Fibulin 2, a tyrosine O-sulfated protein, is up-regulated following retinal detachment [Glycobiology and Extracellular Matrices]

April 1st, 2014 by Kanan, Y., Brobst, D., Han, Z., Naash, M. I., Al-Ubaidi, M. R.

Retinal detachment is the physical separation of the retina from the retinal pigment epithelium. It occurs during aging, trauma or during a variety of retinal disorders such as age-related macular degeneration, diabetic retinopathy, retinopathy of prematurity or as complication following cataract surgery. This report investigates the role of fibulin 2, an extracellular component, in retinal detachment. A major mechanism for detachment resolution is enhancement of cellular adhesion between the retina and the retinal pigment epithelium and prevention of its cellular migration. This report shows that fibulin 2 is mainly present in the RPE, Bruch s membrane, choriocapillary, and to a lesser degree in retina. In vitro studies revealed the presence of two isoforms for fibulin 2. The small isoform located inside the cell while the large isoform present inside and outside the cells. Furthermore, fibulin 2 is post-translationally modified by tyrosine sulfation and the sulfated isoform is present outside the cell while the unsulfated pool is internally located. Interestingly, sulfated fibulin 2 significantly reduced the rate of cellular growth and migration. Finally, levels of fibulin 2 dramatically increased in the retinal pigment epithelium following retinal detachment, suggesting a direct role for fibulin 2 in the re-attachment of the retina to the retinal pigment epithelium. Understanding the role of fibulin 2 in enhancing retinal attachment is likely to help improve the current therapies or allow the development of new strategies for the treatment of this sight-threatening condition