RELATIONSHIP OF MAMMALIAN CONES TO PIGMENT EPITHELIUM

尽管它们在功能和结构上相似，但杆细胞和锥细胞也 表现出显著的形态学和生化差异。 这些 差异几乎肯定反映了细胞的特殊功能， 人们对它们仍然知之甚少。 在这个项目中， 光感受器及其与视网膜色素上皮的关系 (RPE)，强调。 两者的异同 将在发育、成熟、退化 以及使用免疫细胞化学，放射自显影， 和凝集素细胞化学技术。 此外， 光感受器蛋白的定位和生物合成将被分析 当视网膜被实验性地从视网膜色素上皮分离时。 比较 灵长类动物的视杆细胞和视锥细胞外节将产生再生能力。 视蛋白将通过免疫电子显微镜定位在分离的细胞中， 重新附着的视网膜 光感受器间视黄醇结合蛋白（IRBP） 定位，其生物合成将在正常和分离比较， 视网膜 将检测细胞视黄醇结合蛋白（CRALBP） 用作迁移和/或增殖的特异性细胞标记 RPE和Muller细胞。 运输的生物合成途径， 锥外节膜蛋白的插入和扩散， 使用电子显微镜放射自显影进行分析。 凝集素-金结合物 将用作超微结构探针，以识别和定量结合 在光感受器-RPE界面的位点。 最后， 光感受器-RPE界面的糖缀合物及其潜力 在视网膜粘连中的作用，将在用 糖基化选择性抑制剂（衣霉素-B2）。

Despite their functional and structural similarity, rods and cones also exhibit significant morphological and biochemical differences. These differences almost certainly reflect the cells' specialized functions, but they remain poorly understood. In this project, the cell biology of cone photoreceptors, and their relationship to the retinal pigment epithelium (RPE), is emphasized. Similarities and differences between the two photoreceptor classes will be examined in developing, mature, degenerating, and regenerating photoreceptors using immunocytochemical, autoradiographic, and lectin cytochemical techniques. In addition, changes in the localization and biosynthesis of photoreceptor proteins will be analyzed when the retina is experimentally detached from the RPE. Comparisons of regenerative capacity in primate rod and cone outer segments will be made. Opsin will be localized by immunoelectron microscopy in detached and reattached retinas. Interphotoreceptor retinol binding protein (IRBP) will be localized, and its biosynthesis will be compared in normal and detached retinas. Cellular retinaldehyde binding protein (CRALBP) will be tested for use as a specific cellular marker for migrating and/or proliferating RPE and Muller cells. The biosynthetic pathway for the transport, insertion, and diffusion of cone outer segment membrane proteins will be analyzed using electron microscope autoradiography. Lectin-gold conjugates will be used as ultrastructural probes to identify and quantify binding sites at the photoreceptor-RPE interface. Finally, the distribution of glycoconjugates at the photoreceptor-RPE interface, and their potential role in retinal adhesion, will be examined in retinas treated with a selective inhibitor of glycosylation (tunicamycin-B2).