LECTIN BINDING OF THE INTERPHOTORECEPTOR MATRIX DURING RETINAL DEVELOPMENT IN NORMAL AND RCS RATS

The retinas of both normal and Royal College of Surgeons (RCS) rats with inherited retinal dystrophy have been examined using lectin histochemistry to determine the developmental and degenerative changes of the glycoconjugates in the interphotoreceptor matrix (IPM) between postnatal day (P) 10 and P25, when the adult lectin binding patterns are seen in normal rats. Wheat germ agglutinin (WGA; recognizing sialic acid and/or N-acetyl-D-glucosamine) bound to the apical surface of the retinal pigment epithelium (RPE) sparsely at P10 and prominently at P12 in both strains. In both strains at P14, WGA also stained the basal outer segment zone at the inner segment-outer segment junction. Between P14 and P16 in both strains, there was a dramatic increase in the binding of the interstitial region, the space alongside the outer segments and between the apical and basal outer segment zones. The binding pattern of WGA in normal rats remained basically unchanged from P16 to P25, although the intensity of binding was increased somewhat. Ricinus communis agglutinin-1 (RCA-1; specific for galactosyl residues) bound to the outer segment zone prominently and diffusely with increasing intensity with age at P10, P12 and P14 in both strains. At P16 and older, the intense binding of the interstitial zone was dramatically reduced and the RCA-1 bound primarily to the inner and outer segment junctional region, with weak binding to the apical surface of the RPE in both strains. At P25, the binding of the inner and outer segment junctional region was even more restricted, limited to punctate sites in this zone in normal rats and almost missing in RCS rats. These findings demonstrate that a substantial change in the glycoconjugates of the IPM occurs between P14 and P16 in the retinas of both normal and RCS rats, followed by more subtle changes between P16 and P25. © 1990 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.