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Vitreous proteomic analysis of proliferative vitreoretinopathy
Author(s) -
Yu Jing,
Liu Feng,
Cui ShuJian,
Liu Yan,
Song ZhengYu,
Cao Hui,
Chen FengE,
Wang WeiJun,
Sun Tao,
Wang Fang
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700824
Subject(s) - proliferative vitreoretinopathy , proteome , vitrectomy , proteomics , retinal detachment , pars plana , chemistry , medicine , biology , pathology , microbiology and biotechnology , ophthalmology , retinal , biochemistry , visual acuity , gene
Proliferative vitreoretinopathy (PVR) is the most common cause of anatomic failure in retinal detachment surgery. To understand the molecular mechanisms, vitreous proteomes of patients with PVR were investigated by two‐dimensional‐nano‐liquid chromatography coupled with tandem mass spectrometry. Vitreous samples of moderate PVR (grade B), and severe PVR (grade C or D) were aspirated during pars plana vitrectomy before infusion. In the current study, 129, 97 and 137 proteins were identified in vitreous of normal control, moderate and severe PVR, respectively. In PVR vitreous samples, complement components, serine proteinase inhibitors, and extracellular proteins were up‐regulated or appeared, while normal cytoskeleton and metabolism proteins were down‐regulated or disappeared. It was noteworthy that the proteins involved in transcription and translation regulation increased in vitreous with PVR. Among 102 PVR‐specific proteins, kininogen 1 was specifically detected in both vitreous and the corresponding serum. Therefore, it can be concluded that PVR is a complicated pathology process with great amount of proteins involved in metabolism dysfunction, immune reactions, and cytoskeleton remolding. Kininogen 1 may be a candidate biomarker of PVR. Further investigations of these special proteins will provide additional targets for treatment or prevention of ocular proliferative diseases.