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Kyong Jin Cho, Jee won Mok, Chang Rae Roh, Yong Soo Byun, Kyung Sun Na, So Hyang Chung, Choun-ki Joo; Corneal Proteomic Analysis of Patients with Keratoconus. Invest. Ophthalmol. Vis. Sci. 2011;52(14):1110.
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© ARVO (1962-2015); The Authors (2016-present)
We investigated the proteomic profiles of the whole cornea tissue of keratoconus to increase our understanding of the pathogenesis of keratoconus.
Total proteins were extracted from keratoconic cornea and normal cornea and separated by two-dimensional gel electrophoresis (2-DE) and identified 150 differential protein spots under the experimental conditions. All of the 150 protein spots were analyzed the peptide mass finger printing (PMF) with the 4700 MALDI-TOF/TOF mass spectrometer to deduce their possible functions.
Of the 150 protein spots, we identified 100 spots that demonstrated a significant differences between keratoconus and normal cornea with a ProtScore (>or=2). The intensity of 37 spots were markedly higher in keratoconus than normal cornea (>2 folds), and 14 spots were detected only in keratoconic cornea. Key proteins we recognized included type VI collagen alpha 2 chain, Transforming growth factor-beta-induced protein ig-h3, nebulin, spectrin, alpha-enolase, keratin, annexin, peroxiredoxin-6, type VI collagen alpha 2 chain precursor, carbonic anhydrase 1, keratin 3, 5, 14, 79, type I cytoskeletal 12, decorin, aldehyde dehydrogenase, dystonin, transformation/transcription domain-associated protein variant.
From our study, which used proteomic approaches, we have presented the finding of proteins differentially expressed in the keratoconus patients. The identified proteins corresponded to molecules belonging to Cell junction, cell migration, ECM related cytoskeleton, antioxidant protein and transcription/transformation. Therefore it is suggested that our findings could contribute to the knowledge for the further understanding of pathogenesis of keratoconus.
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