Rat Aifm1 (Apoptosis-inducing factor 1, mitochondrial) ELISA Kit

Impaired mitochondrial energy metabolism contributes to a wide range of pathologic conditions, including neurodegenerative diseases. Mitochondrial apoptosis-inducing factor (AIF) is required for the correct maintenance of mitochondrial electron transport chain. An emerging body of clinical evidence indicates that several mutations in the AVM/gene are causally linked to severe forms of mitochondrial disorders. Here we investigate the consequence of WAH-1/AIF deficiency in the survival of the nematode Caenorhabditis elegans. Moreover, we assess the survival of C. elegans strains expressing a disease-associated WAH-1/AIF variant. We demonstrate that wah-1 downregulation compromises the function of the oxidative phosphorylation system and reduces C. elegans lifespan. Notably, the loss of respiratory subunits induces a nuclear-encoded mitochondrial stress response independently of an evident increase of oxidative stress. Overall, our data pinpoint an evolutionarily conserved role of WAH-1/AIF in the maintenance of proper mitochondrial activity.

Background: Osteoarthritis (OA) is one of the most prevalent and degenerative diseases with complicated pathology including articular cartilage degradation, subchondral sclerosis and synovitis. Chondrocytes play a crucial role in maintaining cartilage integrity. Methods: Primary chondrocytes were treated with 10 ng/mL IL-1 beta alone, or pre-treated with 20 mu M baicalin for 5 h followed by co-treatment with 20 mu M baicalin and 10 ng/mL IL-1 beta. CCK-8 assay was used to assess cell viability, and cell apoptosis was analyzed by both PUFITC-Annexin V staining and quantitating apoptosis-related Bc1-2, Box and cleaved-caspase-3 expression at both protein and mRNA level by Western blotting and qRT-PCR, respectively. Chondrocytes were transfected with miRNA-766-3p mimic and autophagy flux was examined by LC3, Beclin and p62 Western blotting and by Cyto-ID assay to quantify autophagic vacuoles. Results: Baicalin treatment decreased the apoptosis rate and the expressions of proapoptotic proteins induced by IL-1 beta, up-regulated anti-apoptotic Bcl-2 expression, and inhibited the degradation of ECM. Baicalin increased autophagy through up-regulating the autophagy markers Beclin-1 expression and LC3 II /LC3 I ratio and promoting autophagic flux. Contrarily, autophagy inhibition partially alleviated the beneficial effects of baicalin on ECM synthesis and anti-apoptosis in the chondrocytes treated with L-1 beta. Furthermore, the differential expressional profiles of miR-766-3p and apoptosis-inducing factor mitochondriaassociated 1 (AIFM1) were determined in IL-1 beta and IL-1 beta + baicalin-treated chondrocytes, and we confirmed AIFM1 was a target of miR-766-3p. MiR-766-3p overexpression suppressed apoptosis and facilitated autophagy and ECM synthesis in the chondrocytes through decreasing AIFM1. Contrarily, silencing of miR-766-3p inhibited chondrocyte autophagy and promoted apoptosis, and this effect could be reversed by AIFM1 silence. Conclusion: Baicalin protects human OA chondrocytes against IL-1 beta-induced apoptosis and the degradation of ECM through activating autophagy via miR-766-3p/AIFM1 axis and serves as a potential therapeutic candidate for OA treatment.