Pterygium is one of the most frequent pathologies in ophthalmology, and is a benign, fibrovascular lesion originating from the bulbar conjunctiva. It is composed of an epithelium and highly vascular, subepithelial, loose connective tissue. The etiology of pterygium is not clearly understood; the most widely recognized originating factor is ultraviolet radiation. It has been proposed that pterygium and neoplasia have common features, raising the possibility that pterygium is a neoplastic-like growth disorder. In this study, proteomic analysis was performed to show that peroxiredoxin 2 is overexpressed in pterygia compared to healthy conjunctivas. Twelve pterygium specimens were obtained together with healthy conjunctival tissue from the same eyes. Total proteins of pterygia and healthy conjunctivas were analyzed in SDS-PAGE. This analysis showed protein bands expressed exclusively in pterygium samples at the range of 20-25 kDa. After this, 2D electrophoresis was performed for the separation of total proteins; differential spots expressed in pterygium were excised and sequenced. Mass spectrometry (MS) data were searched in the NCBInr and EST databases using the MASCOT program. The spot was identified as peroxiredoxin 2. Real-time PCR, western blot and immunohistochemistry showed that peroxiredoxin 2 was increased in pterygium compared to healthy conjunctiva. Although, these results suggest that overexpression of peroxiredoxin 2 in pterygium could protect the cell against oxidative stress-induced apoptosis, further studies are required to establish the functional role of peroxiredoxin 2 in pterygium to determine its role in peroxidation and apoptosis in this pathology.
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http://dx.doi.org/10.1016/j.exer.2013.03.001 | DOI Listing |
Cornea
July 2017
*Department of Genetics, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China; and †Tianjin Key Laboratory of Ophthalmology and Visual Science, Tianjin Eye Hospital, Tianjin Eye Institute, Nankai University Eye Hospital, Clinical College of Ophthalmology, Tianjin Medical University, Tianjin, China.
Mol Vis
December 2015
Department of Bioengineering and Institute for Bioengineering and Biopharmaceutical Research, Hanyang University, Seoul, Korea.
Purpose: To identify differentially expressed proteins in the pterygium compared to healthy conjunctiva using a proteomic analysis.
Methods: Pterygial and healthy conjunctival tissues were obtained from 24 patients undergoing pterygium excision. Total proteins of the pterygia and healthy conjunctiva were analyzed with one-dimensional electrophoresis, and protein bands of interest were excised and subjected to liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-MS/MS) using Thermo's Finnigan ProteomeX workstation LTQ linear ion trap MS/MS.
J Histochem Cytochem
January 2014
Departments of Anatomical Pathology and Human Physiology, School of Medicine, Flinders University, South Australia (SK, TC, JHP).
Peroxiredoxin I and II are both 2-Cys members of the peroxiredoxin family of antioxidant enzymes and inactivate hydrogen peroxide. On western blotting, both enzymes appeared as 22-kD proteins and were present in the sclera, retina and iris. Immunohistochemistry showed strong cytoplasmic labeling in the basal cells of the corneal epithelial layer and the corneoscleral limbus.
View Article and Find Full Text PDFExp Eye Res
May 2013
Microbiology and Ocular Proteomics, Research Unit, Institute of Ophthalmology Fundación de Asistencia Privada Conde de Valenciana, Chimalpopoca, 14 Colonia Obrera, 06800 México City, Mexico.
Pterygium is one of the most frequent pathologies in ophthalmology, and is a benign, fibrovascular lesion originating from the bulbar conjunctiva. It is composed of an epithelium and highly vascular, subepithelial, loose connective tissue. The etiology of pterygium is not clearly understood; the most widely recognized originating factor is ultraviolet radiation.
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