Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of a long-acting somatostatin analogue on the acute renal hypertrophy following induction of experimental diabetes in the rat has been studied. The kidney weight increase occurring at 2 and 7 days after alloxan injection was significantly lower in the diabetic group receiving somatostatin. Similarly, the previously reported increase in glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.44) found in the kidney at 2 and 7 days of diabetes was less marked in the group receiving SMS 201-995. The fall in renal phosphoribosyl pyrophosphate associated with early diabetic renal hypertrophy (7) was also lessened by administration of SMS 201-995. No effects of the drug were found in the normal rat on the same regimen of treatment. These observations indicate involvement of glucagon and/or growth hormone in the initiation of kidney growth in diabetes.
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PMID:The effect of a somatostatin analogue (SMS 201-995, Sandostatin) on the concentration of phosphoribosyl pyrophosphate and the activity of the pentose phosphate pathway in the early renal hypertrophy of experimental diabetes in the rat. 245 25

Rats fasted for 2 days were refed a 60% glucose diet for varying periods of time in order to follow the kinetics for changes in 6-phosphogluconate dehydrogenase synthesis and mRNA content. Hepatocytes isolated from control or induced rats were incubated with actinomycin D and the rate of decline in 6-phosphogluconate dehydrogenase mRNA was determined by translating RNA in a nuclease-treated reticulocyte lysate. The half-life for 6-phosphogluconate dehydrogenase mRNA under both of these conditions was about 2 h. Thus, increases in transcription or the processing of nuclear RNA may increase 6-phosphogluconate dehydrogenase mRNA during the dietary induction of this enzyme. Hepatocytes prepared from fasted rats were cultured with 5% serum and various hormones and energy sources. If hepatocytes were isolated from thyroidectomized rats and cultured in serum from a thyroidectomized calf, the 4-fold induction of 6-phosphogluconate dehydrogenase was primarily dependent upon added insulin. In the presence of optimal insulin concentrations (10(-7) M) triiodothyronine slightly stimulated 6-phosphogluconate dehydrogenase induction. The gut hormones somatostatin and secretin had no effect on 6-phosphogluconate dehydrogenase induction in cultured hepatocytes. Hepatocytes cultured in carbohydrate-free medium and 5% serum required added insulin for maximal induction. 8-Br-cGMP did not significantly affect 6-phosphogluconate dehydrogenase induction in hepatocytes either in the presence or absence of added insulin. Dibutyryl cAMP did not alter the time course or extent of 6-phosphogluconate dehydrogenase induction in cultured hepatocytes. We have concluded that under these conditions insulin is a potent signal regulating the levels of 6-phosphogluconate dehydrogenase mRNA and that this induction is not mediated by cyclic nucleotides.
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PMID:Kinetics for changes in enzyme synthesis and mRNA content and hormones required for induction of 6-phosphogluconate dehydrogenase in hepatocytes. 632 Aug 94