Biswas Sondip, Son Alexander, Yu Qili, Zhou Renping, Lo Woo-Kuen
Department of Neurobiology, Morehouse School of Medicine, Atlanta, GA, USA.
Department of Chemical Biology, College of Pharmacy, Rutgers University, Piscataway, NJ, USA.
Exp Eye Res. 2016 Apr;145:130-139. doi: 10.1016/j.exer.2015.11.017. Epub 2015 Nov 28.
Ephrin-A5, a ligand of the Eph family of receptor tyrosine kinases, plays a key role in lens fiber cell packing and cell-cell adhesion, with approximately 87% of ephrin-A5(-/-) mice develop nuclear cataracts. Here, we investigated the extensive formation of light-scattering globules associated with breakdown of interlocking protrusions during lens opacification in ephrin-A5(-/-) mice. Lenses from wild-type (WT) and ephrin-A5(-/-) mice between 2 and 21 weeks old were studied with light and electron microscopy, immunofluorescence labeling, freeze-fracture TEM and filipin cytochemistry for membrane cholesterol detection. Lens opacities with various densities were first observed in ephrin-A5(-/-) mice at around 60 days old. Dense cataracts in the mutant lenses were seen primarily in the nuclear region surrounded by transparent cortices from all eyes examined. We confirmed that a majority of nuclear cataracts were dislocated posteriorly and ruptured the thinner posterior lens capsule. SEM analysis indicated that numerous interlocking protrusions and wavy ridge-and-valley membrane surfaces in deep cortical and nuclear fibers did not cause lens opacity in both transparent ephrin-A5(-/-) and WT mice. In contrast, abundant isolated membranous globules of approximately 1000 nm in size were distributed randomly along the intact fiber cells during early stage of all ephrin-A5(-/-) cataracts examined. A further examination using both SEM and TEM revealed that isolated globules were generated from the disintegrated interlocking protrusions originally located along the corners of hexagonal fiber cells. Freeze-fracture TEM further revealed the association of square-array aquaporin junctions with both isolated globules and interlocking membrane domains. This study reports for the first time that disrupted interlocking protrusions are the source of numerous large membranous globules that contribute to light scattering and nuclear cataracts in the ephrin-A5(-/-) mice. Our results further suggest that dissociations of N-cadherin and adherens junctions in the associated interlocking domains may result in the formation of isolated globules and nuclear opacities in the ephrin-A5(-/-) mice.
Ephrin-A5是受体酪氨酸激酶Eph家族的一种配体,在晶状体纤维细胞堆积和细胞间黏附中起关键作用,约87%的ephrin-A5基因敲除小鼠会发生核性白内障。在此,我们研究了ephrin-A5基因敲除小鼠晶状体混浊过程中与连锁突起破坏相关的光散射小球的广泛形成。对2至21周龄野生型(WT)和ephrin-A5基因敲除小鼠的晶状体进行了光学和电子显微镜检查、免疫荧光标记、冷冻断裂透射电镜检查以及用于检测膜胆固醇的 Filipin 细胞化学分析。在大约60日龄的ephrin-A5基因敲除小鼠中首次观察到不同密度的晶状体混浊。在所检查的所有眼睛中,突变型晶状体中的致密白内障主要见于被透明皮质包围的核区域。我们证实,大多数核性白内障向后移位并破裂较薄的晶状体后囊。扫描电镜分析表明,在透明的ephrin-A5基因敲除小鼠和WT小鼠中,深层皮质和核纤维中的大量连锁突起和波浪状脊谷膜表面均未导致晶状体混浊。相比之下,在所有检查的ephrin-A5基因敲除白内障早期,大小约为1000纳米的大量孤立膜性小球沿完整的纤维细胞随机分布。使用扫描电镜和透射电镜的进一步检查显示,孤立小球由最初位于六边形纤维细胞角部的解体连锁突起产生。冷冻断裂透射电镜进一步揭示了方形阵列水通道蛋白连接与孤立小球和连锁膜结构域的关联。本研究首次报道,连锁突起的破坏是导致ephrin-A5基因敲除小鼠中大量大膜性小球形成的原因,这些小球导致光散射和核性白内障。我们的结果进一步表明,相关连锁结构域中N-钙黏蛋白和黏附连接的解离可能导致ephrin-A5基因敲除小鼠中孤立小球的形成和核混浊。