Localization and properties of an immunoreactive protein in bovine ciliary body similar to retinal S antigen

Abstract

Immunocytochemical studies showed that monoclonal antibodies to bovine retinal S-antigen recognize an immunoreactive protein present in the bovine ciliary body epithelium. This protein was purified by DEAE-agarose chromatography and found to have a M.W. of 28,000 daltons by SDS polyacrylamide gel electrophoresis. Crude and purified preparations of this protein cross-react with polyclonal antibodies to retinal S-antigen. The relative reactivity of S-antigen monoclonal antibodies to ciliary body protein was determined by ELISA. Lewis rats immunized with crude and purified ciliary body protein failed to develop experimental uveitis. The results indicate that the ciliary body protein contains an antigenic peptide domain which is similar to that of S-antigen but lacks the immunopathogenic domain.

Molecular Evidence That Human Ocular Ciliary Epithelium Expresses Components Involved in Phototransduction

“…Additional studies have also shown the expression in the ocular ciliary epithelium of a visual arrestin (26,27), and the cellular retinaldehyde-binding protein (CRALBP) (28), a component of the visual cycle involved in the transport of 11-cis-retinaldehyde or 11-cis-retinol, retinoid metabolism and visual pigment regeneration (Kennedy et al 1998). These findings are consistent with evidence that the ciliary epithelium and the retina share common genes in part due to their common embryological origin.…”