期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 474, 期 1, 页码 220-224出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.03.014
关键词
O-GlcNAc; protein modification; platelets; aggregation; diabetes
资金
- NHLBI NIH HHS [R21 HL081614, HL081614, HL56652, R21 HL081614-01A1, R21 HL081614-02, R01 HL056652] Funding Source: Medline
It is generally appreciated that platelets derived from diabetic patients display increased responsiveness to low levels of agonists. O-GlcNAcylation has been linked to hyperglycemia-related effects in other tissues; therefore we examined this modification in platelets to determine if O-GlcNAcylation affects platelet function. This post-translational modification consists of an N-acetylglucosamine attached to serine and/or threonine residues. We examined O-GlcNAc levels in platelets from a hyperglycemic murine model of Type I diabetes with known hypersensitivity to agonists and a Type II diabetes model (ob/ob) lacking detectable alterations in the aggregation profile. Neither model showed marked increases in protein O-GlcNAcylation. Treatment of platelets with Multiple O-GlcNAcase inhibitors led to O-GlcNAc accumulation on multiple platelet proteins. However, the inhibitor-induced accumulation of this modification does not correlate with any gross alterations in platelet aggregation. These data suggest that while the modification occurs in platelets, their activity is not globally sensitive to O-GlcNAc levels. (C) 2008 Elsevier Inc. All rights reserved.
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