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Distinct kinetics of subunit autolysis in mammalian m‐calpain activation
Author(s) -
T C Saido,
S Nagao,
M Shiramine,
M Tsukaguchi,
T Yoshizawa,
H Sorimachi,
H Ito,
T Tsuchiya,
S Kawashima,
K Suzuki
Publication year - 1994
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(94)00487-0
Subject(s) - autolysis (biology) , calpain , proteolysis , protein subunit , biochemistry , isozyme , protease , biology , chemistry , microbiology and biotechnology , enzyme , biophysics , gene
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, μ‐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.