Serum Glycoproteomic Alterations in Patients with Diabetic Retinopathy

被引:13
作者
Sharma, Ashok [1 ,2 ,3 ,4 ]
Cox, James [1 ]
Glass, Joshua [1 ]
Lee, Tae Jin [1 ]
Kodeboyina, Sai Karthik [1 ]
Zhi, Wenbo [1 ]
Ulrich, Lane [2 ]
Lukowski, Zachary [2 ]
Sharma, Shruti [1 ,2 ,4 ]
机构
[1] Augusta Univ, Ctr Biotechnol & Genom Med, Augusta, GA 30912 USA
[2] Augusta Univ, Dept Ophthalmol, Augusta, GA 30912 USA
[3] Augusta Univ, Dept Populat Hlth Sci, Augusta, GA 30912 USA
[4] Augusta Univ, Culver Vis Discovery Inst, Augusta, GA 30912 USA
基金
美国国家卫生研究院;
关键词
diabetic retinopathy; glycoproteomics; LC-MS; MS; APOLIPOPROTEIN-CIII; CELL-ADHESION; PROTEIN CONCENTRATIONS; ENDOTHELIAL-CELLS; FETUIN-A; GLYCOSYLATION; FIBRONECTIN; COMPLEMENT; CANCER; VITRONECTIN;
D O I
10.3390/proteomes8030025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The precise molecular mechanisms of diabetic retinopathy (DR) pathogenesis are unclear, and treatment options are limited. There is an urgent need to discover and develop novel therapeutic targets for the treatment of this disease. Glycosylation is a post-translational modification that plays a critical role in determining protein structure, function, and stability. Recent studies have found that serum glycoproteomic changes are associated with the presence or progression of several inflammatory diseases. However, very little is known about the glycoproteomic changes associated with DR. In this study, glycoproteomic profiling of the serum of diabetic patients with and without DR was performed. A total of 15 glycopeptides from 11 glycoproteins were found to be significantly altered (5 upregulated and 10 downregulated) within the serum glycoproteome of DR patients. These glycoproteins are known to be involved in the maintenance of the extracellular matrix and complement system through peptidolytic activity or regulation.
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页数:16
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