RELATIONSHIP OF MAMMALIAN CONES TO PIGMENT EPIHELIUM

尽管它们的功能和结构相似，但杆和锥体也 表现出显著的形态和生化差异。这些 差异几乎可以肯定地反映了细胞的特殊功能，但 人们仍然对它们知之甚少。在本项目中，锥体的细胞生物学 光感受器及其与视网膜色素上皮的关系 (RPE)，强调了这一点。两者之间的异同 光感受器类将在发育、成熟、退化、 并使用免疫细胞化学、放射自显影、 和凝集素细胞化学技术。此外， 将分析光感受器蛋白的定位和生物合成。 当视网膜实验性地从RPE中分离出来时。比较 灵长类的杆状和锥状外节的再生能力将得到提高。 视蛋白将通过免疫电子显微镜定位在分离的和 再连的视网膜。光受体间视黄醇结合蛋白(IRBP)将 局部化，其生物合成将在正常和分离中进行比较 视网膜。将测试细胞视黄醛结合蛋白(CRALBP) 用作迁移和/或增殖的特定细胞标志物 RPE和Muller细胞。运输的生物合成途径， 锥体外段膜蛋白的插入、扩散 用电子显微镜放射自显影进行分析。凝集素-金偶联物 将被用作超微结构探针来鉴定和量化结合 位于光感受器-RPE界面的部位。最后，分布情况。 光感受器-RPE界面上的糖偶联物及其潜力 在视网膜粘连中的作用，将在使用 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).