic adenoma.

Topics: Adenocarcinoma; Adenolymphoma; Adenoma, Pleomorphic; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Chymotrypsin; Ferritins; Histocytochemistry; Humans; Immunoenzyme Techniques; Lactoferrin; Lactoglobulins; Muramidase; Parotid Neoplasms

Fourteen cases of mixed müllerian tumour (MMT) of the endometrium, six stromal sarcomas, five uterine leiomyosarcomas, and five leiomyomas were examined, using an immunoperoxidase technique, for the presence of alpha-1-antitrypsin (A1AT), alpha-1-antichymotrypsin (A1ACT), actin, and myosin. In addition, six cases of endometrial adenocarcinoma were examined for the presence of A1AT and A1ACT. Eleven MMT were positive for A1AT and 13 for A1ACT. All stromal sarcomas, four adenocarcinomas, four leiomyomas, and three leiomyosarcomas were positive for both. All leiomyomas and leiomyosarcomas were positive for myosin as were seven. MMT and three stromal sarcomas. Four leiomyomas, four leiomyosarcomas, six MMT, and three stromal sarcomas were positive for actin. These findings are related to those in the normal uterus and their practical and theoretical significance discussed.

Topics: Actins; Adenocarcinoma; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Chymotrypsin; Endometriosis; Female; Histocytochemistry; Humans; Leiomyoma; Leiomyosarcoma; Myosins; Sarcoma; Uterine Neoplasms

The immunologic reactivity of glycoprotein antigens extractable from individual, histologically different ovarian and uterine cancers was studied taking into account their relationship with carcinoembryonic antigen (CEA), nonspecific cross-reacting antigen (NCA), alpha-feto-protein (AFP), and alpha-1-antichymotrypsin. All studies were performed using specific immune sera against perchloric acid (PCA) extracts of ovarian mucinous cystadenocarcinoma (anti-PCA-CaOm) and cervical squamous cell carcinoma (anti-PCA-CaCx), and antisera against the reference antigens mentioned above. A considerable antigenic heterogeneity and the existence of several immunologically related antigenic systems were found: 1) CEA-like antigens; 2) NCA-type antigens; 3) an antigen different from CEA and NCA present in ovarian mucinous adenocarcinomas and often cross-reacting, but not identical with respective antigens of uterine body and cervical carcinomas; 4) an antigen reacting with anti-alpha-1-anti-chymotrypsin serum; and 5) an antigen reacting with anti-AFP serum.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; alpha-Fetoproteins; Antigens, Neoplasm; Carcinoembryonic Antigen; Carcinoma, Squamous Cell; Cell Adhesion Molecules; Chymotrypsin; Cross Reactions; Cystadenocarcinoma; Female; Genital Neoplasms, Female; Glycoproteins; Humans; Immune Sera; Immunologic Techniques; Ovarian Neoplasms; Tissue Extracts; Uterine Cervical Neoplasms; Uterine Neoplasms

Topics: Adenocarcinoma; Aged; alpha 1-Antichymotrypsin; Bronchial Neoplasms; Carcinoma, Squamous Cell; Chymotrypsin; Female; Humans; Immunoenzyme Techniques; Male; Middle Aged

We have studied the distribution of lysozyme (Ly), a1-antitrypsin (a1AT) and a1-antichymotrypsin ( a1AChy ) in the normal, chronically inflamed and neoplastic gall bladder mucosa using the peroxidase-anti-peroxidase (PAP) method. Ly was absent from the normal mucosa but it was found only in areas of glandular metaplasia of true antral type and in crypts of possible early metaplastic nature in cases of chronic cholecystitis. a1AT and a1AChy were also found in such metaplastic areas, but their presence was also observed immunohistochemically in areas of essentially normal and in non-metaplastic, chronically inflamed gall bladder mucosa. The possible local production of these substances by gall bladder epithelial cells is discussed. Ly, a1AT and a1AChy were also found in various histological types of adenocarcinoma of the gall bladder in varying degrees of frequency and intensity, unrelated to the histological type and invasiveness of the tumour.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Cholecystitis; Chymotrypsin; Gallbladder; Gallbladder Neoplasms; Histocytochemistry; Humans; Immunoenzyme Techniques; Muramidase

