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The Role of Adrenergic Agonists on Glycogenolysis in Rat Hepatocyte Cultures and Possible Involvement of NO.
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- Author(s): Hodis, J.; Kutinová-Canová, N.; Potmêšil, P.; Kameníková, L.; Kmoníčková, E.; Zídek, Z.; Farghali, H.
- Source:
Physiological Research; 2007, Vol. 56 Issue 4, p419-425, 7p, 1 Black and White Photograph, 1 Chart, 2 Graphs
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- Additional Information
- Abstract:
Certain liver metabolic diseases point to the presence of disturbances in glycogen deposition. Epinephrine raises the cAMP level that activates protein kinase A leading to the activation of phosphorylase and glycogen breakdown. In the present report, we sought to investigate whether NO is produced during adrenoceptor agonist-induced glycogenolysis in rat hepatocytes in cultures. Isolated glycogen rich rat hepatocytes in cultures were used. NO production (NO2-) was assessed under the effect of adrenergic agonists and adrenergic agonist/antagonist pairs, dibutyryl cyclic AMP sodiumpotassium salt (db-cAMP), NO synthase (NOS) inhibitors Nω-nitro-L-arginine methyl ester (L-NAME), aminoguanidine (AG) and the NO donor S-nitroso-N-acetyl penicillamine (SNAP). The inducible NO synthase (iNOS) mRNA was examined by the reverse transcription-polymerase chain reaction (RT-PCR). Glycogenolysis was quantified by glucose levels released into medium. The amount of glucose and NO2- released by hepatocytes was increased as a result of epinephrine, phenylephrine or db-cAMP treatments. The increase in glucose and NO2- released by epinephrine or phenylephrine was blocked or reduced by prazosin pretreatment and by NOS inhibitors aminoguanidine and LNAME. iNOS gene expression was up-regulated by epinephrine. It can be concluded that glycogenolysis occurs through α-adrenoceptor stimulation and a signaling cascade may involve NO production. [ABSTRACT FROM AUTHOR]
- Abstract:
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