Two modes of activation of the permeability transition pore: the role of mitochondrial cyclophilin.
Mol Cell Biochem
; 174(1-2): 181-4, 1997 Sep.
Article
en En
| MEDLINE
| ID: mdl-9309684
ABSTRACT
Mitochondria possess an inner membrane channel, the permeability transition pore, which is inhibited by cyclosporin A (CsA) and by matrix protons. As suggested recently by our laboratory, pore closure by these inhibitors may be due to dissociation of mitochondrial cyclophilin (CyP-M), a matrix peptidyl-prolyl-cis-trans isomerase, from its putative binding site on the pore. Unbinding of CyP-M would follow a CsA-dependent or proton-dependent change in conformation of the CyP-M molecule. It is interesting that upon binding of CsA the enzymatic activity of CyP-M is inhibited, but it is not clear whether this event plays a role in pore inhibition. Here we report experiments designed to further test the role of CyP-M in pore function. Our results indicate that CyP-M-dependent and independent mechanisms of pore activation may exist, and that the peptidylprolyl-cis-trans-isomerase activity of CyP-M is not necessarily involved in pore modulation by CyP-M.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Mitocondrias Hepáticas
/
Isomerasa de Peptidilprolil
Límite:
Animals
Idioma:
En
Revista:
Mol Cell Biochem
Año:
1997
Tipo del documento:
Article
País de afiliación:
Italia