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J Biol Chem, Vol. 275, Issue 1, 82-86, January 7, 2000
From the Department of Experimental Medicine, Biochemistry Section,
University of Genoa, Viale Benedetto XV,1, 16132 Genoa, Italy
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 µ-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.
Acyl-CoA-binding Protein Is a Potent m-Calpain Activator*
,
*
This work was supported by grants from the Italian National
Research Council (CNR), "Target Project Biotechnology" and
"Biotechnology Project" and from the Italian Ministry of University
and Scientific and Technilogical Research (MURST), National Interest
Projects (PRIN 1997-1998).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Fax: 39 010 518343;
E-mail: melloni@csita.unige.it.
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