The proteomic profile of a mouse model of proliferative vitreoretinopathy. Issue 8 (29th June 2017)

• Record Type: Journal Article
• Authors: Márkus, Bernadett; Pató, Zsuzsanna; Sarang, Zsolt; Albert, Réka; Tőzsér, József; Petrovski, Goran; Csősz, Éva
• Is Part Of: FEBS open bio. Volume 7:Issue 8(2017)
• Page Start: 1166
• Page End: 1177
• Publication Date: 2017-06-29
• Subjects: 2D electrophoresis -- animal model -- mass spectrometry -- PVR -- TG2; Molecular biology -- Periodicals; Cytology -- Periodicals; Life sciences -- Periodicals; Biological Science Disciplines -- Periodicals; Molecular Biology -- Periodicals; Cell Biology -- Periodicals; Cytology; Life sciences; Molecular biology; Periodicals; 572.805
• DOI: 10.1002/2211-5463.12252
• Languages: English
• ISSNs: 2211-5463

Abstract

Abstract : Proliferative vitreoretinopathy (PVR) develops as a complication of retinal detachment surgery and represents a devastating condition leading to serious vision loss. A good animal model that permits extensive functional studies and drug testing is crucial in finding better therapeutic modalities for PVR. A previously established mouse model, using dispase injection, was analyzed from the proteomic point of view, examining global protein profile changes by 2D electrophoresis, image analysis and HPLC–tandem mass spectrometry‐based protein identification. The easy applicability of the mouse model was used to study the role of transglutaminase 2 (TG2) in PVR formation by proteomic examination of dispase‐induced TG2 knockout vitreous samples. Our data demonstrate that, despite the altered appearance of crystallin proteins, the lack of TG2 did not prevent the development of PVR. Abstract : Proliferative vitreoretinopathy (PVR) is a complication of eye surgery and can lead to vision loss. Two‐dimensional electrophoresis and mass spectrometry were used to study the differential expression of proteins in wild‐type and transglutaminase 2 (TG2) knockout mouse models of dispase‐induced PVR. The data demonstrate an altered appearance of crystallin proteins and provide further evidence of the utility and applicability of the dispase‐induced mouse model for studying PVR.