Salidroside (Sal) exerted widely pharmacological effects in multitudinous diseases had been certified. The actual study clarified the protective activity of Sal in H 2 O 2 -injured human trabecular meshwork (HTM) cells. HTM cells were disposed with H 2 O 2 to construct an oxidative damage model in vitro. Then, Sal was utilized to administrate HTM cells, and cell viability, apoptosis, apoptosis-interrelated proteins and ROS production were appraised using CCK-8, flow cytometry, western blot and DCFH-DA staining. MiR-27a inhibitor and its control were transfected into HTM cells, and the influences of miR-27a inhibition in HTM cells stimulated with H 2 O 2 and Sal were detected. PI3K/AKT and Wnt/b-catenin pathways were ultimately investigated to uncover the underlying mechanism. We found that H 2 O 2 evoked HTM cells oxidative damage, as evidenced by repressing cell viability, inducing apoptosis, activating cleavedcaspase-3/-9 expression and increasing ROS production. Sal significantly lightened H 2 O 2 -evoked oxidative damage in HTM cells. Additionally, miR-27a was up-regulated by Sal, and miR-27a suppression significantly reversed the protective effect of Sal on H 2 O 2 -injured HTM cells. Finally, Sal activated PI3K/ AKT and Wnt/b-catenin pathways through enhancement of miR-27a in H 2 O 2 -injured HTM cells. In conclusion, these discoveries suggested that Sal could protect HTM cells against H 2 O 2 -evoked oxidative damage by activating PI3K/AKT and Wnt/b-catenin pathways through enhancement of miR-27a. HIGHLIGHTS 1. H 2 O 2 evokes HTM cells oxidative damage; 2. Sal relieves H 2 O 2 -induced oxidative damage in HTM cells; 3. Sal enhances miR-27a expression in H 2 O 2 -injured HTM cells; 4. Repressed miR-27a reverses the protective impacts of Sal on H 2 O 2 -injured HTM cells; 5. Sal activates PI3K/AKT and Wnt/b-catenin pathways by increasing miR-27a.
Objective of the study: To identify the pathogenic gene and mutation site of a Chinese family with congenital cataract. Methods: Eight family members and 100 controls were employed, and targeted exome sequencing was used to identify the genetically pathogenic factor of the proband. Results: Targeted next-generation sequencing identified a novel missense mutation c.209A>C (p.Q70P) of CRYBB1 gene in the family. Sanger sequencing results showed that this heterozygous mutation was a causative mutation, which was not found in unaffected family members and healthy controls. Bioinformatics predicts that the effect of this mutation on protein function is probably harmful. Conclusion: We demonstrate that c.209A>C of CRYBB1 gene is a pathogenic mutation in the family of congenital nuclear cataract in this study. This is the first report that this mutation leads to congenital nuclear cataract, which broadens the mutation spectrum of CRYBB1 gene in congenital nuclear cataract.
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