Overexpression of peroxiredoxin 2 in pterygium. A proteomic approach

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 mos...

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Veröffentlicht in:Experimental eye research 2013-05, Vol.110, p.70-75
Hauptverfasser: Bautista-de Lucio, V.M., López-Espinosa, N.L., Robles-Contreras, A., Pérez-Cano, H.J., Mejía-López, H., Mendoza, G., Jiménez-Martínez, M.C., Garfias, Y.
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container_title Experimental eye research
container_volume 110
creator Bautista-de Lucio, V.M.
López-Espinosa, N.L.
Robles-Contreras, A.
Pérez-Cano, H.J.
Mejía-López, H.
Mendoza, G.
Jiménez-Martínez, M.C.
Garfias, Y.
description 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. ► Peroxiredoxin 2 was exclusively identified in pterygia by means of 2D electrophoresis and mass spectrometry. ► Peroxiredoxin 2 was overexpressed in pterygia compared to healthy conjunctivas. ► Overexpression of peroxiredoxin 2 was corroborated using real-time PCR and western blot.
doi_str_mv 10.1016/j.exer.2013.03.001
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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. ► Peroxiredoxin 2 was exclusively identified in pterygia by means of 2D electrophoresis and mass spectrometry. ► Peroxiredoxin 2 was overexpressed in pterygia compared to healthy conjunctivas. ► Overexpression of peroxiredoxin 2 was corroborated using real-time PCR and western blot.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>23499777</pmid><doi>10.1016/j.exer.2013.03.001</doi><tpages>6</tpages></addata></record>
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subjects Adult
Amino Acid Sequence
Blotting, Western
Conjunctiva - enzymology
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Eye Proteins - chemistry
Eye Proteins - genetics
Eye Proteins - metabolism
Female
Humans
Immunohistochemistry
Isoelectric Focusing
Male
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Oxidation-Reduction
oxidative stress
peroxiredoxin 2
Peroxiredoxins - chemistry
Peroxiredoxins - genetics
Peroxiredoxins - metabolism
Proteomics
pterygium
Pterygium - enzymology
Reverse Transcriptase Polymerase Chain Reaction
RNA, Messenger - metabolism
title Overexpression of peroxiredoxin 2 in pterygium. A proteomic approach
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