A dataset of human cornea proteins identified by Peptide mass fingerprinting and tandem mass spectrometry
(2005) In Molecular & Cellular Proteomics 4(9). p.1406-1408- Abstract
- Diseases of the cornea are extremely common and cause severe visual impairment worldwide. To explore the basic molecular mechanisms involved in corneal health and disease, the present study characterizes the proteome of the normal human cornea. All proteins were extracted from the central 7-mm region of 12 normal human donor corneas containing all layers: epithelium, Bowman's layer, stroma, Descemet's membrane, and endothelium. Proteins were fractionated and identified using two different procedures: (i) two-dimensional gel electrophoresis and protein identification by MALDI-MS and (ii) strong cation exchange or one-dimensional SDS gel electrophoresis followed by LC-MS/MS. All together, 141 distinct proteins were identified of which 99 had... (More)
- Diseases of the cornea are extremely common and cause severe visual impairment worldwide. To explore the basic molecular mechanisms involved in corneal health and disease, the present study characterizes the proteome of the normal human cornea. All proteins were extracted from the central 7-mm region of 12 normal human donor corneas containing all layers: epithelium, Bowman's layer, stroma, Descemet's membrane, and endothelium. Proteins were fractionated and identified using two different procedures: (i) two-dimensional gel electrophoresis and protein identification by MALDI-MS and (ii) strong cation exchange or one-dimensional SDS gel electrophoresis followed by LC-MS/MS. All together, 141 distinct proteins were identified of which 99 had not previously been identified in any mammalian corneas by direct protein identification methods. The characterized proteins are involved in many processes including antiangiogenesis, antimicrobial defense, protection from and transport of heme and iron, tissue protection against UV radiation and oxidative stress, cell metabolism, and maintenance of intracellular and extracellular structures and stability. This proteome study of the healthy human cornea provides a basis for further analysis of corneal diseases and the design of bioengineered corneas. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1134231
- author
- Karring, Henrik LU ; Thogersen, Ida B ; Klintworth, Gordon K ; Moller-Pedersen, Torben and Enghild, Jan J
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular & Cellular Proteomics
- volume
- 4
- issue
- 9
- pages
- 1406 - 1408
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:15911533
- scopus:26844575542
- pmid:15911533
- ISSN
- 1535-9484
- DOI
- 10.1074/mcp.D500003-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
- 22193647-1275-479a-82ed-72af60d04262 (old id 1134231)
- date added to LUP
- 2016-04-01 12:38:46
- date last changed
- 2022-01-27 07:55:57
@article{22193647-1275-479a-82ed-72af60d04262,
abstract = {{Diseases of the cornea are extremely common and cause severe visual impairment worldwide. To explore the basic molecular mechanisms involved in corneal health and disease, the present study characterizes the proteome of the normal human cornea. All proteins were extracted from the central 7-mm region of 12 normal human donor corneas containing all layers: epithelium, Bowman's layer, stroma, Descemet's membrane, and endothelium. Proteins were fractionated and identified using two different procedures: (i) two-dimensional gel electrophoresis and protein identification by MALDI-MS and (ii) strong cation exchange or one-dimensional SDS gel electrophoresis followed by LC-MS/MS. All together, 141 distinct proteins were identified of which 99 had not previously been identified in any mammalian corneas by direct protein identification methods. The characterized proteins are involved in many processes including antiangiogenesis, antimicrobial defense, protection from and transport of heme and iron, tissue protection against UV radiation and oxidative stress, cell metabolism, and maintenance of intracellular and extracellular structures and stability. This proteome study of the healthy human cornea provides a basis for further analysis of corneal diseases and the design of bioengineered corneas.}},
author = {{Karring, Henrik and Thogersen, Ida B and Klintworth, Gordon K and Moller-Pedersen, Torben and Enghild, Jan J}},
issn = {{1535-9484}},
language = {{eng}},
number = {{9}},
pages = {{1406--1408}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Molecular & Cellular Proteomics}},
title = {{A dataset of human cornea proteins identified by Peptide mass fingerprinting and tandem mass spectrometry}},
url = {{http://dx.doi.org/10.1074/mcp.D500003-MCP200}},
doi = {{10.1074/mcp.D500003-MCP200}},
volume = {{4}},
year = {{2005}},
}