Retinoschisin also known as X-linked juvenile retinoschisis protein is a lectin[5][6] that in humans is encoded by the RS1 gene.[7]
It is a soluble, cell-surface protein that plays an important role in the maintenance of the retina where it is expressed and secreted by retinal bipolar cells and photoreceptors,[8][9] as well as in the pineal gland.[10] Retinoschisin (RS1) is encoded by the gene RS1 located on the X chromosome at p22.1.[7] Young males who have an RS1 mutation are susceptible to retinoschisis, and X-linked eye disease which causes macular degeneration and can lead to a loss of vision.[5][9]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000102104 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031293 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b Vijayasarathy C, Ziccardi L, Sieving PA (2012). "Biology of Retinoschisin". Retinal Degenerative Diseases. Advances in Experimental Medicine and Biology. Vol. 723. pp. 513–8. doi:10.1007/978-1-4614-0631-0_64. ISBN 978-1-4614-0630-3. PMC 3475158. PMID 22183371.
- ^ Wu WW (October 2005). RS1 structure-function relationships: roles in retinal adhesion and X-linked retinoschisis (Ph.D. thesis). The University of British Columbia.
- ^ a b Sauer CG, Gehrig A, Warneke-Wittstock R, Marquardt A, Ewing CC, Gibson A, Lorenz B, Jurklies B, Weber BH (October 1997). "Positional cloning of the gene associated with X-linked juvenile retinoschisis". Nature Genetics. 17 (2): 164–70. doi:10.1038/ng1097-164. PMID 9326935. S2CID 7829510.
- ^ Tolun G, Vijayasarathy C, Huang R, Zeng Y, Li Y, Steven AC, Sieving PA, Heymann JB (May 2016). "Paired octamer rings of retinoschisin suggest a junctional model for cell-cell adhesion in the retina". Proceedings of the National Academy of Sciences of the United States of America. 113 (19): 5287–92. Bibcode:2016PNAS..113.5287T. doi:10.1073/pnas.1519048113. PMC 4868477. PMID 27114531.
- ^ a b Kotova S, Vijayasarathy C, Dimitriadis EK, Ikonomou L, Jaffe H, Sieving PA (August 2010). "Retinoschisin (RS1) interacts with negatively charged lipid bilayers in the presence of Ca2+: an atomic force microscopy study". Biochemistry. 49 (33): 7023–32. doi:10.1021/bi1007029. PMC 2929131. PMID 20677810.
- ^ Plössl K, Royer M, Bernklau S, Tavraz NN, Friedrich T, Wild J, Weber BH, Friedrich U (August 2017). "Retinoschisin is linked to retinal Na/K-ATPase signaling and localization". Molecular Biology of the Cell. 28 (16): 2178–2189. doi:10.1091/mbc.e17-01-0064. PMC 5531734. PMID 28615319.