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Identification of O‐GlcNAcylated Proteins in Diabetic Blood Cells
Author(s) -
Park Kyoungsook,
Wang Zihao,
Saudek Christopher D,
Hart Gerald W
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1009
O‐linked N‐acetylglucosamine (O‐GlcNAc) is a dynamic post‐translational modification found on nucleocytoplasmic proteins. O‐GlcNAc serves as a nutrient/stress sensor to modulate cell signaling, transcription and cellular survival. Diabetic blood cells are episodically or chronically exposed to high glucose and this results in increased O‐GlcNAcylation in blood cells. The level of O‐GlcNAc in blood cells appears to be a good indicator of the risk of diabetes and is a measurement of the extent and duration of the dysregulation of glucose homeostasis. In this study, we examined the changes of O‐GlcNAcylation in normal and diabetic human red blood cells (RBCs) and identified 29 O‐GlcNAcylated proteins by antibodies and by keto‐galactose labeling method. Western‐blotting of immunoprecipitated proteins confirm that O‐GlcNAc levels on Band3 protein and catalase increased significantly in diabetic RBCs. Currently we are investigating the O‐GlcNAc modification site of each protein. This study will broaden our understanding of the role of O‐GlcNAc in diabetes and could be used to develop a potential biomarker(s) of diabetes. Supported by NIH grants DK071280‐02 and G.W. H. receives a share of royalty received by the university on sales of the CTD 110.6 antibody. The terms of this arrangement are being managed by The Johns Hopkins University in accordance with its conflict of interest policies.