Document Detail


N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease.
MedLine Citation:
PMID:  11567025     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Epithin was originally identified as a mouse type II membrane serine protease. Its human orthologue membrane type-serine protease 1 (MT-SP1)/matriptase has been reported to be localized on the plasma membrane. In addition, soluble forms of matriptase were isolated from human breast milk and breast cancer cell-conditioned medium. In this paper, we report a processing mechanism that appears to be required for the release of epithin. CHO-K1 or COS7 cells transfected with single full-length epithin cDNA generated two different-sized proteins in cell lysates, 110 and 92 kDa. The 92-kDa epithin was found to be an N-terminally truncated form of the 110-kDa epithin, and it was the only form detected in the culture medium. The 92-kDa epithin was also found on the cell surface, where it was anchored by the N-terminal fragment. The results of in vivo cell labeling experiments indicate that the 110-kDa epithin is rapidly processed to the 92-kDa epithin. Using site-directed mutagenesis experiments, we identified Gly(149) of the GSVIA sequence in epithin as required for the processing and release of the protein. These results suggest that N-terminal processing of epithin at Gly(149) is a necessary prerequisite step for release of the protein.
Authors:
E G Cho; M G Kim; C Kim; S R Kim; I S Seong; C Chung; R H Schwartz; D Park
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2001-09-20
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  276     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-23     Completed Date:  2002-01-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  44581-9     Citation Subset:  IM    
Affiliation:
School of Biological Sciences, Seoul National University, Seoul 151-742, Republic of Korea.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biotinylation
CHO Cells
COS Cells
Cell Membrane / enzymology*
Cricetinae
Culture Media, Conditioned / pharmacology
DNA, Complementary / metabolism
Drosophila
Endopeptidases / metabolism
Glutathione Transferase / metabolism
Glycine / chemistry
Mice
Mutagenesis, Site-Directed
Precipitin Tests
Protein Binding
Protein Biosynthesis
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Fusion Proteins / metabolism
Serine Endopeptidases / chemistry*,  metabolism*
Trypsin / metabolism,  pharmacology
Chemical
Reg. No./Substance:
0/Culture Media, Conditioned; 0/DNA, Complementary; 0/Recombinant Fusion Proteins; 56-40-6/Glycine; EC 2.5.1.18/Glutathione Transferase; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.-/St14 protein, mouse; EC 3.4.21.-/matriptase; EC 3.4.21.4/Trypsin

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


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