The Structural Requirements of Matriptase in Its Ectodomain Release in Polarized Epithelial Cells

Abstract

Matriptase is a type-II transmembrane serine protease abundantly expressed in polarized epithelia. The ectodomain of matriptase is released from the cell surface. In the present study, we found that the post-translational cleavage between Gly149 and Ser150 and the existence of catalytic domain are critical for the ectodomain release of matriptase in stable transfection experiments using the polarized Madin–Darby canine kidney epithelial cell line.

• catalytic domain
• ectodomain release
• matriptase
• post-translational cleavage
• simple epithelial cells