The phosphorylation or dephosphorylation of many proteins plays a vital role in insulin actions, beginning with the receptor which is itself a protein tyrosine kinase. Acetyl-CoA carboxylase is an important “downstream target” for insulin action, showing increased phosphorylation and activation in response to the hormone. Our current studies are therefore concerned with:
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the structure, function and regulation of acetyl-CoA carboxylase,
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purification and characterization of insulin-stimulated protein kinases,
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actions of insulin-mimetic and potentially anti-diabetic agents which are able to affect protein phosphorylation and dephosphorylation reactions — notably actions of vanadium,
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development of techniques to employ primary human cells (especially circulating mononuclear cells) in order to apply our biochemical understanding of insulin actions to expose abnormalities in human diabetes.