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Molecular & Cellular Proteomics 4:1406-1408, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.



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From the
Center for Insoluble Protein Structure (inSPIN) at the Department of Molecular Biology, Science Park, University of Aarhus, Gustav Wieds Vej 10c, 8000 Aarhus C, Denmark, the
Departments of Pathology and Ophthalmology, Duke University Medical Center, Durham, North Carolina 27710, and the ¶ Department of Ophthalmology, Aarhus University Hospital, Nørrebrogade 44, 8000 Aarhus C, Denmark
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, Bowmans layer, stroma, Descemets 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.
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