N-terminal Processing Is Essential for Release of Epithin, a Mouse Type II Membrane Serine Protease

Eun Gyung Cho, Moon Gyo Kim, Chungho Kim, Seung Ryul Kim, Ihn Sik Seong, Chinha Chung, Ronald H. Schwartz, Dongeun Park

Research output: Contribution to journalArticle

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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 Gly149 of the GSVIA sequence in epithin as required for the processing and release of the protein. These results suggest that N-terminal proeessing processing of epithin at Gly 149 is a necessary prerequisite step for release of the protein.

Original languageEnglish
Pages (from-to)44581-44589
Number of pages9
JournalJournal of Biological Chemistry
Volume276
Issue number48
DOIs
Publication statusPublished - 2001 Nov 30
Externally publishedYes

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Serine Proteases
Membranes
Processing
Human Milk
Mutagenesis
Proteins
Cell membranes
Conditioned Culture Medium
Labeling
Culture Media
Complementary DNA
Experiments
Cells
Site-Directed Mutagenesis
Cell Membrane
Breast Neoplasms
matriptase

ASJC Scopus subject areas

  • Biochemistry

Cite this

N-terminal Processing Is Essential for Release of Epithin, a Mouse Type II Membrane Serine Protease. / Cho, Eun Gyung; Kim, Moon Gyo; Kim, Chungho; Kim, Seung Ryul; Seong, Ihn Sik; Chung, Chinha; Schwartz, Ronald H.; Park, Dongeun.

In: Journal of Biological Chemistry, Vol. 276, No. 48, 30.11.2001, p. 44581-44589.

Research output: Contribution to journalArticle

Cho, EG, Kim, MG, Kim, C, Kim, SR, Seong, IS, Chung, C, Schwartz, RH & Park, D 2001, 'N-terminal Processing Is Essential for Release of Epithin, a Mouse Type II Membrane Serine Protease', Journal of Biological Chemistry, vol. 276, no. 48, pp. 44581-44589. https://doi.org/10.1074/jbc.M107059200
Cho, Eun Gyung ; Kim, Moon Gyo ; Kim, Chungho ; Kim, Seung Ryul ; Seong, Ihn Sik ; Chung, Chinha ; Schwartz, Ronald H. ; Park, Dongeun. / N-terminal Processing Is Essential for Release of Epithin, a Mouse Type II Membrane Serine Protease. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 48. pp. 44581-44589.
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