Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mitogenic signals that control fructose 2,6-bisphosphate metabolism in murine Swiss 3T3 fibroblasts have been studied. Bombesin, vasopressin, insulin, protein kinase C activation by phorbol esters, or increase in the intracellular cAMP concentration by forskolin induced an increase in fructose 2,6-bisphosphate levels. When the cells were incubated in the presence of insulin or phorbol esters, an increase in the Vmax of 6-phosphofructo-2-kinase activity was observed. However, forskolin did not produce this effect. The increase in 6-phosphofructo-2-kinase activity elicited by phorbol 12,13-dibutyrate was blocked by cycloheximide. In contrast, the effect of insulin did not require protein synthesis. This study demonstrates that different mitogenic signal transduction pathways control the levels of fructose 2,6-bisphosphate. The high rate of glycolysis in proliferating Swiss 3T3 cells may be explained by an increase in the levels of this regulatory metabolite.
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PMID:Control of fructose 2,6-bisphosphate metabolism by different mitogenic signals in Swiss 3T3 fibroblasts. 817 46

The purpose of this study was to identify the mechanism by which proglycosyn and resorcinol decrease the phosphorylase a content and the fructose 2,6-bisphosphate concentration in isolated hepatocytes. The intracellular concentrations of the glucuronide derivatives of proglycosyn and resorcinol have been measured by HPLC in hepatocytes incubated for 5 min or 30 min with different concentrations of these agents. At both times, there was a reciprocal relationship between the phosphorylase a content and the intracellular concentration of the glucuronidated metabolites, half-maximal inactivation being observed at about 2 mumol/g protein and 0.25 mumol/g protein for resorcinylglucuronide and proglycosyn-glucuronide, respectively. Glycogen synthase was not significantly activated by these agents after 5 min but was well activated after 30 min. Preincubation of hepatocytes with 1 mM resorcinol or with 100 microM proglycosyn resulted in a decrease in the rate at which phosphorylase was activated following the addition of glucagon, vasopressin, the protein phosphatase inhibitor calyculin A or the calcium ionophore A 23187, but did not reduce the rate of synthase inactivation. Proglycosynglucuronide and resorcinylglucuronide inhibited phosphorylase kinase in liver Sephadex filtrates, with Ki values of about 0.75 mM and 4 mM, respectively. Preincubation of the filtrates with ATP and cAMP decreased the sensitivity of phosphorylase kinase to resorcinylglucuronide by about fourfold. It is concluded that the effect of resorcinol and proglycosyn on the phosphorylase a content is due, at least partly, to an inhibition of phosphorylase kinase by their glucuronidated metabolites. Resorcinol and proglycosyn caused a parallel decrease in the concentration of fructose 2,6-bisphosphate and of hexose 6-phosphates, without significantly changing the activity of 6-phosphofructo-2-kinase. The decrease in the fructose 2,6-bisphosphate concentration appears therefore to be secondary to the decrease in the hexose 6-phosphate concentration.
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PMID:Involvement of phosphorylase kinase inhibition in the effect of resorcinol and proglycosyn on glycogen metabolism in the liver. 852 56