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Myopia is a chronic ocular disease, emerging as the most common type of refractive error. This study intends to preliminarily explore the roles of protein S\u2010nitrosylation of nitric oxide (NO) in the regulation of myopia by detecting the expression of neuronal nitric oxide synthase (nNOS) and downstream S\u2010nitrosylation, using the animal model of lens\u2010induced myopia (LIM) in mice. <jats:italic>Methods<\/jats:italic>. The 3\u2010week\u2010old C57BL\/6 J mice were divided into three groups: group I, lens\u2010induced 0\u2010week group (take eyeballs at the age of 3 weeks); group II, self\u2010control eyes of experimental group (take eyeballs at the age of 7 weeks); and group III, lens\u2010induced 4\u2010week group (take eyeballs at the age of 7 weeks). The diopter and axial length of each group were measured by streak retinoscopes and optical coherence tomography (OCT) before and after model establishment. The protein expressions and locations of nNOS and S\u2010nitrosylated proteins (PSNOs) were measured by western blot and immunofluorescence staining. Site\u2010specific proteomic for protein S\u2010nitrolysation was used to detect the existence and location of S\u2010nitrosylation proteins in the retina of myopic and nonmyopic mice. The Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG), and motif enrichment analyses were performed. The differential sites were analyzed by GO, KEGG, and motif. Irreversible biotinylation procedure combined with protein purification and western blot was used to detect the protein expression of <jats:italic>\u03b1<\/jats:italic>\u2010enolase (ENO1), a key player in the hypoxia\u2010related signal pathway. <jats:italic>Results<\/jats:italic>. The expressions of nNOS and PSNOs were significantly lower in the retina of experimental eyes than that in self\u2010control eyes and 3\u2010week\u2010old baseline group. A total of 595 S\u2010nitrosylated proteins, 709 S\u2010nitrosylated peptides, and 708 S\u2010nitrosylated sites were identified by site\u2010specific S\u2010nitrolysation proteomics in the retina of myopic and control eyes. A total of 19 differentiation loci were screened, of which 13 sites were downregulated and 6 sites were upregulated in experimental eyes compared with the self\u2010control group. Specifically, the expression of SNO\u2010ENO1 was significantly lower in the retina of experimental eyes than that in self\u2010control eyes and 3\u2010week\u2010old baseline group. <jats:italic>Conclusion<\/jats:italic>. LIM induces the decrease of nNOS and PSNO protein levels in the retina of myopic mice. NO\u2010mediated nonclassical protein S\u2010nitrosylation modification may play an important role in the regulation of lens\u2010induced myopia. ENO1 may be a key factor in the regulation of S\u2010nitrosylation modification of myopia.<\/jats:p>","DOI":"10.1155\/2022\/8296043","type":"journal-article","created":{"date-parts":[[2022,11,16]],"date-time":"2022-11-16T23:05:09Z","timestamp":1668639909000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Mechanisms of NO\u2010Mediated Protein S\u2010Nitrosylation in the Lens\u2010Induced 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