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Submitted on January 31, 2004
Revised on March 30, 2004
Accepted on March 30, 2004

Proteomic analysis of the soluble fraction from human corneal fibroblasts with reference to ocular transparency

Henrik Karring, Ida B. Thøgersen, Gordon K. Klintworth, Jan J. Enghild, and Torben Møller-Pedersen

Ophthalmology, Aarhus University Hospital, Aarhus DK-8000 C

Corresponding Author: torbenmp{at}akhphd.au.dk

The transparent corneal stroma contains a population of corneal fibroblasts termed keratocytes, which are interspersed between the collagen lamellae. Under normal conditions, the keratocytes are quiescent and transparent. However, after corneal injury the keratocytes become activated and transform into backscattering wound-healing fibroblasts resulting in corneal opacification. At present, the most popular hypothesis suggests that particular abundant water-soluble proteins called enzyme-crystallins are involved in maintaining corneal cellular transparency. Specifically, corneal haze development is thought to be related to low levels of cytoplasmic enzyme-crystallins in reflective corneal fibroblasts. To further investigate this hypothesis we have used a proteomic approach to identify and quantify the most abundant water-soluble proteins in serum-cultured human corneal fibroblasts that represent an in vitro model of the reflective wound-healing keratocyte phenotype. Densitometry of 1D gels revealed that no single protein isoform exceeded 5% of the total water-soluble protein fraction, which is the qualifying property of a corneal enzyme-crystallin according to the current definition. This result indicates that wound-healing corneal fibroblasts do not contain enzyme-crystallins. A total of 254 protein identifications from 2D gels were performed representing 118 distinct proteins. Proteins protecting against oxidative stress and protein misfolding were prominent suggesting that these processes may participate in the generation of cytoplasmic light-scattering from corneal fibroblasts.


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