Abstract
The structures of calcium‐activated neutral protease (CANP) and its endogenous inhibitor elucidated recently have revealed novel features with respect to their structure‐function relationship and enzyme activity regulation. The protease is regarded as a proenzyme which can be activated at the cell membrane in the presence of Ca2+ and phospholipid, and presumably regulates the functions of proteins, especially membrane‐associated proteins, by limited proteolysis. Protein kinase C is hydrolysed and activated by CANP at the cell membrane to a cofactor‐independent form. These results are reviewed and the possible involvement of CANP in signal transduction is discussed.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:57 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 11:07 p.m.) |
Indexed | 1 month, 3 weeks ago (July 11, 2025, 6:22 a.m.) |
Issued | 38 years ago (Aug. 17, 1987) |
Published | 38 years ago (Aug. 17, 1987) |
Published Online | 23 years, 10 months ago (Oct. 19, 2001) |
Published Print | 38 years ago (Aug. 17, 1987) |
@article{Suzuki_1987, title={Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function}, volume={220}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(87)80828-1}, DOI={10.1016/0014-5793(87)80828-1}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Suzuki, Koichi and Imajoh, Shinobu and Emori, Yasufumi and Kawasaki, Hiroshi and Minami, Yasufumi and Ohno, Shigeo}, year={1987}, month=aug, pages={271–277} }