LAUSR

Using liquid chromatography-tandem mass spectrometry (LC-MS/MS) as a protein quantification technique for the analysis of the proteomic profile of myopia patient tear fluid, to clarify the role of dysregulated proteins in high myopia (HM) in order to provide a more thorough understanding of the molecular processes involved in the development of the disease. Schirmer strips were used to acquire the tear films from 20 subjects (10 high myopia patients and 10 control subjects). LC-MS/MS was utilized to identify the proteome profile of the tears in order to assess protein interrelationships utilizing bioinformatics. The tear preparations from the HM group and the control group included a total of 1544 proteins. The expression of 79 proteins out of the identified ones differed significantly between the two groups. 51 proteins showed overexpression and 28 proteins showed downregulation. 15 differentially expressed proteins (DEPs) were enriched in metabolic pathways, 15 DEPs were enriched in extracellular exomes, and 5 DEPs were enriched in the complement and coagulation cascades pathway. Potentially important proteins and therapeutic targets in human HM include TTR and Antithrombin-III. The proteomic analysis of tear fluid in high myopia patients identifies key proteins and pathways involved in the disease, offering potential biomarkers for its pathogenesis and therapeutic targets.