Nepafenac was more effective than fluorometholone in preventing angiographic CME and BAB disruption, and results indicate nepafenac leads to more rapid visual recovery.

Heparan sulphate 6- O -sulphotransferase (HS6ST) catalyses the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in HS. We previously described the occurrence of three isoforms of mouse HS6ST, mHS6ST-1, -2, and -3 [Habuchi, Tanaka, Habuchi, Yoshida, Suzuki, Ban and Kimata (2000) J. Biol. Chem. 275, 2859-2868]. In the present study, we have characterized HS6ST-2 and HS6ST-1 human isologues, including their chromosomal localizations. In the process of their cDNA cloning, we found two forms of HS6ST-2: the original (hHS6ST-2) and a short form (hHS6ST-2S) with 40 amino acids deleted. Both hHS6ST-2 and hHS6ST-2S catalysed the same sulphation reaction, but their preferences for sulphation sites in HS substrates were different. Dot-blot analysis of the two forms showed that the original form was exclusively expressed in adult and foetal brain tissues, whereas the short form was expressed preferentially in ovary, placenta and foetal kidney, suggesting that the expression of two forms of hHS6ST-2 is strictly regulated to yield tissue-dependent differences in the fine structure of HS. A refined analysis of their reaction products has led us to another finding, that HS6STs could also transfer sulphate to N -sulphoglucosamine residues located at the non-reducing terminal of HS with high affinity.

MY-174 is an IgM class monoclonal antibody originally established against chick PG-M/versican. The antibody specifically stains the photoreceptor layer, where we recently reported an absence of PG-M/versican. In this study, we re-characterized the antibody and identified the molecule that reacts to MY-174 at the photoreceptor layer. Immunohistochemistry localized the antigen to the matrix surrounding photoreceptors. A variety of glycosidase digestions showed that the antigen is the 150-kDa glycoprotein that has sialylated N-and O-linked glycoconjugates having a molecular mass of more than 30-kDa. The peptide sequences obtained from purified MY-174 antigen showed we had sequenced a full-length cDNA with an open reading frame of 2787 base pairs, encoding a polypeptide of 928 amino acids, with 56 and 54% identities to human and mouse sialoprotein associated with cones and rods (SPACRs), respectively, and with the structural features observed in SPACRs. The specific sialylated O-glycoconjugates here are involved in the epitope structure for MY-174. SPACR first appeared by embryonic days 15-16, and expression increased with developmental age, paralleling the adhesion between neural retina and retinal pigment epithelium. Thus, we concluded that the MY-174 antigen at the photoreceptor layer, a developmentally regulated glycoprotein, is identical to chick SPACR and may be involved in a novel system mediating adhesion between neural retina and retinal pigment epithelium.MY-174, a monoclonal antibody, has been shown to recognize chick PG-M/versican (1), a member of the hyaluronan-binding chondroitin sulfate proteoglycan family (2-4). In the eye, MY-174 specifically stains the photoreceptor layer (1). However, recently we demonstrated an absence of PG-M/versican at the chick photoreceptor layer using a polyclonal antibody that recognizes all alternatively spliced forms of PG-M/versican (5). These inconsistent results suggest that MY-174 does not recognize PG-M/versican but another molecule in the photoreceptor layer.The IPM (interphotoreceptor matrix), 1 resides in an extracellular compartment between the outer limiting membrane of the neural retina and apical surface of the retinal pigment epithelium and is composed of proteins, glycoproteins, proteoglycans, and glycosaminoglycans (6, 7). A variety of important reactions relating to vision, including visual pigment chromophore exchange, metabolite trafficking, photoreceptor alignment, and membrane turnover, is thought to be mediated by the IPM (8). However, one of the most essential functions of IPM is that of a biological glue for retinal adhesion through its viscous adhesive properties (9, 10). Retinal adhesiveness can be weakened by treatments with enzymes such as neuraminidase, hyaluronidase, and chondroitinase ABC (11,12). Intracellular blocking of glycosylation with xyloside also prevents the secretion of proteoglycans and results in retinal detachment (13). These results suggest that the proteoglycans, glycosaminoglycans, or glycoproteins of the IPM are involved in...

Mr. Shibuya is an employee of Hoya Corporation Medical Division. No other author has a financial or proprietary interest in any material or method mentioned.