alpha-chymotrypsin has been researched along with Salivary-Gland-Neoplasms* in 5 studies
5 other study(ies) available for alpha-chymotrypsin and Salivary-Gland-Neoplasms
Article | Year |
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The 3rd Salivary Gland Tumor Workshop meeting report.
Topics: Carcinoma; Chymotrypsin; DNA-Binding Proteins; Gene Fusion; Genes, myb; HMGA2 Protein; Humans; NFI Transcription Factors; Nuclear Proteins; Protein-Tyrosine Kinases; Salivary Gland Neoplasms; Trans-Activators; Transcription Factors | 2013 |
Expression of pancreatic digestive enzymes in normal and pathologic epithelial cells of the human gastrointestinal system.
Pancreatic digestive enzymes have rarely been reported in human nonpancreatic organs. We examined their expression in the epithelial cells of the nonpancreatic gastrointestinal organs, looking for pancreatic alpha-amylase, trypsin, chymotrypsin and pancreatic lipase. Western blotting, enzyme assay and pancreatic alpha-amylase mRNA were also used in selected specimens. In normal tissues, immunoreactivity of one or more of these enzymes was frequently noted in cells of the salivary glands, stomach, duodenum, large pancreatic ducts, extrahepatic bile ducts and gall bladder. The epithelium of the normal oesophagus, small intestine and colon were consistently negative for these enzymes. In pathologic tissues, immunoreactivity for one or more enzymes was present in epithelial cells of pleomorphic adenomas of the salivary glands, oesophageal squamous cell carcinoma, gastric adenoma and adenocarcinoma, pancreatic adenocarcinoma, cholecystitis, adenocarcinoma of the gall bladder and extrahepatic bile duct, and colon adenoma and adenocarcinoma. Western blotting showed a specific band of each enzyme in some specimens of normal stomach. In situ hybridization for pancreatic alpha-amylase mRNA showed specific signals in the normal stomach, but not in the normal colon. Reverse transcriptase polymerase chain reaction analysis for pancreatic alpha-amylase mRNA revealed specific signals in the normal stomach. Enzyme assay revealed that the stomach and gall bladder showed these activities. The data suggest that pancreatic digestive enzymes are produced by several epithelial cell types of the nonpancreatic gastrointestinal organs, that the organs positive for pancreatic enzyme have a common cell lineage, and that neoplasms continue to express or neoexpress these enzymes after neoplastic transformation. Topics: Adult; Aged; alpha-Amylases; Blotting, Western; Chymotrypsin; Digestive System; Digestive System Diseases; Digestive System Neoplasms; Epithelium; Female; Humans; Hydrolases; Immunohistochemistry; In Situ Hybridization; Lipase; Male; Middle Aged; Salivary Gland Neoplasms; Salivary Glands; Trypsin | 1997 |
Immunohistochemical localization of alpha 1-antitrypsin and alpha 1-antichymotrypsin in salivary pleomorphic adenomas.
Immunohistochemical identification of alpha 1-antitrypsin (alpha 1-AT) and alpha 1-antichymotrypsin (alpha 1-ACh) in pleomorphic adenomas of salivary glands is reported in order to compare their distribution profiles with those of lysozyme and lactoferrin, already described elsewhere. Normal salivary glands indicated positive alpha 1-AT staining in ductal segments and had no alpha 1-ACh in any glandular cell. Pleomorphic adenomas displayed moderate positivity to alpha 1-AT staining in duct-like, tubular and glandular epithelia which was particularly intense in luminal cells. The limited number of tumour cells which showed duct-like structures with a single cellular layer arrangement, displayed the highest staining to alpha 1-ACh. Strongly alpha 1-AT positive tumour cells located on the inner side of luminal cavities were also markedly positive to alpha 1-ACh. Spindle shaped tumour cells existed outside tubular and ductal structures and were negative to alpha 1-AT and alpha 1-ACh. Distribution of alpha 1-AT in salivary glands was similar to that of lysozyme as is usual in ductal segments or their transformed cells, and occurrence of alpha 1-ACh localization rather resembled that of lactoferrin, with occurrence in acinar compartments and changed epithelia within acini. The biological role of a specific immunohistochemical distribution of alpha 1-AT and alpha 1-ACh in pleomorphic adenomas may be associated with a self regulating mechanism which inhibits degradation by tissue proteinases. Topics: Adenoma, Pleomorphic; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Chymotrypsin; Histocytochemistry; Humans; Immunochemistry; Lymphadenitis; Salivary Gland Neoplasms; Salivary Glands; Submandibular Gland | 1985 |
[Electron microscope and experimental investigations on degranulation in tissue mast cells].
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 | 1969 |
[Stromal mastocytosis of viral-induced transplantable adenocarcinomas of the rat].
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 | 1969 |