Nitric oxide inhibits glycogen synthesis in isolated rat hepatocytes
| Autor: | Johannes A. Romijn, F. Sprangers, Alfred J. Meijer, G M van Woerkom, Hans P. Sauerwein |
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| Přispěvatelé: | Other departments |
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
Male
medicine.medical_specialty In Vitro Techniques Nitric Oxide Biochemistry Glycogen debranching enzyme Glycogen phosphorylase chemistry.chemical_compound Internal medicine medicine Glycogen branching enzyme Animals Rats Wistar Glycogen synthase Molecular Biology biology Glycogen Penicillamine Gluconeogenesis Cell Biology Liver Glycogen Rats Pyruvate carboxylase Isoenzymes Glycogen Synthase Endocrinology Liver chemistry Glycogenesis Glycogen-Synthase-D Phosphatase biology.protein Research Article |
| Zdroj: | Biochemical journal, 330 ( Pt 2), 1045-1049. Portland Press Ltd. |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj3301045 |
| Popis: | There is increasing evidence for the existence of intrahepatic regulation of glucose metabolism by Kupffer cell products. Nitric oxide (NO) is known to inhibit gluconeogenic flux through pyruvate carboxylase and phosphoenolpyruvate carboxykinase. However, NO may also influence glucose metabolism at other levels. Using hepatocytes from fasted rats incubated with the NO-donor S-nitroso-N-acetylpenicillamine, we have now found that the synthesis of glycogen from glucose is even more sensitive to inhibition by NO than gluconeogenesis. Inhibition of glycogen production by NO was accompanied by a rise in intracellular glucose 6-phosphate and UDPglucose. Activity of glycogen synthase, as measured in extracts of hepatocytes after the cells had been exposed to NO, was decreased. Experiments with gel-filtered liver extracts revealed that inhibition of glycogen synthase was caused by an inhibitory effect of NO on the conversion of glycogen synthase b into glycogen synthase a. |
| Databáze: | OpenAIRE |
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