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rdf:type |
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lifeskim:mentions |
umls-concept:C0030685,
umls-concept:C0205224,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C0769218,
umls-concept:C1283071,
umls-concept:C1366520,
umls-concept:C1420785,
umls-concept:C1522424,
umls-concept:C1709694,
umls-concept:C1963578
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pubmed:issue |
48
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pubmed:dateCreated |
2001-11-23
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/St14 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/matriptase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44581-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11567025-Animals,
pubmed-meshheading:11567025-Biotinylation,
pubmed-meshheading:11567025-CHO Cells,
pubmed-meshheading:11567025-COS Cells,
pubmed-meshheading:11567025-Cell Membrane,
pubmed-meshheading:11567025-Cricetinae,
pubmed-meshheading:11567025-Culture Media, Conditioned,
pubmed-meshheading:11567025-DNA, Complementary,
pubmed-meshheading:11567025-Drosophila,
pubmed-meshheading:11567025-Endopeptidases,
pubmed-meshheading:11567025-Glutathione Transferase,
pubmed-meshheading:11567025-Glycine,
pubmed-meshheading:11567025-Mice,
pubmed-meshheading:11567025-Mutagenesis, Site-Directed,
pubmed-meshheading:11567025-Precipitin Tests,
pubmed-meshheading:11567025-Protein Binding,
pubmed-meshheading:11567025-Protein Biosynthesis,
pubmed-meshheading:11567025-Protein Structure, Secondary,
pubmed-meshheading:11567025-Protein Structure, Tertiary,
pubmed-meshheading:11567025-Recombinant Fusion Proteins,
pubmed-meshheading:11567025-Serine Endopeptidases,
pubmed-meshheading:11567025-Trypsin
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pubmed:year |
2001
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pubmed:articleTitle |
N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease.
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pubmed:affiliation |
School of Biological Sciences, Seoul National University, Seoul 151-742, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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