Myopia, the most common cause of impaired vision, may induce sight- threatening diseases or ocular complications due to axial elongation. The exact mechanisms underlying myopia development have received much attention and understanding of these is necessary for clinical prevention or therapeutics. In this study, quantitative proteomics using Isotope Coded Protein Label (ICPL) was applied to identify differentially regulated proteins in the retinas of myopic chicks and, from their presence, infer the possible pathogenesis of excessive ocular elongation. Newly hatched white leghorn chicks (n = 15) wore -10D and + 10D lenses bilaterally for 3 and 7 days, respectively, to develop progressive lens-induced myopia (LIM) and hyperopia (LIH). Retinal proteins were quantified with nano-liquid chromatography electrospray ionization coupled with tandem mass spectrometry (nanoLC-ESI-MS/MS). Bioinformatics analysis of differentially regulated proteins revealed that the majority originated from the cytoplasmic region and were related to various metabolic, glycolytic, or oxidative processes. The fold changes of four proteins of interest (vimentin, apolipoprotein A1, interphotoreceptor retinoid binding protein, and glutathione S-transferase) were further confirmed by a novel high-resolution multiple reaction monitoring mass spectrometry (MRM-HR) using a label-free approach. SIGNIFICANCE: Discovery of effective protein biomarkers of myopia has been extensively studied to inhibit myopia progression. This study first applied lens-induced hyperopia and myopia in the same chick to maximize the inter-ocular differences, aiming to discover more protein biomarker candidates. The findings provided new evidence that myopia was metabolism related, accompanied by altered energy generation and oxidative stress at retinal protein levels. The results in the retina were also compared to our previous study in vitreous using ICPL quantitative technology. We have now presented the protein changes in these two adjacent tissues, which may provide extra information of protein changes during ocular growth in myopia.

中文翻译：

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视网膜代谢和氧化应激的改变可能与近视眼的生长有关：来自动物模型中发现和靶向蛋白质组学的证据。

近视是视力障碍的最常见原因，可能由于轴伸长而诱发视力障碍疾病或眼部并发症。近视发展的确切机制已受到广泛关注，对这些的理解对于临床预防或治疗是必不可少的。在这项研究中，使用同位素编码蛋白质标记（ICPL）的定量蛋白质组学被用于鉴定近视雏鸡视网膜中差异调节的蛋白质，并根据它们的存在推断出过度眼球延长的可能发病机理。新孵化的白色来亨鸡雏（n = 15）分别在双侧分别佩戴-10D和+ 10D眼镜3天和7天，以发展为进行性晶状体引起的近视（LIM）和远视（LIH）。用纳米液相色谱电喷雾电离结合串联质谱法（nanoLC-ESI-MS / MS）对视网膜蛋白进行定量。对差异调节蛋白的生物信息学分析表明，大多数蛋白起源于细胞质区域，并且与各种代谢，糖酵解或氧化过程有关。通过使用无标记方法的新型高分辨率多反应监测质谱（MRM-HR），进一步证实了四种目标蛋白（波形蛋白，载脂蛋白A1，感光体类视黄醇结合蛋白和谷胱甘肽S-转移酶）的倍数变化。意义：已经广泛研究了抑制近视进展的有效蛋白质生物标记物。这项研究首先在同一只鸡上应用了晶状体引起的远视和近视，以最大程度地扩大眼内差异，旨在发现更多的蛋白质生物标志物候选物。这些发现提供了新的证据，即近视与代谢有关，并伴随着视网膜蛋白水平的能量产生和氧化应激改变。还使用ICPL定量技术将视网膜中的结果与我们先前在玻璃体中的研究进行了比较。现在，我们介​​绍了这两个相邻组织中的蛋白质变化，这可能为近视眼生长期间的蛋白质变化提供更多信息。还使用ICPL定量技术将视网膜中的结果与我们先前在玻璃体中的研究进行了比较。现在，我们介​​绍了这两个相邻组织中的蛋白质变化，这可能为近视眼生长期间的蛋白质变化提供更多信息。还使用ICPL定量技术将视网膜中的结果与我们先前在玻璃体中的研究进行了比较。现在，我们介​​绍了这两个相邻组织中的蛋白质变化，这可能为近视眼生长期间的蛋白质变化提供更多信息。