Structural modifications associated with the change in Ca2+ sensitivity on activation of m‐calpain
- 3 May 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 322 (1), 65-68
- https://doi.org/10.1016/0014-5793(93)81112-d
Abstract
Autolysis of the Ca2+-dependent cysteine protease m-calpain involves cleavage of the large (80 kDa) and small (30 kDa) subunits of the enzyme, and an increase in Ca2+ sensitivity. The appearance of increased Ca2+ sensitivity was found to correlate with the cleavage of the large subunit after residue 9.Keywords
This publication has 22 references indexed in Scilit:
- Polyclonal antisera specific for the proenzyme form of each calpainBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
- Two-stage autolysis of the catalytic subunit initiates activation of calpain IBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Investigation of the structural basis of the interaction of calpain II with phospholipid and with carbohydrateBiochemical Journal, 1990
- Molecular cloning of the cDNA for the large subunit of the high-calcium-requiring form of human calcium-activated neutral proteaseBiochemistry, 1988
- The effects of autolysis on the structure of chicken calpain IIBiochemical Journal, 1987
- Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological functionFEBS Letters, 1987
- Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequenceFEBS Letters, 1986
- Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?Nature, 1984
- Comparison of low- and high-calcium-requiring forms of the calcium-activated protease with their autocatalytic breakdown productsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970