Proteomic analysis of the soluble fraction from human corneal fibroblasts with reference to ocular transparency
(2004) In Molecular & Cellular Proteomics 3(7). p.660-674- Abstract
- 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,... (More)
- 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 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 one-dimensional 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 two-dimensional 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1131069
- author
- Karring, Henrik LU ; Thogersen, Ida B ; Klintworth, Gordon K ; Enghild, Jan J and Moller-Pedersen, Torben
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular & Cellular Proteomics
- volume
- 3
- issue
- 7
- pages
- 660 - 674
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:15054125
- scopus:4043144280
- ISSN
- 1535-9484
- DOI
- 10.1074/mcp.M400016-MCP200
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)
- id
- 74a4fb49-8e25-4632-815c-1e3ccdd64531 (old id 1131069)
- date added to LUP
- 2016-04-01 12:21:00
- date last changed
- 2022-03-13 08:44:59
@article{74a4fb49-8e25-4632-815c-1e3ccdd64531,
abstract = {{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 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 one-dimensional 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 two-dimensional 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.}},
author = {{Karring, Henrik and Thogersen, Ida B and Klintworth, Gordon K and Enghild, Jan J and Moller-Pedersen, Torben}},
issn = {{1535-9484}},
language = {{eng}},
number = {{7}},
pages = {{660--674}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Molecular & Cellular Proteomics}},
title = {{Proteomic analysis of the soluble fraction from human corneal fibroblasts with reference to ocular transparency}},
url = {{http://dx.doi.org/10.1074/mcp.M400016-MCP200}},
doi = {{10.1074/mcp.M400016-MCP200}},
volume = {{3}},
year = {{2004}},
}