Protein tyrosine-O-sulfation (aka sulfonation, sulfation) has been recently identified as an important posttranslational modification for vision. In the absence of sulfation, rod and cone ERGs are reduced and vision is compromised. With the goal of identifying the sulfated retinal proteins in the eye, various bovine ocular tissues were examined. To that end, the cornea, aqueous humor, lens, iris, vitreous humor, retina, RPE, and sclera were examined for the presence of sulfated proteins using the PSG2 antibody, which has previously been used to identify and isolate sulfated proteins from various tissues. Data presented show that the vitreous humor is the richest source of sulfated proteins in the eye while the lens expressed the least. Furthermore, the sulfated proteins in the retinal pigment epithelium and retina were either soluble members of the extracellular matrix and/or membrane-associated proteins. Future plans are directed towards the identification of the different sulfated proteins by immunoaffinity purification with the PSG2 antibody and the determination of the role of sulfation in the function of these ocular proteins.
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This study was partly supported by grants from the National Center For Research Resources (P20RR017703), the National Eye Institute P30EY12190, Oklahoma Center for the Advancement of Science and Technology (OCAST) (YK), R01 EY14052 and R01 EY018137 (MRA), FFB (MRA), Hope For Vision, NY (MRA), and the Reynolds Oklahoma Center on Aging (MRA).
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