TY - JOUR
T1 - Protein tyrosine-O-sulfation in the retina
AU - Kanan, Yogita
AU - Hoffhines, Adam
AU - Rauhauser, Alysha
AU - Murray, Anne
AU - Al-Ubaidi, Muayyad R.
N1 - Funding Information:
The project described was supported by a grant from the Foundation Fighting Blindness (MRA) and partially supported by grants from the National Center For Research Resources [P20RR017703] and the National Eye Institute [P30EY12190] and [R01EY14052] (MRA), [R01EY018137] (MRA), Hope For Vision (MRA), Reynolds Oklahoma Center on Aging (MRA), and the Knights Templar Eye Foundation, Inc. (YK). The content is solely the responsibility of the authors and does not necessarily represent the official views of NIH or any of its institutes.
PY - 2009/10
Y1 - 2009/10
N2 - Tyrosine-O-sulfation, a post-translational modification, is catalyzed by two independent tyrosylprotein sulfotransferases (TPSTs). As an initial step towards understanding the role of TPSTs in retinal function, this study was undertaken to determine the extent to which tyrosine-O-sulfation of proteins is utilized in the retina. A previously characterized anti-sulfotyrosine antibody was used to determine the presence and localization of tyrosine-O-sulfated proteins (TOSPs) in the retina. Using Western blot, RT-PCR and immunohistochemical analyses, we detected TOSPs in the retinas from diverse species, including frog, fish, mouse and human. Some of the variability in the observed sizes of retinal TOSPs in the mouse, at least, may result from differential patterns of glycosylation; however, there seem to be species-specific sulfated retinal proteins as well. TOSPs were detected in most of the retinal layers as well as in the retinal pigment epithelium from human and mouse. Several retinal TOSPs were detected in the inter-photoreceptor matrix, which is consistent with the secreted nature of some sulfated proteins. Transcripts for both TPST-1 and TPST-2 were expressed in both the human and mouse retinas. These data show that retinal protein tyrosine-O-sulfation is highly conserved which suggest a functional significance of these proteins to retinal function and structure.
AB - Tyrosine-O-sulfation, a post-translational modification, is catalyzed by two independent tyrosylprotein sulfotransferases (TPSTs). As an initial step towards understanding the role of TPSTs in retinal function, this study was undertaken to determine the extent to which tyrosine-O-sulfation of proteins is utilized in the retina. A previously characterized anti-sulfotyrosine antibody was used to determine the presence and localization of tyrosine-O-sulfated proteins (TOSPs) in the retina. Using Western blot, RT-PCR and immunohistochemical analyses, we detected TOSPs in the retinas from diverse species, including frog, fish, mouse and human. Some of the variability in the observed sizes of retinal TOSPs in the mouse, at least, may result from differential patterns of glycosylation; however, there seem to be species-specific sulfated retinal proteins as well. TOSPs were detected in most of the retinal layers as well as in the retinal pigment epithelium from human and mouse. Several retinal TOSPs were detected in the inter-photoreceptor matrix, which is consistent with the secreted nature of some sulfated proteins. Transcripts for both TPST-1 and TPST-2 were expressed in both the human and mouse retinas. These data show that retinal protein tyrosine-O-sulfation is highly conserved which suggest a functional significance of these proteins to retinal function and structure.
KW - RPE
KW - post-translation modification
KW - protein sulfation
UR - http://www.scopus.com/inward/record.url?scp=69749091703&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=69749091703&partnerID=8YFLogxK
U2 - 10.1016/j.exer.2009.05.010
DO - 10.1016/j.exer.2009.05.010
M3 - Article
C2 - 19523945
AN - SCOPUS:69749091703
SN - 0014-4835
VL - 89
SP - 559
EP - 567
JO - Experimental eye research
JF - Experimental eye research
IS - 4
ER -