The spontaneous capillary tube migration of metastatic MAT 13762 rat mammary adenocarcinoma cells has been measured and compared with that of a non-metastatic variant, TGR. MAT 13762 cells migrated to a greater extent in the presence than in the absence of serum, and in both cases migration areas were considerably greater than for TGR cells. Different clones of hybrids, formed by fusing metastatic and non-metastatic variants, showed migration areas ranging from those of the metastatic to those of the non-metastatic parent cells. Despite their differing migrations, all of these clones were either non or only slightly metastatic. Treatment of TGR cells with trypsin enhanced their migration to that of MAT 13762 cells, whereas trypsin-treated MAT 13762 cells showed a slightly decreased migration. Although MAT 13762 cells, unlike TGR cells, produced large amounts of plasminogen activator (PA), no evidence was obtained for the direct involvement of PA in the high migration rate of MAT 13762 cells.

Topics: Adenocarcinoma; Animals; Cell Line; Cell Movement; Chymotrypsin; Colchicine; Female; Mammary Neoplasms, Experimental; Neoplasm Metastasis; Plasminogen Activators; Rats; Rats, Inbred F344; Trypsin

Antigenic reactivity of 35 perchloric acid (PCA) extracts of different histologic human lung cancer tissues was studied--in comparison with the reactivity of the carcinoembryonic antigen (CEA), the nonspecific cross-reacting antigen (NCA), and alpha-1-antichymotrypsin--with the use of specific immune sera against PCA extracts of lung squamous cell carcinoma, and anti-CEA, anti-NCA, and anti-alpha-1-antichymotrypsin sera. The following antigenic systems were found in lung cancers: a) antigens specific for most squamous cell cancers and adenocarcinomas, which are undetectable in small cell cancers; b) NCA-type antigens; c) CEA-like antigens; and d) the antigen responsible for alpha-1-antichymotrypsin reactivity. A considerable antigenic heterogeneity among lung cancers indicates the necessity for precise histopathologic verification of individual lung cancer cases before commencement of immunologic studies and purification of antigens specific for lung cancers.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; Antibody Specificity; Antigens, Neoplasm; Carcinoembryonic Antigen; Carcinoma, Small Cell; Carcinoma, Squamous Cell; Chymotrypsin; Cross Reactions; Humans; Immunodiffusion; Lung Neoplasms

Serum IAP and IS levels were studied in patients with stomach cancer. We found that the serum levels of IAP and IS increased as the disease progressed; their true positive rates as tumor markers were 49.3% and 39.8%, respectively. There was some delicate difference between these glycoproteins and T-cell subpopulation. IAP and IS correlated well with a correlation coefficient of 0.847, their value in clinical oncology are thought to be equivalent. Some difference was found between their substances and ASP, this might indicate the heterogeneous nature of the circulating glycoproteins in varying cancer-bearing status.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; Chymotrypsin; Glycoproteins; Humans; Immunity, Cellular; Neoplasm Proteins; Sialic Acids; Stomach Neoplasms

Lysozyme, alpha 1-Antichymotrypsin and alpha 1-Antitrypsin were demonstrated by an immunoperoxidase technique (PAP) in malignant cells of adenocarcinomas of the stomach but not of the large intestine. Lymph-node metastases showed identical immunoreactivity to that of the primary tumour. Neoplasms arising from the cardia, the body and the pyloric antrum of the stomach showed different immunostaining reactions. It seems that these differences partly reflect the distribution of lysozyme, alpha 1-Antichymotrypsin and alpha 1-Antitrypsin in the normal gastric mucosa. The usefulness of our findings in the identification of the primary tumour in cases of lymph node metastases of unknown origin, is also discussed.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Cardia; Chymotrypsin; Colonic Neoplasms; Gastric Mucosa; Histocytochemistry; Humans; Immunoenzyme Techniques; Lymphatic Metastasis; Muramidase; Pyloric Antrum; Stomach Neoplasms

