April 2014
Volume 55, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2014
Proteomic analysis in pterygium
Author Affiliations & Notes
  • Sun Woong Kim
    Ophthalmology, Hando general hospital, Ansan, Republic of Korea
  • Taiyoun Rhim
    Bioengineering, Hanyang University, Seoul, Republic of Korea
  • Footnotes
    Commercial Relationships Sun Woong Kim, None; Taiyoun Rhim, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science April 2014, Vol.55, 394. doi:
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      Sun Woong Kim, Taiyoun Rhim; Proteomic analysis in pterygium. Invest. Ophthalmol. Vis. Sci. 2014;55(13):394.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract
 
Purpose
 

To identify differentially expressed proteins in 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 pterygia and healthy conjunctiva were analyzed by one-dimensional electrophoresis, and protein bands of interest were excised and subjected to LC-MS/MS analysis using Thermo’s Finnigan ProteomeX workstation LTQ linear IT MS (Thermo Electron, San Jose, CA) equipped with an NSI source (San Jose, CA). Using bioinformatics, differentially expressed proteins were classified, and three proteins closely involved in the response to oxidative stress were selected for further validation. Differential expression of these proteins was confirmed by Western blot and immunohistochemistry.

 
Results
 

A web-based gene ontology program, DAVID, was used to classify 230 proteins that were differentially expressed in pterygial tissues. Among them, we chose three proteins, aldehyde dehydrogenase, dimeric NADP-preferring (ALDH3A1), protein disulfide-isomerase A3 (PDIA3) and peroxiredoxin-2 (PRDX2), that were significantly overexpressed in pterygium and further overexpressed in recurrent pterygium. Immunohistochemistry and Western blot analysis confirmed that these three proteins were mainly detected in the basal epithelial layer, and their expression was significantly increased in pterygium compared to normal conjunctiva.

 
Conclusions
 

This study reported increased expressions of ALDH3A1, PDIA3, and PRDX2 in pterygia using a proteomic approach. These proteins are presumed to have a protective role against oxidative stress-induced apoptosis. This result is consistent with the hypothesis that oxidative stress is a significant factor in the pathogenesis of pterygium.

 
 
Representative images of Western blot analysis, showing increased expression of Aldehyde dehydrogenase, dimeric NADP-preferring (ALDH3A1), Protein disulfide-isomerase A3 (PDIA3) and Peroxiredoxin-2 (PRDX2) in pterygium compared to healthy conjunctiva.
 
Representative images of Western blot analysis, showing increased expression of Aldehyde dehydrogenase, dimeric NADP-preferring (ALDH3A1), Protein disulfide-isomerase A3 (PDIA3) and Peroxiredoxin-2 (PRDX2) in pterygium compared to healthy conjunctiva.
 
 
Immunolocalization of Aldehyde dehydrogenase, dimeric NADP-preferring (ALDH3A1), Protein disulfide-isomerase A3 (PDIA3), and Peroxiredoxin-2 (PRDX2) in pterygium.
 
Immunolocalization of Aldehyde dehydrogenase, dimeric NADP-preferring (ALDH3A1), Protein disulfide-isomerase A3 (PDIA3), and Peroxiredoxin-2 (PRDX2) in pterygium.
 
Keywords: 480 cornea: basic science • 665 pterygium • 663 proteomics  
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