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  • Title: Cytoplasmic cellular structures control permeability of outer mitochondrial membrane for ADP and oxidative phosphorylation in rat liver cells.
    Author: Fontaine EM, Keriel C, Lantuejoul S, Rigoulet M, Leverve XM, Saks VA.
    Journal: Biochem Biophys Res Commun; 1995 Aug 04; 213(1):138-46. PubMed ID: 7639727.
    Abstract:
    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.
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