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To: nigel bates who wrote (6827)	8/20/2010 9:51:47 AM
From: Jibacoa	Respond to of 7143

Resolving the PPAR? paradox. Researchers at the Dana-Farber Cancer Institute and Scripps Florida have found an alternative mechanism by which peroxisome proliferation–activated receptor-? agonists exert their antidiabetic effects.1 By blocking phosphorylation of the protein, these compounds actually may improve insulin sensitivity independent of receptor agonism. They have shown that PPAR? is phosphorylated by the obesity-activated cyclin dependent kinase 5 (CDK5), which results in misregulation of a subset of genes that are important for insulin sensitivity. Spiegelman's team demonstrated the function of CDK5-mediated phosphorylation by transplanting fibroblasts subcutaneously into mice and allowing them to differentiate into adipocytes. Transplantation of adipocytes that expressed PPAR? lacking this phosphorylation site led to greater levels of adiponectin, a key hormone that maintains insulin sensitivity, whereas transplantation of adipocytes that expressed wild-type PPAR? did not. The most striking result was shown in patients taking a TZD agonist, in this case Avandia, in which a decrease in PPAR? phosphorylation was significantly correlated with improvement in glucose infusion rate, a measure of insulin sensitivity (p=0.001). nature.com Bernard