A novel aspect of calpain activation.

Abstract

Calpain, a Ca2+-dependent biomodulator, alters the properties of substrate proteins by cleaving them at a limited number of specific sites. Recent studies of the structure-function relationship of calpain and X-ray analysis of its Ca2+-binding domain have revealed hitherto unknown features of the regulation of calpain activity. A novel dissociation/autolysis mechanism for the activation of calpain at the membrane is proposed, which incorporates recent findings from structure-function studies of calpain, and its implications are discussed.

• Authors: K Suzuki, H Sorimachi
• Journal: FEBS letters (FEBS Lett) Vol. 433 Issue 1-2 Pg. 1-4 (Aug 14 1998) ISSN: 0014-5793 [Print] England
• PMID: 9738920 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Calpain
• Calcium

Topics

• Animals
• Binding Sites
• Calcium (metabolism, pharmacology)
• Calpain (chemistry, metabolism)
• Enzyme Activation
• Humans
• Structure-Activity Relationship