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| N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease |
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| Author(s): Cho EG, Kim MG, Kim C, Kim SR, Seong IS, Chung CH, Schwartz RH, Park D |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 276 Issue: 48 Pages: 44581-44589 Published: NOV 30 2001 |
| Times Cited: 32 References: 22 |
| Abstract: 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 Gly149 is a necessary prerequisite step for release of the protein. |
| Document Type: Article |
| Language: English |
| Reprint Address: Park, D (reprint author), Seoul Natl Univ, Sch Biol Sci, Seoul 151742, South Korea |
Addresses:
1. Seoul Natl Univ, Sch Biol Sci, Seoul 151742, South Korea
2. NIAID, Cellular & Mol Immunol Lab, NIH, Bethesda, MD 20892 USA
3. Chungbuk Natl Univ, Coll Med, Cheongju 361763, South Korea |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: 496QD |
| ISSN: 0021-9258 |
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