Cytoplasmic cellular structures control permeability of outer mitochondrial membrane for ADP and oxidative phosphorylation in rat liver cells.
The kinetics of regulation mitochondrial respiration by external ADP in permeabilized hepatocytes was studied further. In digitonin-permeabilized hepatocytes, the apparent Km for ADP in regulation of respiration was decreased from 275 +/- 35 microM in control to 48 +/- 8 microM by a treatment with trypsin (15 min, 0.125 mg/ml). In liver tissue homogenates, trypsin treatment similarly decreased the Km value for ADP. These results show that ADP diffusion in hepatocytes may be retarded due to some unknown cytoplasmic trypsin-sensitive protein factor(s) which may be lost during isolation of mitochondria. Since we have previously reported a limited permeability of the outer mitochondrial membrane in isolated hepatocytes (Saks et al. 1995, Biochem. Biophys. Res. Commun., 208, 919-926), we conclude that an important site of control of respiration in liver cells in vivo is located at the porin channels of the outer mitochondrial membrane.
Fontaine
E M
EM
Laboratoire de Bioénergétique, Université Joseph Fourier, Grenoble, France.
Keriel
C
C
Lantuejoul
S
S
Rigoulet
M
M
Leverve
X M
XM
Saks
V A
VA
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D003593:Cytoplasm / Q000378:metabolism / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000378:metabolism* / Q000648:ultrastructure; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D010085:Oxidative Phosphorylation; D010101:Oxygen Consumption; D010539:Permeability; D051381:Rats; D014357:Trypsin / Q000494:pharmacology
D000244:Adenosine Diphosphate; D014357:Trypsin