Prostasin is a glycosylphosphatidylinositol-anchored active serine protease
Abbreviated Journal Title
J. Biol. Chem.
HUMAN GLANDULAR KALLIKREIN; HUMAN TISSUE KALLIKREIN; ENDOPLASMIC-RETICULUM; MOLECULAR-CLONING; NUCLEAR-ENVELOPE; SODIUM-CHANNEL; ANTIGEN; PROTEINASE; ALPHA-1-ANTITRYPSIN; PURIFICATION; Biochemistry & Molecular Biology
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 of Biological Chemistry
"Prostasin is a glycosylphosphatidylinositol-anchored active serine protease" (2001). Faculty Bibliography 2000s. 7935.