concanavalin-a and Mouth-Neoplasms

The prevalence of oral squamous cell carcinoma (OSCC) is high in South and Southeast Asia regions. Most OSCC patients are detected at advanced stages low 5-year survival rates. Aberrant expression of glycosylated proteins was found to be associated with malignant transformation and cancer progression. Hence, identification of cancer-associated glycoproteins could be used as potential biomarkers that are beneficial for diagnosis or clinical management of patients. This study aims to identify the differentially expressed glycoproteins using lectin-based glycoproteomics approaches. Serum samples of 40 patients with OSCC, 10 patients with oral potentially malignant disorder (OPMD), and 10 healthy individuals as control group were subjected to two-dimensional gel electrophoresis (2-DE) coupled with lectin Concanavalin A and Jacalin that specifically bind to N- and O-glycosylated proteins, respectively. Five differentially expressed N- and O-glycoproteins with various potential glycosylation sites were identified, namely N-glycosylated α1-antitrypsin (AAT), α2-HS-glycoprotein (AHSG), apolipoprotein A-I (APOA1), and haptoglobin (HP); as well as O-glycosylated AHSG and clusterin (CLU). Among them, AAT and APOA1 were further validated using enzyme-linked immunosorbent assay (ELISA) (n = 120). It was found that AAT and APOA1 are significantly upregulated in OSCC and these glycoproteins are independent risk factors of OSCC. The clinical utility of AAT and APOA1 as potential biomarkers of OSCC is needed for further evaluation.

Topics: Adult; Aged; alpha 1-Antitrypsin; Apolipoprotein A-I; Biomarkers, Tumor; Carcinoma, Squamous Cell; Case-Control Studies; Chromatography, Affinity; Chromatography, Agarose; Concanavalin A; Enzyme-Linked Immunosorbent Assay; Female; Glycoproteins; Glycosylation; Humans; Male; Mass Spectrometry; Middle Aged; Mouth Neoplasms; Plant Lectins; Precancerous Conditions; Squamous Cell Carcinoma of Head and Neck

A new cell line (CoMS) was established from a 3-year-old male mongrel dog with mast cell tumor of the oral mucosa. CoMS cells grow in suspension with a doubling time of 27.0 +/- 0.7 hr. The cytoplasmic granules were formalin-sensitive, showed diverse appearances in their ultrastructural findings and contained heparin proteoglycan and neutral protease chymase. Calcium ionophore A23187, substance P and concanavalin A caused significant histamine release from CoMS cells, while compound 48/80 failed to release histamine. This cell line will make an available source for studies on canine mast cell tumors.

Topics: Animals; Antibodies, Anti-Idiotypic; Calcimycin; Cell Division; Concanavalin A; Dog Diseases; Dogs; Histamine; Histocytochemistry; Ionophores; Male; Mastocytosis; Microscopy, Electron; Mouth Neoplasms; p-Methoxy-N-methylphenethylamine; Substance P; Tumor Cells, Cultured

To investigate the mechanism whereby serum dipeptidyl peptidase (DPP) IV activity in oral cancer patients is decreased, we examined the expression of cell surface DPP IV, also known as CD26, in cultured peripheral blood T lymphocytes of these patients and the amounts of DPP IV released into culture medium; values were compared with those found in healthy subjects. When peripheral blood T lymphocytes were cultured in the presence of phytohemagglutinin, concanavalin A and/or interleukin-2, the proliferative response and expression of CD26 (DPP IV) in their plasma membranes were greatly diminished in oral cancer patients as compared with those in healthy subjects. In addition, DPP IV activity in lymphocyte culture medium was reduced more in oral cancer patients than in healthy subjects, indicating decreased shedding of DPP IV from activated T lymphocytes in the patients. Based on these findings, it is suggested that suppression of DPP IV expression in peripheral blood T lymphocytes is one of the important factors involved in the mechanism of decrease of serum DPP IV activity in oral cancer patients.

Topics: Adult; Aged; Aged, 80 and over; Antigens, Surface; Blotting, Western; Cell Division; Cell Membrane; Cells, Cultured; Concanavalin A; Culture Media, Conditioned; Dipeptidyl Peptidase 4; Female; Fluorescent Antibody Technique, Direct; Gene Expression Regulation, Neoplastic; Humans; Interleukin-2; Lymphocyte Activation; Male; Middle Aged; Mitogens; Mouth Mucosa; Mouth Neoplasms; Phytohemagglutinins; T-Lymphocytes

The in vitro responsiveness of peripheral blood mononuclear cells (PBMC) T lymphocytes was studied in 81 patients with limited or extended head and neck squamous cell carcinoma (HNSCC), as judged by T, N and T + N stages. Patients included in the study were males below 80 years of age, without auto-immune disease or cachexia, who were not taking any immuno-active medication at the time of diagnosis. The patients were divided into groups according to TNM stage T0-2 vs T3-4, N0-1 vs N2-3 or T + N0-3 vs T + N4-7. When cells from patients with early and late stage, according to T, N or T + N stage, were compared, we found a decreased level of mitogen stimulated T-cells and decreased spontaneous proliferation with increasing disease stage. The same was true if the in vitro mitogenesis of T-cells was analysed separately, depending on the laryngeal or oral cavity/pharyngeal origin of the patients' tumours. If the patients were divided into two groups based on N stage, decreased gamma-interferon, and to some extent interleukin (IL-2), but not IL-4 levels, were found to be related to the disease stage.

