The present study investigated the regulatory effects of growth hormone (GH), human insulin-like growth factor I (hIGF-I), thyroxine (T(4)), triiodothyronine (T(3)) and cortisol, on mRNA expression of key enzymes involved in carbohydrate metabolism, including glucokinase (GK), glucose-6-phosphatase (G6Pase), glycogen synthase (GS), glycogen phosphorylase (GP) and glucose-6-phosphate dehydrogenase (G6PDH) in hepatocytes isolated from silver sea bream. Genes encoding GK, G6Pase, GS and GP were partially cloned and characterized from silver sea bream liver and real-time PCR assays were developed for the quantification of the mRNA expression profiles of these genes in order to evaluate the potential of these carbohydrate metabolic pathways. GK mRNA level was elevated by GH and hIGF-I, implying that GH-induced stimulation of GK expression may be mediated via IGF-I. GH was found to elevate GS and G6Pase expression, but reduce G6PDH mRNA expression. However, hIGF-I did not affect mRNA levels of GS, G6Pase and G6PDH, suggesting that GH-induced modulation of GS, G6Pase and G6PDH expression levels is direct, and occurs independently of the action of IGF-I. T(3) and T(4) directly upregulated transcript abundance of GK, G6Pase, GS and GP. Cortisol significantly increased transcript amounts of G6Pase and GS but markedly decreased transcript abundance of GK and G6PDH. These changes in transcript abundance indicate that (1) the potential of glycolysis is stimulated by GH and thyroid hormones, but attenuated by cortisol, (2) gluconeogenic and glycogenic potential are augmented by GH, thyroid hormones and cortisol, (3) glycogenolytic potential is upregulated by thyroid hormones but not affected by GH or cortisol, and (4) the potential of the pentose phosphate pathway is attenuated by GH and cortisol but unaffected by thyroid hormones.
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