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DISTINCT KINETICS OF SUBUNIT AUTOLYSIS IN MAMMALIAN M-CALPAIN ACTIVATION
Author(s): SAIDO TC, NAGAO S, SHIRAMINE M, TSUKAGUCHI M, YOSHIZAWA T, SORIMACHI H, ITO H, TSUCHIYA T, KAWASHIMA S, SUZUKI K
Source: FEBS LETTERS    Volume: 346    Issue: 2-3    Pages: 263-267    Published: JUN 13 1994  
Times Cited: 47     References: 18     
Abstract: Subunit autolysis of mammalian m-calpain upon activation was examined in kinetic terms using a set of antibodies recognizing different portions of the protease. Activation of m-calpain by calcium resulted in no apparent autolysis in the large catalytic subunit, whereas the small regulatory subunit underwent immediate autolysis followed by substrate proteolysis. This profile of subunit autolysis is distinct from that of the other ubiquitous isozyme, mu-calpain, in which autolysis of the large subunit and then of the small subunit precedes substrate proteolysis under the normal conditions. The activation state of m-calpain thus is not reflected by the large subunit autolysis. The mode and role of autolysis may vary among calpain isozymes.
Document Type: Article
Language: English
Reprint Address: SAIDO, TC (reprint author), TOKYO METROPOLITAN INST MED SCI, DEPT MOLEC BIOL, BUNKYO KU, 3-18-22 HONKOMAGOME, TOKYO 113, JAPAN
Addresses:
1. SOPHIA UNIV, FAC SCI & TECHNOL, DEPT CHEM, CHIYODA KU, TOKYO 102, JAPAN
2. AOYAMA GAKUIN UNIV, COLL SCI & ENGN, DEPT CHEM, SETAGAYA KU, TOKYO 157, JAPAN
3. UNIV TOKYO, INST MOLEC & CELLULAR BIOSCI, BUNKYO KU, TOKYO 113, JAPAN
Publisher: ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology
IDS Number: NR569
ISSN: 0014-5793
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