Abstract
Lack of tyrosine O Sulfation compromises both rod and cone electroretinographic responses emphasizing the importance of this post-translational modification for vision. To identify tyrosine sulfated proteins in retina, cow retinal lysates were subjected to immunoaffinity purification using an anti-sulfotyrosine antibody. The tyrosine sulfated proteins were eluted from the column using a sulfotyrosine pentapeptide and identified using mass spectrometry. Similarly, tyrosine sulfated proteins secreted by the 661W cell line were identified. Proteins identified were vitronectin, fibronectin, fibulin 2, nidogen, collagen V alpha 2, complement component 3 and C4 and fibrinogen beta. All proteins were subjected to analysis by ‘Sulfinator’ to determine potential sulfated tyrosines.
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Acknowledgments
This study was supported by grants from Oklahoma Center for Advancement of Science and Technology (OCAST to YK), Foundation Fighting Blindness (MRA), the National Eye Institute EY018137 (MRA) and a P30EY021725. The funders had no role in design, collection and analysis of data, decision to publish, or manuscript preparation.
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Kanan, Y., Al-Ubaidi, M. (2016). Identification of Tyrosine O Sulfated Proteins in Cow Retina and the 661W Cell Line. In: Bowes Rickman, C., LaVail, M., Anderson, R., Grimm, C., Hollyfield, J., Ash, J. (eds) Retinal Degenerative Diseases. Advances in Experimental Medicine and Biology, vol 854. Springer, Cham. https://doi.org/10.1007/978-3-319-17121-0_86
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DOI: https://doi.org/10.1007/978-3-319-17121-0_86
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