Project description:The sclera provides an opaque protective coat for five-sixths of the surface of the human eye. A detailed investigation of the proteome of the normal human sclera may provide insights into the biology and pathophysiology of the sclera. We conducted an in-depth proteomic analysis of sclera from five adults. Proteins were fractionated using SDS-PAGE. After in-gel digestion, peptides were analyzed using LC-MS/MS on an Orbitrap Elite mass spectrometer. We identified 1952 non-redundant proteins in the human sclera, including 18 different collagen protein chains (types 1, II, III, IV, VI, VIII, X, XII, XIV, XV, XVI, XVIII), proteins of the small leucine-rich proteoglycan family (decorin, biglycan, lumican, keratocan, prolargin, fibromodulin, and mimecan), non-collagenous glycoproteins (fibronectin, vitronectin, and laminin), extracellular matrix proteins (thrombospondins 1, 2, 3, 4, dystroglycan, and transgelins 1, 2, 3), matrix metalloproteinases 3 and 14, matrix metalloproteinase inhibitors 1, 2, and 3, and integrins alpha-V, alpha-1, alpha-2, beta-1, beta-2, and beta-5.
2022-03-01 | PXD004223 | Pride