Inhibition of the mitochondrial cyclosporin A-sensitive permeability transition pore by the arginine reagent phenylglyoxal.

Abstract:

:The mitochondrial permeability transition pore, a cyclosporin A-sensitive channel, is controlled by the transmembrane electric potential difference across the inner membrane. Here, we show that treatment of rat liver mitochondria with the arginine reagent phenylglyoxal inhibits the permeability transition pore triggered by depolarization with uncoupler after Ca2+ accumulation. Phenylglyoxal does not change the extent of mitochondrial Ca2+ uptake or the extent of membrane depolarization, indicating that covalent modification of arginine (and possibly lysine) residues directly affects the open probability of the pore. We propose that arginine residues play a role in the physiological control of the permeability transition pore by the mitochondrial transmembrane potential.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Eriksson O,Fontaine E,Petronilli V,Bernardi P

doi

10.1016/s0014-5793(97)00549-8

subject

Has Abstract

pub_date

1997-06-16 00:00:00

pages

361-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00549-8

journal_volume

409

pub_type

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