title: The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma.
abstract: OBJECTIVE
  The invasion and metastasis of carcinoma cells require the proteolytic degradation of the extracellular matrix by various cell surface proteases. Among these, seprase is a type II transmembrane serine protease absent in normal tissues and it has been implicated in the invasion of the extracellular matrix by both tumor and stromal cells in human breast carcinoma and melanoma. In the present study, the expression of seprase mRNA, protein and its gelatin-degrading activity in human gastric carcinoma were examined to substantiate the potential role of seprase in gastric carcinoma invasion.
  
  
  METHODS
  We have examined the seprase expression in human gastric carcinoma (n = 34) by RT-PCR, Western immunoblotting analysis, immunohistochemistry, and gelatin zymography.
  
  
  RESULTS
  Immunoblotting analysis using mAb D8 directed against seprase showed that the carcinoma tissues in 26 out of 34 cases of gastric cancer expressed a dimeric form of seprase but their normal counterparts did not. Gelatin zymography confirmed that the isolated seprase exhibited the gelatin-degrading activity and was active. Seprase-expressing carcinoma tissues were more often found in the scirrhous type than in other types of gastric carcinoma. RT-PCR analysis showed that seprase mRNA was present in carcinoma tissues but not in normal tissues. Immunohistochemically, seprase was mainly located in gastric carcinoma cells, weakly in stromal cells and microvessel endothelial cells in the tumor nest, and none in normal cells.
  
  
  CONCLUSIONS
  Our studies showed the unique expression and localization of seprase in the tumor and stromal cells within human gastric carcinoma but not in normal tissues, suggesting a role of seprase in the invasive and metastatic progression of gastric carcinoma.
authors.affiliation: Department of Pathology, School of Medicine, Faculty of Medicine, University of Yamanashi, Yamanashi, Japan. yoshim@ka3.so-net.ne.jp
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Mori
authors.forename: Koji
authors.initials: K
authors.lastname: Kono
authors.forename: Yoshirou
authors.initials: Y
authors.lastname: Matsumoto
authors.forename: Hideki
authors.initials: H
authors.lastname: Fujii
authors.forename: Tetsu
authors.initials: T
authors.lastname: Yamane
authors.forename: Masako
authors.initials: M
authors.lastname: Mitsumata
authors.forename: Wen-Tien
authors.initials: WT
authors.lastname: Chen
mesh_terms: D014408:Biomarkers, Tumor / Q000032:analysis / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D015153:Blotting, Western; D002277:Carcinoma / Q000201:enzymology* / Q000473:pathology; D010450:Endopeptidases; D018093:Gelatinases / Q000032:analysis / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D007150:Immunohistochemistry; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D009361:Neoplasm Invasiveness; D012333:RNA, Messenger / Q000032:analysis; D012334:RNA, Neoplasm / Q000032:analysis; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012697:Serine Endopeptidases / Q000032:analysis / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D013274:Stomach Neoplasms / Q000201:enzymology* / Q000473:pathology; D000099167:Fibroblast Activation Protein Alpha
chemical_list: D014408:Biomarkers, Tumor; D010450:Endopeptidases; D018093:Gelatinases; D008565:Membrane Proteins; D012333:RNA, Messenger; D012334:RNA, Neoplasm; D012697:Serine Endopeptidases; D000099167:Fibroblast Activation Protein Alpha