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calpain <enzyme> Calcium activated cytoplasmic proteases containing the EF hand motif. Calpain I is activated by micromolar calcium, Calpain II by millimolar calcium.
Calpain has two subunits, the larger (80 kD) has 4 domains one homologous with papain, one with calmodulin, the smaller (30 kD) has one domain homologous with calmodulin. First isolated from erythrocytes, but now described from other cells.
(13 Oct 1997)
calpains Calcium-dependent proteinases.
Origin: calcium + suffix -pain, protease, fr. Papain
(05 Mar 2000)
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  • Calpain - »õâ Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including neuropeptides, cytoskeletal proteins, proteins from smooth muscle, cardiac muscle, liver, platelets and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.
    Synonyms : Ca2+-Activated Protease, Calcium-Activated Neutral Proteinase, Calcium-Activated Protease, Calcium-Dependent Neutral Protease, Calpain I, Calpain II, Desminase, Ca2+ Activated Protease, Calcium Activated Neutral Protease, Calcium Activated Neutral Proteinase
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calpain (cal
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