Quantitative proteomics and weighted correlation network analysis of tear samples in adults and children with diabetes and dry eye

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Abstract

Purpose: Diabetics are more prone to suffer from dry eye (DE). The ages of diabetes are decreasing, so ocular surface status in younger generations is worthy of attention. We used tandem mass tag (TMT)–labeled proteomics and weighted correlation network analysis (WGCNA) to identify differentially expressed proteins in the tear proteome of adults and children with diabetic DE. Methods: Study subjects were divided into six groups of 10, including three groups each for adults and children. The adult groups included diabetics with DE (A), diabetics without DE (B), and normal controls (C); the corresponding groups of children were identified as (D), (E), and (F). DE tests were performed on all subjects. We extracted total proteins and labeled them with TMTs for analysis. WGCNA was used to recognize hub genes. Results: Tear film function was poorer in patients with diabetic DE. In adults, 1922 proteins were identified, and WGCNA analysis revealed three hub genes related to diabetic DE. For children, 2709 proteins were identified, and WGCNA analysis identified one hub gene related to diabetic DE. Kyoto Encyclopedia of Genes and Genomes analysis found similarities among metabolic pathways involved in differential expression of proteins in adult and child tear samples. Conclusions: The pathogenesis of diabetic DE was highly similar in adults and children. The differentially expressed tear proteins in type 2 diabetes of adults and children was associated with inflammation, immune factors, and lipid metabolism. Translational Relevance: Our findings found high similarities in the pathogenesis of diabetic DE in adults and children.

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Zou, X., Wang, S., Zhang, P., Lu, L., & Zou, H. (2020). Quantitative proteomics and weighted correlation network analysis of tear samples in adults and children with diabetes and dry eye. Translational Vision Science and Technology, 9(13), 1–15. https://doi.org/10.1167/tvst.9.13.8

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