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Open AccessJournal ArticleDOI

Activation of pyruvate dehydrogenase in adipose tissue by insulin. Evidence for an effect of insulin on pyruvate dehydrogenase phosphate phosphatase.

C Mukherjee, +1 more
- 15 May 1975 - 
- Vol. 148, Iss: 2, pp 229-235
TLDR
It is suggested that insulin increases the fraction of pyruvate dehydrogenase present in the tissue in the active dephospho form by increasing the activity of pyRuvatehydrogenase phosphate phosphatase.
Abstract
1. The mechanism by which insulin activates pyruvate dehydrogenase in rat epididymal adipose tissue was further investigated. 2. When crude extracts, prepared from tissue segments previously exposed to insulin (2m-i.u/ml) for 2min, were supplemented with Mg-2+, Ca-2+, glucose and hexokinase and incubated at 30 degrees C, they displayed an enhanced rate of increase in pyruvate dehydrogenase activity compared with control extracts. 3. When similar extracts were instead supplemented with fluoride, ADP, creatine phosphate and creatine kinase, the rate of decrease in pyruvate dehydrogenase activity observed during incubation at 30 degrees C was unaffected by insulin treatment. 4. It is suggested that insulin increases the fraction of pyruvate dehydrogenase present in the tissue in the active dephospho form by increasing the activity of pyruvate dehydrogenase phosphate phosphatase.

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Book ChapterDOI

Hormonal control of hepatic gluconeogenesis.

TL;DR: This chapter describes the hormonal control of hepatic gluconeogenesis, which is the process whereby lactate, pyruvate, glycerol, and certain amino acids are converted into glucose and glycogen.
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Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents.

TL;DR: A close relationship was observed between the cellular content of glutathione (GSH) and glucose utilization, and induction of a peroxidative metabolism within these cells, coupled with glucose oxidation, appears to be a major effect of insulin.
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Purification and properties of pyruvate dehydrogenase phosphatase from bovine heart and kidney.

TL;DR: It is proposed that the second site may be at the interface between the phosphatase and E2, with Ca2+ acting as a bridging ligand for specific attachment of the phosph atase to E2.
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Activation and mitochondrial translocation of protein kinase Cδ are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells

TL;DR: In muscle and liver cells, insulin causes activation and mitochondrial translocation of PKCδ, accompanied by PDP phosphorylation and activation, which are necessary for insulin activation of the PDH complex in these cells.
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