| Popis: |
This study aims to explore the changes in the vitreous proteomics of form deprivation myopia (FDM) in guinea pigs, in order to reveal the molecular mechanisms involved in the onset and development of myopia. The myopia model in guinea pigs was successfully established by covering one eye of the guinea pigs with a latex bead sac for 4 weeks. This study used 4D data-independent acquisition proteomics technology to analyze vitreous body samples from both the FDM group and the control group. The goal of the proteomics analysis was to identify differences in protein expression within the vitreous body of FDM guinea pigs. Myopia was successfully induced in the FDM group after 4 weeks of modeling. A total of 6298 proteins were identified, among which 348 were differentially expressed proteins (DEPs), with 81 upregulated and 267 downregulated. These DEPs were subjected to in-depth bioinformatics analyses, including Gene Ontology, the Eukaryotic Orthologous Groups, and the Kyoto Encyclopedia of Genes and Genomes. These analyses revealed significant involvement in cellular processes, metabolic pathways, biological regulation, cytoskeletal organization, and cell movement. Our results indicate that calcium signaling plays a critical role in mediating eye changes associated with form deprivation, which may bear similarities to mechanisms observed in neurodegenerative diseases. A total of 348 DEPs related to the development and progression of myopia were identified. These changes involve key biological processes, including protein degradation, cell adhesion, and transport, especially alterations in calcium signaling pathways. Stromal interaction molecule 1 (STIM1) is an important biological marker of FDM, which was confirmed by Western blot, immunohistochemistry and ELISA. Our study found clear differences in the expression of proteins in the vitreous during the development of myopic guinea pigs, especially those related to calcium signaling pathway. Our study offers new insights into the pathogenesis of myopia, particularly changes related to protein metabolism pathways. |
