HSPB4/CRYAA Protect Photoreceptors during Retinal Detachment in Part through FAIM2 Regulation.

IF 3.2 Q2 CLINICAL NEUROLOGY Neurology International Pub Date : 2024-08-26 DOI:10.3390/neurolint16050068
Cagri G Besirli, Madhu Nath, Jingyu Yao, Mercy Pawar, Angela M Myers, David Zacks, Patrice E Fort
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Abstract

Our previous study discussed crystallin family induction in an experimental rat model of retinal detachment. Therefore, we attempted to evaluate the role of α-crystallin in photoreceptor survival in an experimental model of retinal detachment, as well as its association with the intrinsically neuroprotective protein Fas-apoptotic inhibitory molecule 2 (FAIM2). Separation of retina and RPE was induced in rat and mouse eyes by subretinal injection of hyaluronic acid. Retinas were subsequently analyzed for the presence αA-crystallin (HSPB4) and αB-crystallin (HSPB5) proteins using immunohistochemistry and immunoblotting. Photoreceptor death was analyzed using terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick end labeling (TUNEL) staining and cell counts. The 661W cells subjected to FasL were used as a cell model of photoreceptor degeneration to assess the mechanisms of the protective effect of αA-crystallin and its dependence on its phosphorylation on T148. We further evaluated the interaction between FAIM2 and αA-crystallin using a co-immunoprecipitation assay. Our results showed that α-crystallin protein levels were rapidly induced in response to retinal detachment, with αA-crystallin playing a particularly important role in protecting photoreceptors during retinal detachment. Our data also show that the photoreceptor intrinsically neuroprotective protein FAIM2 is induced and interacts with α-crystallins following retinal detachment. Mechanistically, our work also demonstrated that the phosphorylation of αA-crystallin is important for the interaction of αA-crystallin with FAIM2 and their neuroprotective effect. Thus, αA-crystallin is involved in the regulation of photoreceptor survival during retinal detachment, playing a key role in the stabilization of FAIM2, serving as an important modulator of photoreceptor cell survival under chronic stress conditions.

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HSPB4/CRYAA在视网膜脱离过程中部分通过FAIM2调控保护光感受器
我们之前的研究讨论了晶体蛋白家族在大鼠视网膜脱离实验模型中的诱导作用。因此,我们尝试在视网膜脱离实验模型中评估α-结晶素在感光细胞存活中的作用,以及它与固有神经保护蛋白 Fas-apoptotic inhibitory molecule 2(FAIM2)的关联。通过在大鼠和小鼠眼球视网膜下注射透明质酸诱导视网膜和 RPE 分离。随后使用免疫组织化学和免疫印迹法分析视网膜中是否存在αA-结晶素(HSPB4)和αB-结晶素(HSPB5)蛋白。使用末端脱氧核苷酸转移酶介导的脱氧尿苷三磷酸缺口末端标记(TUNEL)染色和细胞计数分析感光细胞的死亡。我们将受FasL作用的661W细胞作为光感受器变性的细胞模型,以评估αA-结晶素的保护作用机制及其对T148磷酸化的依赖性。我们使用共沉淀免疫分析法进一步评估了FAIM2与αA-结晶素之间的相互作用。我们的结果表明,视网膜脱落时,α-结晶素蛋白水平会被迅速诱导,而αA-结晶素在视网膜脱落期间保护光感受器方面发挥着特别重要的作用。我们的数据还显示,视网膜脱离后,光感受器固有神经保护蛋白FAIM2会被诱导并与α-结晶蛋白相互作用。从机理上讲,我们的研究还证明了αA-结晶蛋白的磷酸化对αA-结晶蛋白与FAIM2的相互作用及其神经保护作用非常重要。因此,αA-结晶素参与了视网膜脱离过程中感光细胞存活的调控,在稳定FAIM2方面发挥了关键作用,是慢性应激条件下感光细胞存活的重要调节因子。
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来源期刊
Neurology International
Neurology International CLINICAL NEUROLOGY-
CiteScore
3.70
自引率
3.30%
发文量
69
审稿时长
11 weeks
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