Sp1 Mediates Glucose Activation of the Acetyl-CoA Carboxylase Promoter
نویسندگان
چکیده
منابع مشابه
Regulation of acetyl-coA carboxylase: properties of coA activation of acetyl-coA carboxylase.
Acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] is activated by physiological concentrations of CoA. The CoA concentration dependency of this activation is sigmoidal; below 60 microM there is little or no activation, but the activation observed between 60 and 120 microM indicates that small changes in the concentration of CoA can cause significant changes in ...
متن کاملDephosphorylation of Sp1 by protein phosphatase 1 is involved in the glucose-mediated activation of the acetyl-CoA carboxylase gene.
When mouse 30A5 preadipocytes are exposed to high glucose concentrations, acetyl-CoA carboxylase is induced through glucose activation of promoter II of the acetyl-CoA carboxylase gene. Glucose treatment of the cells increases Sp1 binding to two GC-rich glucose response elements in promoter II. We have investigated the mechanism by which glucose increases Sp1 binding and transactivation of prom...
متن کاملPlant acetyl-CoA carboxylase.
medium containing [” Plphosphate, the distribution of 32P-labelled acetyl-CoA carboxylase in the fractions can be investigated and it has been found that a greater proportion of the phosphorylated enzyme is present in the polymeric form after exposure of the intact tissue to insulin. Present studies are concerned with investigating whether this polymeric active form is phosphorylated to a great...
متن کاملLiver acetyl CoA carboxylase: insight into the mechanism of activation by tricarboxylic acids and acetyl CoA.
Recent investigations in this laboratory have shownl 2 that the isocitrate(or citrate-) activated form of liver acetyl CoA carboxylase (E.C. 6.4.1.2) is a large protein structure having a molecular weight of about four million. Electron microscopic examination of the carboxylase in the presence of isocitrate reveals' that it has a filamentous structure with dimensions of SG-100 A by up to 5000 ...
متن کاملInsulin stimulates the dephosphorylation and activation of acetyl-CoA carboxylase.
The mechanism underlying the ability of insulin to acutely activate acetyl-CoA carboxylase [acetyl-CoA: carbon-dioxide ligase (ADP-forming), EC 6.4.1.2; AcCoA-Case] has been examined in Fao Reuber hepatoma cells. Insulin promotes the rapid activation of AcCoACase, as measured in cell lysates, and this stimulation persists to the same degree after isolation of AcCoACase by avidin-Sepharose chrom...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.3.1385