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The structural requirements of matriptase in its ectodomain release in polarized epithelial cells.
- Source :
-
Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2010; Vol. 74 (6), pp. 1295-7. Date of Electronic Publication: 2010 Jun 07. - Publication Year :
- 2010
-
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.
- Subjects :
- Animals
Blotting, Western
Cell Line
Dogs
Epithelial Cells enzymology
Humans
Mice
Protein Processing, Post-Translational
Protein Structure, Tertiary
Serine Endopeptidases genetics
Cell Polarity
Epithelial Cells cytology
Epithelial Cells metabolism
Serine Endopeptidases chemistry
Serine Endopeptidases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1347-6947
- Volume :
- 74
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Bioscience, biotechnology, and biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 20530886
- Full Text :
- https://doi.org/10.1271/bbb.100074