Poulsen, Ebbe Toftgaard5; Dyrlund, Thomas F5; Runager, Kasper5; Scavenius, Carsten5; Krogager, Toke Peter5; Hojrup, Peter5; Thøgersen, Ida B5; Sanggaard, Kristian Wejse6; Vorum, Henrik7; Hjortdal, Jesper5; Enghild, Jan Johannes5
1 The Faculty of Medicine, Aalborg University, VBN2 Aalborg University Hospital, The Faculty of Medicine, Aalborg University, VBN3 Klinik Hoved-Orto, The Faculty of Medicine, Aalborg University, VBN4 Øjensygdomme, The Faculty of Medicine, Aalborg University, VBN5 unknown6 Institut for Molekylærbiologi og Genetik - Proteinvidenskab7 Department of Clinical Medicine, The Faculty of Medicine, Aalborg University, VBN
Fuchs' endothelial corneal dystrophy (FECD) is a major corneal disorder affecting the innermost part of the cornea, leading to visual impairment. As the morphological changes in FECD are mainly observed in the extracellular matrix of the Descemet's membrane/endothelial layer we determined the protein profiles of diseased and control tissues using two relative quantitation MS methods. The first quantitation method based on the areas of the extracted ion chromatograms, quantified the 51 and 48 most abundant proteins of the Descemet's membrane/endothelial layer in patient and control tissues, respectively, of which 10 were significantly regulated. The results indicated that the level of type VIII collagen was unaltered even though the protein previously has been implicated in familial early onset forms of the disease. Using the second relative quantitation method iTRAQ we identified 22 differentially regulated proteins, many of which are extracellular proteins known to be involved in proper assembly of the basement membrane in other tissues. In total 26 differentially regulated proteins were identified, of which 6 proteins were regulated by both methods. These results support that the morphological changes observed in FECD is caused in part by an aberrant assembly of the extracellular matrix within the Descemet's membrane/endothelial layer.
Journal of Proteome Research, 2014, Vol 13, Issue 11, p. 4659-4667