Neural retina and MerTK-independent apical polarity of alphavbeta5 integrin receptors in the retinal pigment epithelium.

Neural retina and MerTK-independent apical polarity of alphavbeta5 integrin receptors in the retinal pigment epithelium.
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DOI:
10.1007/978-1-4419-1399-9_15
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发表时间:
2010
影响因子:
--
通讯作者:
Finnemann, Silvia C.
Finnemann, Silvia C.
中科院分区:
医学4区
文献类型:
--
作者:
Mallavarapu, Mallika;Finnemann, Silvia C.

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眼睛中视网膜色素上皮(RPE)细胞的顶端质膜结构域面向视杆和视锥的外节部分以及视网膜下腔中的感光器间基质。视网膜色素上皮(RPE)的顶面和相邻光感受器之间的两个重要的受体介导的相互作用是粘附,其确保外段对齐和有助于外段更新的脱落外段片段的昼夜吞噬作用。两者都依赖于整合素家族粘附受体αvβ5的顶端分布,因为小鼠中缺乏αvβ5会导致视网膜粘附减弱和异步吞噬作用。随着年龄的增长,αvβ5的缺乏导致有害脂褐素在RPE中积累并导致视力丧失。在这里,我们讨论了三种不同的可能机制,可以产生在RPE中的αvβ5整合素受体的独家顶端分布。(1)αvβ5可能在RPE中位于顶端,因为RPE通常附着于神经视网膜或αvβ5配体特异性地在视网膜下腔中稳定顶端而非基底外侧αvβ5表面受体。(2)αvβ5可能位于RPE的顶端,因为它存在于与吞噬机制的其他组分的复合物中,该复合物在RPE的顶端吞噬表面组装。(3)由于该受体蛋白(特别是其β5整联蛋白亚基)固有的机制,αvβ5可能位于顶端。
The apical plasma membrane domain of retinal pigment epithelial (RPE) cells in the eye faces the outer segment portions of rods and cones and the inter-photoreceptor matrix in the subretinal space. Two important receptor-mediated interactions between the apical surface of the retinal pigment epithelium (RPE) and adjacent photoreceptors are adhesion ensuring outer segment alignment and diurnal phagocytosis of shed outer segment fragments contributing to outer segment renewal. Both depend on the apical distribution of the integrin family adhesion receptor αvβ5 as lack of αvβ5 in mice causes weakened retinal adhesion and asynchronous phagocytosis. With age, lack of αvβ5 leads to accumulation of harmful lipofuscin in the RPE and to vision loss. Here, we discuss three different possible mechanisms that could generate the exclusive apical distribution of αvβ5 integrin receptors in the RPE. (1) αvβ5 could be apical in the RPE because RPE attachment to neural retina generally or αvβ5 ligands specifically in the subretinal space stabilize apical but not basolateral αvβ5 surface receptors. (2) αvβ5 could be apical in the RPE because it resides in a complex with other components of the phagocytic machinery that assembles at the apical, phagocytic surface of the RPE. (3) αvβ5 could be apical due to mechanisms intrinsic to this receptor protein and specifically to its β5 integrin subunit.
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