Abstract
1. Regulation of the reduction of ferricyanide by the isolated perfused rat liver was studied. 2. The rate of reduction was dependent on the rate of supply of ferricyanide and independent of perfusate oxygen concentration. 3. The effect of pH was also examined; the rate of reduction was optimal at pH 7.4 and was inhibited to a greater extent by pH values below 7.4 than those above 7.4. 4. The effects of substrates on the rate of ferricyanide reduction was assessed. Reductants of the cytosolic and mitochondrial NADH/NAD+ couple were tested. 2-Hydroxybutyrate (10mm), lactate (10mm), glycerol (10mm) and ethanol (10mm) each had no effect. Dihydroxyacetone (10mm) stimulated the rate. 5. Dehydroascorbate (1mm), stimulated the rate of ferricyanide reduction; the stimulation did not appear to be attributable to the production of reduced substances that were excreted to reduce extracellular ferricyanide. 6. The effects of glucagon and cyclic AMP on the rate of ferricyanide reduction were examined. Glucagon inhibited the rate by approx. 30% and half-maximal inhibition occurred at 0.1 nm, corresponding to the concentration at which half-maximal stimulation of glucose release occurred. Cyclic AMP stimulated glucose release but had no significant effect on the rate of ferricyanide reduction. It is concluded that the trans-plasma membrane redox system of liver that reduces extracellular ferricyanide is regulated by glucagon. The rate is also altered by the substrate dihydroxyacetone. The effect of glucagon may be direct as it cannot be mimicked by cyclic AMP and it occurs directly following exposure to the hormone.
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Selected References
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- Clark M. G., Kneer N. M., Bosch A. L., Lardy H. A. The fructose 1,6-diphosphatase-phosphofructokinase substrate cycle. A site of regulation of hepatic gluconeogenesis by glucagon. J Biol Chem. 1974 Sep 25;249(18):5695–5703. [PubMed] [Google Scholar]
- Clark M. G., Partick E. J., Patten G. S., Crane F. L., Löw H., Grebing C. Evidence for the extracellular reduction of ferricyanide by rat liver. A trans-plasma membrane redox system. Biochem J. 1981 Dec 15;200(3):565–572. doi: 10.1042/bj2000565. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldenberg H., Crane F. L., Morré D. J. Influence of hormones on NADH-dehydrogenase in mouse liver plasma membrane. Biochem Biophys Res Commun. 1978 Jul 14;83(1):234–240. doi: 10.1016/0006-291x(78)90421-7. [DOI] [PubMed] [Google Scholar]
- Löw H., Crane F. L. Hormone regulated redox function in plasma membranes. FEBS Lett. 1976 Oct 1;68(2):157–159. doi: 10.1016/0014-5793(76)80426-7. [DOI] [PubMed] [Google Scholar]
- Löw H., Crane F. L. Redox function in plasma membranes. Biochim Biophys Acta. 1978 Jul 31;515(2):141–161. doi: 10.1016/0304-4157(78)90002-3. [DOI] [PubMed] [Google Scholar]
- MANYAI S., SZEKELY M. Die Wirkung von Natriumfluorid und Monojodessigsäure auf die Glykolyse von menschlichen roten Blutkörperchen. Acta Physiol Acad Sci Hung. 1954;5(1-2):7–18. [PubMed] [Google Scholar]
- Orringer E. P., Roer M. E. An ascorbate-mediated transmembrane-reducing system of the human erythrocyte. J Clin Invest. 1979 Jan;63(1):53–58. doi: 10.1172/JCI109277. [DOI] [PMC free article] [PubMed] [Google Scholar]
- STAUDINGER H., WEIS W. REINDATSTELLUNG UND KRISTALLISATION VON DEHYDRO-L-ASCORBINSAEURE. Hoppe Seylers Z Physiol Chem. 1964;337:284–285. doi: 10.1515/bchm2.1964.337.1.284. [DOI] [PubMed] [Google Scholar]
- SZEKELY M., MANYAI S., STRAUB F. B. Uber den mechanismus der osmotischen hämolyse. Acta Physiol Acad Sci Hung. 1952;3(3-4):571–584. [PubMed] [Google Scholar]