Title

Prostasin is a glycosylphosphatidylinositol-anchored active serine protease

Authors

Authors

L. M. Chen; M. L. Skinner; S. W. Kauffman; J. Chao; L. Chao; C. D. Thaler;K. X. Chai

Comments

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Abbreviated Journal Title

J. Biol. Chem.

Keywords

HUMAN GLANDULAR KALLIKREIN; HUMAN TISSUE KALLIKREIN; ENDOPLASMIC-RETICULUM; MOLECULAR-CLONING; NUCLEAR-ENVELOPE; SODIUM-CHANNEL; ANTIGEN; PROTEINASE; ALPHA-1-ANTITRYPSIN; PURIFICATION; Biochemistry & Molecular Biology

Abstract

A recombinant human prostasin serine protease was expressed in several human cell lines. Subcellular fractionation showed that this serine protease is synthesized as a membrane-bound protein while a free-form prostasin is secreted into the culture medium, Prostasin was identified in nuclear and membrane fractions. Membrane-bound prostasin can be released by phosphatidylinositol-specific phospholipase C treatment, or labeled by [H-3]ethanolamine, indicating a glycosylphosphatidylinositol anchorage. A prostasin-binding protein was identified in mouse and human seminal vesicle fluid. Both the secreted and the membrane-bound prostasin were able to form a covalently linked 82-kDa complex when incubated with seminal vesicle fluid. The complex formation between prostasin and the prostasin-binding protein was inhibited by a prostasin antibody, heparin, and serine protease inhibitors. Prostasin's serine protease activity was inhibited when bound to the prostasin-binding protein in mouse seminal vesicle fluid. This study indicates that prostasin is an active serine protease in its membrane-bound form.

Journal Title

Journal of Biological Chemistry

Volume

276

Issue/Number

24

Publication Date

1-1-2001

Document Type

Article

Language

English

First Page

21434

Last Page

21442

WOS Identifier

WOS:000169297900086

ISSN

0021-9258

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