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Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function
Author(s) -
Suzuki Koichi,
Imajoh Shinobu,
Emori Yasufumi,
Kawasaki Hiroshi,
Minami Yasufumi,
Ohno Shigeo
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80828-1
Subject(s) - proteolysis , protease , biochemistry , chemistry , membrane , enzyme , endogeny , microbiology and biotechnology , cell membrane , calcium , phospholipid , signal transduction , biology , organic chemistry
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 Ca 2+ 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.