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Articles in PresS, published online ahead of print October 22, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00382.2002
Submitted on August 28, 2002
Accepted on October 16, 2002
-tubulin
1 Department of Pharmacology, Medical University of South Carolina, Charleston, SC, USA; Department of Medicine, Division of Endocrinology, Diabetes, and Medical Genetics, Medical University of South Carolina, Charleston, SC, USA
2 Department of Pathology, Medical University of South Carolina, Charleston, SC, USA
3 Department of Pharmacology, Medical University of South Carolina, Charleston, SC, USA
4 Department of Medicine, Division of Endocrinology, Diabetes, and Medical Genetics, Medical University of South Carolina, Charleston, SC, USA; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA
* To whom correspondence should be addressed. E-mail: busemg{at}musc.edu.
Increased flux through the hexosamine biosynthesis pathway has been implicated in the development of glucose-induced insulin resistance and may promote the modification of certain proteins with O-linked GlcNAc. L6 myotubes (a model of skeletal muscle) were incubated for 18 hrs in 5 mM or 25 mM glucose ± 10 nM insulin. As assessed by immunoblotting with an O-GlcNAc-specific antibody, high glucose and/or insulin enhanced O-GlcNAcylation of numerous proteins, including the transcription factor Sp1, a known substrate for this modification. To identify novel proteins that may be O-GlcNAc-modified in a glucose concentration/insulin-responsive manner, total cell membranes were separated by 1D or 2D gel electrophoresis. Selected O-GlcNAcylated proteins were identified by mass spectrometry (MS) analysis. MS sequencing of tryptic peptides identified member(s) of the heat shock protein 70 (HSP70) family and rat 
-tubulin. Immunoprecipitation/immunoblot studies demonstrated several HSP70 isoforms and/or post-translational modifications, some with selectively enhanced O-GlcNAcylation following exposure to high glucose + insulin. In conclusion, in L6 myotubes, Sp1, membrane-associated HSP70, and -tubulin are O-GlcNAcylated; the modification is markedly enhanced by sustained increased glucose flux.
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