HMGCR Protein, Human (His)

Cyclophilin A protein serves as a catalyst for the cis-trans isomerization of proline imidic peptide bonds within oligopeptides. Beyond its enzymatic role, it exerts diverse cellular effects, including a potent chemotactic influence on leukocytes, mediated in part through the activation of its membrane receptor BSG/CD147, initiating a signaling cascade leading to MAPK/ERK activation. The protein also activates endothelial cells (ECs) in a pro-inflammatory manner, inducing NF-kappa-B and MAP-kinase pathways and promoting the expression of adhesion molecules. Furthermore, Cyclophilin A induces apoptosis in ECs by modulating the expression of key factors involved in chemotaxis and apoptosis. In response to oxidative stress, it initiates both proapoptotic and antiapoptotic signaling in ECs, highlighting its multifaceted role. The protein negatively regulates MAP3K5/ASK1 kinase activity and is crucial for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein complexes, influencing TARDBP binding to RNA and regulating the expression of associated genes. Additionally, Cyclophilin A plays a significant role in platelet activation and aggregation, as well as in the regulation of calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling through increased ROS production and facilitation of integrin-cytoskeleton interaction. It also exhibits binding affinity for heparan sulfate glycosaminoglycans.