Interphotoreceptor matrix domains ensheath vertebrate cone photoreceptor cells.
Interphotoreceptor matrix domains ensheath vertebrate cone photoreceptor cells.
复制标题
DOI：
--
复制
发表时间：
1986-02
影响因子：
4.4
通讯作者：
Lincoln V. Johnson;G. Hageman;J. Blanks
中科院分区：
文献类型：
--
作者：
Lincoln V. Johnson;G. Hageman;J. Blanks
视网膜感光间基质（IPM）占据神经视网膜和视网膜色素上皮（RPE）（两种神经外胚层来源的上皮）之间的空间。虽然 IPM 似乎是感光细胞接收重要代谢因子的主要途径，但对其结构和功能知之甚少。这里报道的研究描述了猪、猴和人类视网膜中 IPM 的特殊结构域的存在，这些特殊结构域包裹着视锥细胞，而不是视杆细胞、内节和外节。这些视锥细胞外基质鞘在化学和结构上与 IPM 的其余部分不同，正如它们与凝集素花生凝集素 (PNA) 的特异性结合及其在视网膜物理解离过程中的结构稳定性所揭示的那样。生化研究表明，锥体基质鞘的 PNA 结合成分是胰蛋白酶敏感的糖蛋白。这些结构可能在为视锥细胞光感受器建立专门的微环境、维持视锥细胞外节的正确方向和/或促进视锥细胞-RPE相互作用方面发挥作用。
The retinal interphotoreceptor matrix (IPM) occupies the space between the neural retina and the retinal pigmented epithelium (RPE), two neuroectoderm-derived epithelia. While the IPM appears to be a major route by which photoreceptor cells receive vital metabolic factors, relatively little is known concerning its structure and function. The studies reported here describe the presence of specialized domains of the IPM that ensheath cone, but not rod, inner and outer segments in pig, monkey, and human retinae. These cone extracellular matrix sheaths are chemically and structurally distinct from the remainder of the IPM as revealed by their specific binding of the lectin peanut agglutinin (PNA) and their structural stability during physical dissociation of the retina. Biochemical studies suggest that the PNA-binding components of the cone matrix sheaths are trypsin-sensitive glycoproteins. These structures may play a role in establishing a specialized microenvironment for cone photoreceptors, maintaining proper orientation of cone outer segments, and/or facilitating cone-RPE interactions.