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...
Gespeichert in:
Veröffentlicht in: | Experimental eye research 2013-05, Vol.110, p.70-75 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 75 |
---|---|
container_issue | |
container_start_page | 70 |
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 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1345513107</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014483513000559</els_id><sourcerecordid>1345513107</sourcerecordid><originalsourceid>FETCH-LOGICAL-c356t-54997d25c0148cd050eaa4bd8db61a883a5a2bd1631ac5377f4618f46b2dbe83</originalsourceid><addsrcrecordid>eNp9UE1PwzAMjRCIjcEf4IB65NKSNEnTSVwmvqVJu-wepYkLmdamJO20_XtSbXBEsp4t6_nZfgjdEpwRTIqHTQZ78FmOCc1wDEzO0JTgeZFijMU5msYOS1lJ-QRdhbCJXcoEu0STnLL5XAgxRc-rHXjYdx5CsK5NXJ104N3eejAR2yRPInQ9-MOnHZosWSSddz24xupEdbFW-usaXdRqG-DmlGdo_fqyfnpPl6u3j6fFMtWUF33Kx6Um5zqeVWqDOQalWGVKUxVElSVVXOWVIQUlSnMqRM0KUkaoclNBSWfo_igbt34PEHrZ2KBhu1UtuCFIQhnnhBIsIjU_UrV3IXioZedto_xBEixH8-RGjubJ0TyJY8Q8Q3cn_aFqwPyN_LoVCY9HAsQndzaOB22h1WCiXbqXxtn_9H8APOSAOw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1345513107</pqid></control><display><type>article</type><title>Overexpression of peroxiredoxin 2 in pterygium. A proteomic approach</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><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.</creator><creatorcontrib>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.</creatorcontrib><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.</description><identifier>ISSN: 0014-4835</identifier><identifier>EISSN: 1096-0007</identifier><identifier>DOI: 10.1016/j.exer.2013.03.001</identifier><identifier>PMID: 23499777</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>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</subject><ispartof>Experimental eye research, 2013-05, Vol.110, p.70-75</ispartof><rights>2013 Elsevier Ltd</rights><rights>Copyright © 2013 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-54997d25c0148cd050eaa4bd8db61a883a5a2bd1631ac5377f4618f46b2dbe83</citedby><cites>FETCH-LOGICAL-c356t-54997d25c0148cd050eaa4bd8db61a883a5a2bd1631ac5377f4618f46b2dbe83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014483513000559$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23499777$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bautista-de Lucio, V.M.</creatorcontrib><creatorcontrib>López-Espinosa, N.L.</creatorcontrib><creatorcontrib>Robles-Contreras, A.</creatorcontrib><creatorcontrib>Pérez-Cano, H.J.</creatorcontrib><creatorcontrib>Mejía-López, H.</creatorcontrib><creatorcontrib>Mendoza, G.</creatorcontrib><creatorcontrib>Jiménez-Martínez, M.C.</creatorcontrib><creatorcontrib>Garfias, Y.</creatorcontrib><title>Overexpression of peroxiredoxin 2 in pterygium. A proteomic approach</title><title>Experimental eye research</title><addtitle>Exp Eye Res</addtitle><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.</description><subject>Adult</subject><subject>Amino Acid Sequence</subject><subject>Blotting, Western</subject><subject>Conjunctiva - enzymology</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Eye Proteins - chemistry</subject><subject>Eye Proteins - genetics</subject><subject>Eye Proteins - metabolism</subject><subject>Female</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Isoelectric Focusing</subject><subject>Male</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Oxidation-Reduction</subject><subject>oxidative stress</subject><subject>peroxiredoxin 2</subject><subject>Peroxiredoxins - chemistry</subject><subject>Peroxiredoxins - genetics</subject><subject>Peroxiredoxins - metabolism</subject><subject>Proteomics</subject><subject>pterygium</subject><subject>Pterygium - enzymology</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><issn>0014-4835</issn><issn>1096-0007</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UE1PwzAMjRCIjcEf4IB65NKSNEnTSVwmvqVJu-wepYkLmdamJO20_XtSbXBEsp4t6_nZfgjdEpwRTIqHTQZ78FmOCc1wDEzO0JTgeZFijMU5msYOS1lJ-QRdhbCJXcoEu0STnLL5XAgxRc-rHXjYdx5CsK5NXJ104N3eejAR2yRPInQ9-MOnHZosWSSddz24xupEdbFW-usaXdRqG-DmlGdo_fqyfnpPl6u3j6fFMtWUF33Kx6Um5zqeVWqDOQalWGVKUxVElSVVXOWVIQUlSnMqRM0KUkaoclNBSWfo_igbt34PEHrZ2KBhu1UtuCFIQhnnhBIsIjU_UrV3IXioZedto_xBEixH8-RGjubJ0TyJY8Q8Q3cn_aFqwPyN_LoVCY9HAsQndzaOB22h1WCiXbqXxtn_9H8APOSAOw</recordid><startdate>201305</startdate><enddate>201305</enddate><creator>Bautista-de Lucio, V.M.