Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The main purpose of the present study was to test the hypothesis that adrenergic stimulation of muscle fibres during exercise is a major stimulus for the training-induced enhancement of skeletal muscle respiratory capacity. Therefore, Sprague-Dawley rats either underwent bilateral surgical ablation of the adrenal medulla or were sham-operated. Furthermore, unilateral surgical extirpation of the lumbar sympathetic chain was performed. Half of the rats were then trained for 12 weeks by swimming (up to 5.5 h X day-1, 4 days X week-1) and the remaining rats were sedentary controls. In the gastrocnemius muscle, training significantly increased the mitochondrial enzymes citrate synthase, succinate dehydrogenase, cytochrome c oxidase, and 3-hydroxyacyl-CoA dehydrogenase. In sham-operated rats, the increases were 40%, 43%, 66%, and 25%, respectively, in legs with intact sympathetic innervation. The training-induced enzyme adaptation after adrenodemedullation and/or sympathectomy was not significantly lower than these control values. In sham-operated rats, training decreased resting plasma insulin and glucagon levels and increased liver glycogen content. Similar changes were induced by adrenodemedullation, but training did not augment these changes in adrenodemedullated rats. In conclusion, the data suggest that neither adrenomedullary hormones nor local sympathetic nerves are prerequisites for the training-induced increase in muscle mitochondrial enzymes. The training-induced decline in resting plasma insulin and glucagon levels in intact rats may be mediated by adrenomedullary hormones.
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PMID:Skeletal muscle and hormonal adaptation to physical training in the rat: role of the sympatho-adrenal system. 298 95

Glucagon was found to increase the mRNA level of the uricase-encoding gene (UOX), but not that of genes encoding other peroxisomal enzymes, such as catalase, acyl-CoA oxidase and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase. The possible involvement of cAMP in the glucagon-induced transcription of rat UOX was studied by measuring the enhancer activity of the isolated 5'-untranslated region of the gene. An 84-bp sequence spanning positions -169 to -86 was found to be essential for cAMP-mediated expression of rat UOX, on deletional analysis of the upstream 1.4-kb portion by means of a transient transfection assay (CAT assay). The 30-mer oligodeoxyribonucleotide (positions from -169 to -140) was found to form a DNA-protein complex by an electrophoretic mobility shift assay. The core sequence for the DNA-protein complex formation, 5'-CAAAAATGTC-3', was found to be located in positions from -164 to -155. In addition, the binding assays suggested that the DNA-binding protein(s) was different from cAMP-response element binding protein (CREB). Thus, this report shows that a novel cis-acting element of rat UOX and the binding protein(s) possibly play an essential role in the glucagon-induced transcription via cAMP.
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PMID:Transcription of the rat liver uricase-encoding gene is regulated via a cis-acting element responsive to cAMP. 856 90