The synthesis and release of glycoproteins were studied in organ cultures of human breast surgical specimens and in established breast epithelial cell lines, MCF-7 and MDA-MB-231. Biosynthesis was monitored by the incorporation of 14C-glucosamine. Labeled macromolecules in the culture supernatants were analyzed by biochemical and immunological techniques. One to 8% of the labeled glycoproteins from benign breast and infiltrating ductal carcinoma specimens was precipitated by antibodies produced against human serum alpha-1-antichymotrypsin. Twelve percent of the total glycoproteins from the culture supernatants of the MCF-7 cell line was identified as alpha-1-antichymotrypsin. Both the normal serum and the human breast epithelia-derived proteinase inhibitor can be resolved into similar subclasses by two-dimensional gel electrophoresis. MDA-MD-231 and MCF-7 cells which were extensively washed with EDTA, serum-free medium, and phosphate-buffered saline retain this proteinase inhibitor on their cell surfaces. Three to 4% of the total cell-surface iodinated components was immunoprecipitated by these specific antibodies. Since alpha-1-antichymotrypsin is a potent inhibitor of neutral proteinases such as cathepsin G, the demonstration of its synthesis by benign and malignant breast epithelial cells is of considerable interest. This glycoprotein may represent the epithelia's own protective shield of cell surface components and the cell's attempt to moderate the effects of invading leukocytes. In addition, it may play a regulatory role in the maintenance of three-dimensional glandular structures.

Topics: Adenocarcinoma; alpha 1-Antichymotrypsin; Breast; Breast Neoplasms; Cell Line; Chymotrypsin; Epithelium; Female; Humans; Molecular Weight; Organ Culture Techniques; Protease Inhibitors

The alpha-protein which we previously detected in PCA extracts of malignant tumours, normal tissues, sera and other body fluids has been further tested. The alpha-protein was identified by immunological methods as alpha1-antichymotrypsin. Experiments by crossed immunoelectrophoresis showed that this protein cross-reacts with the betaE-protein found in the PCA extracts. The betaE-protein shows heterogeneity in molecular size, electrophoretic mobility and it has been demonstrated that it shares antigenic determinants with the CEA or betaI-molecule. Cross-reaction between betaE and other glycoproteins found in the PCA extract of normal or malignant tissue or serum was not detected.

Topics: Adenocarcinoma; Carcinoembryonic Antigen; Chromatography, Gel; Chymotrypsin; Colonic Neoplasms; Cross Reactions; Epitopes; Humans; Immune Sera; Immunoelectrophoresis; Neoplasm Proteins; Perchlorates

Topics: Adenocarcinoma; Adenosine Triphosphatases; Alkaline Phosphatase; Carboxypeptidases; Carcinoembryonic Antigen; Chymotrypsin; Colonic Neoplasms; Cystinyl Aminopeptidase; Esterases; Glucuronidase; Humans; Liver Neoplasms; Neoplasm Metastasis; Sulfatases

Topics: Adenocarcinoma; Animals; Bees; Chymotrypsin; Cytoplasmic Granules; Dextrans; Heparin; Histamine Release; Mast Cells; Microscopy, Electron; Neoplasm Transplantation; Neoplasms, Experimental; Polyomavirus; Rats; Salivary Gland Neoplasms; Venoms

Topics: Adenocarcinoma; Animals; Bees; Cell Differentiation; Chymotrypsin; Cytoplasmic Granules; Dextrans; Female; Glycosaminoglycans; Heparin; Histamine; Histocytochemistry; Male; Mast Cells; Microscopy, Electron; Neoplasm Transplantation; Neoplasms, Experimental; Polyomavirus; Rats; Salivary Gland Neoplasms; Serotonin; Submandibular Gland; Venoms

Topics: Adenocarcinoma; Animals; Chymotrypsin; Hyaluronoglucosaminidase; Mammary Neoplasms, Experimental; Mice; Neoplasm Transplantation; Transplantation Immunology; Transplantation, Homologous

Topics: Achlorhydria; Adenocarcinoma; Anemia; Anemia, Pernicious; Chymotrypsin; Cytodiagnosis; Gastric Acidity Determination; Gastroscopy; Geriatrics; Humans; Mass Screening; Neoplasm Metastasis; Radiography; Stomach Neoplasms; Surgical Procedures, Operative