期刊
EXPERIMENTAL EYE RESEARCH
卷 138, 期 -, 页码 87-95出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.exer.2015.06.011
关键词
Retina; Branch retinal vein occlusion; Proteomics; Mass spectrometry; Biological marker; Integrin; Lipocalin; Osteopontin; Myosin 9; Adhesion; Extracellular matrix
资金
- Svend Andersen Foundation
- Bagger-Sorensen Foundation
- Obel Family Foundation
- Herta Christensen Foundation
- North Denmark Region [2013-0076797]
Branch retinal vein occlusion (BRVO) is a common retinal vascular disease, but global protein changes following the condition remain largely unelucidated. To bring new insights into pathological processes and identify potential therapeutic targets, large-scale retinal protein changes following BRVO were studied by combining a porcine model of experimental BRVO with proteomic analysis by label-free liquid chromatography mass spectrometry. Among a total set of 1974 proteins, 52 significantly upregulated proteins and 10 significantly downregulated proteins were identified in retinas with BRVO after 15 days. Significantly upregulated proteins were involved in signaling pathways of focal adhesion via integrin and blood coagulation. Proteins involved in focal adhesion signaling included collagen alpha-2 chain, laminin subunit beta-2, laminin subunit gamma-1, lipocalin-7, nidogen-2, osteopontin, integrin-beta, alpha-actinin-1, isoform 2 of alpha-actinin-1, talin-2 and filamin C. The identified proteins indicate that BRVO was associated with extracellular matrix remodeling processes. The present study identified focal adhesion signaling and ECM remodeling as important biological mechanisms to evaluate in the search for signaling pathways that promote neovascularisation and macular edema following BRVO. (C) 2015 Elsevier Ltd. All rights reserved.
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