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J.J. Enghild, I.B. Thogersen, H. Karring, G.K. Klintworth, T. Moller-Pedersen; The Corneal Proteome . Invest. Ophthalmol. Vis. Sci. 2003;44(13):838.
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Purpose: Proteins, such as hormones, antibodies, enzymes, and structural components of the extracellular matrix, are all responsible for biological activity. Although the genes provide the "blue print&rsquotdbl;, the proteins carry out the work. Thus, pathological processes can be described as aberrations in the normal protein function. Proteomics is the systematic identification and characterization of all proteins in a given biological system. The information obtained from such analyses may reveal how proteins interact to maintain homostasis, and may help to understand the underlying causes of disease and to develop new drugs and diagnostic procedures. The purpose of this study is to describe the proteome of the normal human cornea. Methods: All proteins were extracted from 8 normal human corneas (aged 22-84 years) containing all layers: epithelium, Bowman's layer, stroma, Descemet's membrane, and endothelium. Proteins were separated and quantified using liquid chromatography and 2D-gel electrophoresis. Proteins were identified and characterized using mass spectrometry. Results: More than 100 different proteins and many isoforms were found in the normal human cornea. Interestingly, the corneal proteome did not change much with age. Visit www.corneaproteomics.org for more information. Conclusions: These data characterize the normal protein expression of the healthy human cornea and provide a basis for further analysis of disease processes.
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