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C.–H. Sung, J.–Z. Chuang; CLIC4–Mediated RPE Morphogenesis and RPE–Photoreceptor Interaction . Invest. Ophthalmol. Vis. Sci. 2006;47(13):4226.
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© ARVO (1962-2015); The Authors (2016-present)
The retinal pigment epithelium (RPE) is a multifunctional and indispensable component of the vertebrate retina. Its asymmetry, specialized membrane structures, and membrane motility, which are essential for many of its functions, rely heavily on a highly ordered cytoskeletons. At present, relatively little is known about the machinery and the molecular mechanism regulating cytoskeleton–mediated RPE functions. We found CLIC4, a recently identified actin–associated protein, was abundantly expressed in apical RPE microvilli. The purpose of these studies is to determine the functions of CLIC4 in RPE in vivo.
We performed CLIC4 silencing by transfecting siRNA (small interfering RNA) against CLIC4 into RPE of rodent eyes. RPE sheets or retina sections containing CLIC4–suppressed RPE were examined histologically and immunohistochemically.
The CLIC4 suppressed RPE cells developed several morphological changes including microvillus shortening, cytoskeleton re–arrangement, and cell–cell contact breakdown. Moreover, these animals developed profound retinal detachment and photoreceptor dystrophy.
CLIC4 is a key molecule involved in the morphogenesis of RPE and its interdigit interaction with neural photoreceptors.
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