A dataset of human cornea proteins identified by Peptide mass fingerprinting and tandem mass spectrometry.
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.
Karring
Henrik
H
Center for Insoluble Protein Structure (inSPIN), Department of Molecular Biology, Science Park, University of Aarhus, and the Department of Ophthalmology, Aarhus University Hospital, Nørrebrogade 44, 8000 Aarhus C, Denmark.
Thøgersen
Ida B
IB
Klintworth
Gordon K
GK
Møller-Pedersen
Torben
T
Enghild
Jan J
JJ
D005591:Chemical Fractionation; D002853:Chromatography, Liquid; D003315:Cornea / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000737:chemistry*; D010449:Peptide Mapping; D020543:Proteome / Q000032:analysis*; D014357:Trypsin / Q000494:pharmacology
D008565:Membrane Proteins; D020543:Proteome; D014357:Trypsin