Document Detail


Multiple secretion of matrix serine proteinases by human gastric carcinoma cell lines.
MedLine Citation:
PMID:  1387587     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proteinase species secreted by 10 human gastric carcinoma cell lines were analyzed by gelatin zymography and immunoblotting. These cell lines were classified into the following three groups with respect to proteinase secretion: cell lines secreting mainly gelatinases A and/or B; those secreting multiple types of serine proteinases; and those scarcely secreting these enzymes. Two cell lines of the second group, STKM-1 and MKN28, hardly secreted metalloproteinases but secreted the following four types of serine proteinases: (a) two trypsin-like enzymes (M(r) 26,000 and 24,000 in proenzyme forms); (b) a tissue kallikrein-like enzyme (M(r) 150,000 in a complex form); (c) a plasmin-like enzyme (M(r) 70,000); and (d) a plasminogen activator (urokinase-type, M(r) 57,000, from STKM-1 and tissue-type, M(r) 70,000, from MKN28). The M(r) 70,000 plasmin-like enzyme was also detected at lower levels in the conditioned media of four other cell lines (MKN1, MKN45, NUGC-3, and KATO III). The M(r) 24,000 proenzyme of the trypsin-like enzyme was purified from the serum-free conditioned medium of STKM-1. The proenzyme was activated by enterokinase treatment or autolytically by incubation at neutral pH, decreasing its apparent molecular weight from 24,000 to 23,000 on nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The activated enzyme extensively degraded fibronectin, laminin, and gelatins and to lesser extents type I, III, IV, and V collagens at 30 degrees C. These results suggest that the matrix serine proteinases may play a major role in the matrix degradation by some kinds of human cancer cells.
Authors:
N Koshikawa; H Yasumitsu; M Umeda; K Miyazaki
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cancer research     Volume:  52     ISSN:  0008-5472     ISO Abbreviation:  Cancer Res.     Publication Date:  1992 Sep 
Date Detail:
Created Date:  1992-10-08     Completed Date:  1992-10-08     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2984705R     Medline TA:  Cancer Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5046-53     Citation Subset:  IM    
Affiliation:
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Blotting, Western
Calcium / metabolism
Carcinoma / enzymology*
Fibrinolysin / metabolism
Humans
Kallikreins / metabolism
Molecular Weight
Plasminogen Activators / metabolism
Serine Endopeptidases / chemistry,  secretion*
Stomach Neoplasms / enzymology*
Substrate Specificity
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
7440-70-2/Calcium; EC 3.4.21.-/Kallikreins; EC 3.4.21.-/Plasminogen Activators; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.7/Fibrinolysin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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