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 Lettjournal_title
FEBS lettersauthors
Eriksson O,Fontaine E,Petronilli V,Bernardi Pdoi
10.1016/s0014-5793(97)00549-8subject
Has Abstractpub_date
1997-06-16 00:00:00pages
361-4issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00549-8journal_volume
409pub_type
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