</creator><creator>López-Espinosa, N.L.</creator><creator>Robles-Contreras, A.</creator><creator>Pérez-Cano, H.J.</creator><creator>Mejía-López, H.</creator><creator>Mendoza, G.</creator><creator>Jiménez-Martínez, M.C.</creator><creator>Garfias, Y.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201305</creationdate><title>Overexpression of peroxiredoxin 2 in pterygium. A proteomic approach</title><author>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.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-54997d25c0148cd050eaa4bd8db61a883a5a2bd1631ac5377f4618f46b2dbe83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adult</topic><topic>Amino Acid Sequence</topic><topic>Blotting, Western</topic><topic>Conjunctiva - enzymology</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Eye Proteins - chemistry</topic><topic>Eye Proteins - genetics</topic><topic>Eye Proteins - metabolism</topic><topic>Female</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Isoelectric Focusing</topic><topic>Male</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Oxidation-Reduction</topic><topic>oxidative stress</topic><topic>peroxiredoxin 2</topic><topic>Peroxiredoxins - chemistry</topic><topic>Peroxiredoxins - genetics</topic><topic>Peroxiredoxins - metabolism</topic><topic>Proteomics</topic><topic>pterygium</topic><topic>Pterygium - enzymology</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bautista-de Lucio, V.M.</creatorcontrib><creatorcontrib>López-Espinosa, N.L.</creatorcontrib><creatorcontrib>Robles-Contreras, A.</creatorcontrib><creatorcontrib>Pérez-Cano, H.J.</creatorcontrib><creatorcontrib>Mejía-López, H.</creatorcontrib><creatorcontrib>Mendoza, G.</creatorcontrib><creatorcontrib>Jiménez-Martínez, M.C.</creatorcontrib><creatorcontrib>Garfias, Y.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental eye research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bautista-de Lucio, V.M.</au><au>López-Espinosa, N.L.</au><au>Robles-Contreras, A.</au><au>Pérez-Cano, H.J.</au><au>Mejía-López, H.</au><au>Mendoza, G.</au><au>Jiménez-Martínez, M.C.</au><au>Garfias, Y.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overexpression of peroxiredoxin 2 in pterygium. A proteomic approach</atitle><jtitle>Experimental eye research</jtitle><addtitle>Exp Eye Res</addtitle><date>2013-05</date><risdate>2013</risdate><volume>110</volume><spage>70</spage><epage>75</epage><pages>70-75</pages><issn>0014-4835</issn><eissn>1096-0007</eissn><abstract>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.</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> |
fulltext | fulltext |
identifier | ISSN: 0014-4835 |
ispartof | Experimental eye research, 2013-05, Vol.110, p.70-75 |
issn | 0014-4835 1096-0007 |
language | eng |
recordid | cdi_proquest_miscellaneous_1345513107 |
source | MEDLINE; Elsevier ScienceDirect Journals |
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 |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T23%3A38%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Overexpression%20of%20peroxiredoxin%202%20in%20pterygium.%20A%20proteomic%20approach&rft.jtitle=Experimental%20eye%20research&rft.au=Bautista-de%20Lucio,%20V.M.&rft.date=2013-05&rft.volume=110&rft.spage=70&rft.epage=75&rft.pages=70-75&rft.issn=0014-4835&rft.eissn=1096-0007&rft_id=info:doi/10.1016/j.exer.2013.03.001&rft_dat=%3Cproquest_cross%3E1345513107%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1345513107&rft_id=info:pmid/23499777&rft_els_id=S0014483513000559&rfr_iscdi=true |