Acyl-CoA-binding protein is a potent m-calpain activator

作者：Melloni E^*; Averna M; Salamino F; Sparatore B; Minafra R; Pontremoli S

来源：Journal of Biological Chemistry, 2000, 275(1): 82-86.

DOI：10.1074/jbc.275.1.82

Acyl-CoA-binding protein, a 20-kDa homodimer that exerts many physiological functions, promotes activation of the classic calpain forms, most markedly that of the m-isozyme, This protein factor was purified from rat skeletal muscle and was also expressed in Escherichia coli. Both native and recombinant acyl-CoA-binding proteins show the same molecular properties and an identical capacity to decrease the [Ca2+] required for m-calpain activity. The binding of long chain acyl-CoAs to acyl-CoA-binding protein does not modify the activating effect on calpains. Acyl-CoA-binding protein seems to be involved in the m-calpain regulation process, whereas the previously identified UK114 activator is a specific modulator of m-calpain. Acyl-CoA-binding protein is proposed as a new component of the Ca2+-dependent proteolytic system. A comparative analysis among levels of classic calpains and their activator proteins is also reported.

• 出版日期2000-1-7