Topics: Aged; Analysis of Variance; Carcinoma, Squamous Cell; Cell Division; Concanavalin A; Head and Neck Neoplasms; Humans; Interferon-gamma; Interleukin-2; Interleukin-4; Laryngeal Neoplasms; Lymphocyte Activation; Male; Mitogens; Mouth Neoplasms; Multivariate Analysis; Neoplasm Staging; Pharyngeal Neoplasms; T-Lymphocytes

The binding pattern of two lectins, concanavalin A (ConA) and peanut agglutin (PNA), in various phases of tumour progression in the oral epithelium was studied. These included non-dysplastic, dysplastic and neoplastic lesions as well as normal tissue. ConA and PNA showed intense staining in the basement membrane of all types of lesions. Little difference was observed in the staining patterns between different stages of oral carcinogenesis, either with ConA or PNA. ConA showed mild cytoplasmic and membrane staining in all types of lesions while PNA showed moderate to intense staining in both the cytoplasm and membrane of lower-layer cells in all histological groups. The present study therefore shows that these lectins have limited value in the elucidation of oral carcinogenesis and are of insignificant diagnostic value.

Topics: Carcinoma; Carcinoma, Papillary; Carcinoma, Squamous Cell; Cell Transformation, Neoplastic; Concanavalin A; Glycoconjugates; Humans; Lectins; Leukoplakia, Oral; Mouth Mucosa; Mouth Neoplasms; Neoplasm Proteins; Peanut Agglutinin; Protein Binding

The distribution pattern of certain monosaccharides in the epithelial cells of the hamster buccal pouch was studied during carcinoma development induced by 9,10-dimethyl-1,2-benzathrancene (DMBA). An avidin-biotin-peroxidase complex (ABC) immunohistochemical technique with high affinity biotinylated lectins was employed to identify monosaccharides. Lectins used in this experiment included Concanavalin A (Con A), for identifying mannose or glucose, Ricinus communis agglutinin I(RCA-I), for identifying galactose, and Ulex europaeus agglutinin I(UEA-I), for identifying fucose. The results show that in normal buccal pouch epithelial cells, fuctose or galactose were concentrated predominantly on the cellular membrane, while mannose and glucose were distributed in the cytoplasm. In the epithelial cells undergoing neoplastic transformation induced by DMBA, most cells showed decreased staining of the above-mentioned monosaccharides, while in other areas the cells were heavily stained. However, the most striking change which occurred was that galactose and fucose shifted from the cellular membrane to the intracytoplasmic area during the malignant transformation. Thus, the changes of anatomic location and intensity of staining of monosaccharides in the buccal pouch epithelium may be used as a criteria for early histochemical diagnosis of malignant transformation.

Topics: 9,10-Dimethyl-1,2-benzanthracene; Animals; Carcinoma, Squamous Cell; Concanavalin A; Cricetinae; Epithelium; Immunoenzyme Techniques; Immunohistochemistry; Lectins; Male; Mouth Mucosa; Mouth Neoplasms; Plant Lectins; Receptors, Mitogen

Kupffer cells from the liver of normal rats were checked for their natural cytostatic capabilities using an in vitro target cell growth inhibition assay. A strong cytostatic effect was observed on an human tumor cell line and was shown to be exerted on various transformed or normal target cells with only small differences in their susceptibility. The inhibition of target cell proliferation was shown to depend on the effector/target cell ratio. Different experimental data suggest that an intimate membranal contact between Kupffer cells and target cells is required.

Topics: Animals; Carcinoma; Carcinoma, Squamous Cell; Cell Cycle; Cell Line; Cells, Cultured; Chick Embryo; Concanavalin A; DNA Replication; Embryo, Mammalian; Fibroblasts; Humans; Kupffer Cells; Liver; Mouth Neoplasms; Rats; Rats, Inbred Strains; Ultraviolet Rays

A variety of epithelial cells and fibroblasts fail to move over one another's upper surfaces in culture, resulting in monolayering. The failure of seeded fibroblasts to adhere to and spread on epithelial cell surfaces suggests that monolayering in culture is due to the lack of adhesion of the upper cell surface, at least of epithelial cells. Seeded fibroblasts and postmitotic, rounded fibroblasts likewise fail to spread on the upper surfaces of spread fibroblasts, suggesting that the inability of the upper cell surface to support spreading may be a general phenomenon. Inert particles and cell processes do not adhere directly to the upper cell surface. However, they can initiate adhesions to the surface at a cell's free margin, suggesting a variation of adhesive properties over a cell's surface.

Topics: Animals; Carcinoma; Cell Adhesion; Cell Aggregation; Cell Division; Cell Line; Cell Membrane; Cell Movement; Concanavalin A; Cornea; Epithelial Cells; Epithelium; Erythrocytes; Fibroblasts; Gizzard, Non-avian; Humans; Latex; Microscopy, Phase-Contrast; Microspheres; Mitosis; Motion Pictures; Mouth Neoplasms; Sarcoma; Skin; Time Factors

Topics: Agglutination; Animals; Carcinoma; Carcinoma, Squamous Cell; Cell Line; Cell Transformation, Neoplastic; Concanavalin A; Cricetinae; Fibroblasts; HeLa Cells; Humans; Kidney; Laryngeal Neoplasms; Lectins; Lung; Mice; Mouth Neoplasms; Neoplasms, Experimental; Trypsin