Arnold and Mabel Beckman Macular Research Center, Doheny Eye Institute, Los Angeles, California, United States of America.
PLoS One. 2010 Oct 8;5(10):e12578. doi: 10.1371/journal.pone.0012578.
αB crystallin is a chaperone protein with anti-apoptotic and anti-inflammatory functions and has been identified as a biomarker in age-related macular degeneration. The purpose of this study was to determine whether αB crystallin is secreted from retinal pigment epithelial (RPE) cells, the mechanism of this secretory pathway and to determine whether extracellular αB crystallin can be taken up by adjacent retinal cells and provide protection from oxidant stress. We used human RPE cells to establish that αB crystallin is secreted by a non-classical pathway that involves exosomes. Evidence for the release of exosomes by RPE and localization of αB crystallin within the exosomes was achieved by immunoblot, immunofluorescence, and electron microscopic analyses. Inhibition of lipid rafts or exosomes significantly reduced αB crystallin secretion, while inhibitors of classic secretory pathways had no effect. In highly polarized RPE monolayers, αB crystallin was selectively secreted towards the apical, photoreceptor-facing side. In support, confocal microscopy established that αB crystallin was localized predominantly in the apical compartment of RPE monolayers, where it co-localized in part with exosomal marker CD63. Severe oxidative stress resulted in barrier breakdown and release of αB crystallin to the basolateral side. In normal mouse retinal sections, αB crystallin was identified in the interphotoreceptor matrix. An increased uptake of exogenous αB crystallin and protection from apoptosis by inhibition of caspase 3 and PARP activation were observed in stressed RPE cultures. αB Crystallin was taken up by photoreceptors in mouse retinal explants exposed to oxidative stress. These results demonstrate an important role for αB crystallin in maintaining and facilitating a neuroprotective outer retinal environment and may also explain the accumulation of αB crystallin in extracellular sub-RPE deposits in the stressed microenvironment in age-related macular degeneration. Thus evidence from our studies supports a neuroprotective role for αB crystallin in ocular diseases.
αB 晶状体蛋白是一种具有抗细胞凋亡和抗炎功能的伴侣蛋白,已被确定为与年龄相关的黄斑变性的生物标志物。本研究旨在确定 αB 晶状体蛋白是否从视网膜色素上皮 (RPE) 细胞中分泌,这种分泌途径的机制,以及细胞外 αB 晶状体蛋白是否可以被相邻的视网膜细胞摄取,并提供对抗氧化应激的保护。我们使用人 RPE 细胞证实 αB 晶状体蛋白通过涉及外泌体的非经典途径分泌。通过免疫印迹、免疫荧光和电子显微镜分析证实了 RPE 释放外泌体和 αB 晶状体蛋白在其中定位的证据。抑制脂筏或外泌体显著减少 αB 晶状体蛋白的分泌,而经典分泌途径的抑制剂则没有影响。在高度极化的 RPE 单层中,αB 晶状体蛋白选择性地朝向顶端、面向光感受器的一侧分泌。共聚焦显微镜证实,αB 晶状体蛋白主要定位于 RPE 单层的顶端隔室,部分与外泌体标记物 CD63 共定位。严重的氧化应激导致屏障破坏和 αB 晶状体蛋白释放到基底外侧。在正常的小鼠视网膜切片中,在光感受器间基质中鉴定出 αB 晶状体蛋白。在应激的 RPE 培养物中观察到外源性 αB 晶状体蛋白的摄取增加和 caspase 3 抑制以及 PARP 激活的保护作用,从而阻止了细胞凋亡。在暴露于氧化应激的小鼠视网膜外植体中,感光细胞摄取了 αB 晶状体蛋白。这些结果表明 αB 晶状体蛋白在维持和促进神经保护性外视网膜环境中起着重要作用,也可以解释在年龄相关性黄斑变性中应激微环境中外泌体下 RPE 沉积物中 αB 晶状体蛋白的积累。因此,我们的研究结果支持 αB 晶状体蛋白在眼部疾病中具有神经保护作用。