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    Free Radic Biol Med. 2009 Apr 1;46(7):884-92. Epub 2008 Dec 24.

    Glucose-mediated tyrosine nitration in adipocytes: targets and consequences.

    Koeck T, Willard B, Crabb JW, Kinter M, Stuehr DJ, Aulak KS.

    Source

    Department of Pathobiology, Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, OH 44118, USA. koeckt@ccf.org

    Abstract

    Hyperglycemia, a key factor in insulin resistance and diabetic pathology, is associated with cellular oxidative stress that promotes oxidative protein modifications. We report that protein nitration is responsive to changes in glucose concentrations in 3T3-L1 adipocytes. Alterations in the extent of tyrosine nitration as well as the cellular nitroproteome profile correlated tightly with changing glucose concentrations. The target proteins we identified are involved in fatty acid binding, cell signaling, protein folding, energy metabolism, antioxidant capacity, and membrane permeability. The nitration of adipocyte fatty acid binding protein (FABP4) at Tyr19 decreases, similar to phosphorylation, the binding of palmitic acid to the fatty acid-free protein. This potentially alters intracellular fatty acid transport, nuclear translocation of FABP4, and agonism of PPAR gamma. Our results suggest that protein tyrosine nitration may be a factor in obesity, insulin resistance, and the pathogenesis of diabetes.

    PMID:
    19135148
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2888280
    Free PMC Article

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