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Proteomic Analysis of the Vitreous Body in Proliferative and Non-Proliferative Diabetic Retinopathy

Authors
DUONG VAN ANAhn, JeeyunHan, Na-YoungPark, Jong-MoonMok, Jeong-HunKim, Tae WanLee, Hookeun
Issue Date
May-2021
Publisher
BENTHAM SCIENCE PUBL LTD
Keywords
Gene ontology; LC-MS/MS; Non-proliferative diabetic retinopathy; Proliferative diabetic retinopathy; Proteomics; Vitreous body
Citation
CURRENT PROTEOMICS, v.18, no.2, pp.143 - 152
Journal Title
CURRENT PROTEOMICS
Volume
18
Number
2
Start Page
143
End Page
152
URI
https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/81157
DOI
10.2174/1570164617666200302101442
ISSN
1570-1646
Abstract
Background: Diabetic Retinopathy (DR), one of the major microvascular complications commonly occurring in diabetic patients, can be classified into Proliferative Diabetic Retinopathy (PDR) and Non-Proliferative Diabetic Retinopathy (NPDR). Currently, available therapies are only targeted for later stages of the disease in which some pathologic changes may be irreversible. Thus, there is a need to develop new treatment options for earlier stages of DR through revealing patho-logical mechanisms of PDR and NPDR. Objective: The purpose of this study was to characterize the proteomes of diabetes through quantitative analysis of PDR and NPDR. Methods: Vitreous body was collected from three groups: control (non-diabetes mellitus), NPDR, and PDR. Vitreous proteins were digested to peptide mixtures and analyzed using LC-MS/MS. MaxQuant was used to search against the database and statistical analyses were performed using Perseus. Gene ontology analysis, related-disease identification, and protein-protein interaction were performed using the differential expressed proteins. Results: Twenty proteins were identified as critical in PDR and NPDR. The NPDR group showed different expressions of kininogen-1, serotransferrin, ribonuclease pancreatic, osteopontin, keratin type II cytoskeletal 2 epidermal, and transthyretin. Also, prothrombin, signal transducer and activa-tor of transcription 4, hemoglobin subunit alpha, beta, and delta were particularly up-regulated proteins for PDR group. The up-regulated proteins related to complement and coagulate cascades. Statherin was down-regulated in PDR and NPDR compared with the control group. Transthyretin was the unique protein that increased its abundance in NPDR compared with the PDR and control group. Conclusion: This study confirmed the different expressions of some proteins in PDR and NPDR. Additionally, we revealed uniquely expressed proteins of PDR and NPDR, which would be differential biomarkers: prothrombin, alpha-2-HS-glycoprotein, hemoglobin subunit alpha, beta, and tran-sthyretin. © 2021 Bentham Science Publishers.
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