The structural requirements of matriptase in its ectodomain release in polarized epithelial cells.
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.
Tsuzuki
Satoshi
S
Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan. tkmone@kais.kyoto-u.ac.jp
Murai
Nobuhito
N
Miyake
Yuka
Y
Inouye
Kuniyo
K
Fushiki
Tohru
T
D000818:Animals; D015153:Blotting, Western; D002460:Cell Line; D016764:Cell Polarity; D004285:Dogs; D004847:Epithelial Cells / Q000166:cytology* / Q000201:enzymology / Q000378:metabolism*; D006801:Humans; D051379:Mice; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D012697:Serine Endopeptidases; C485595:matriptase