Serpin family E member 1 mRNA 3′ untranslated region (SERPINE1 mRNA 3′UTR)

The Serpin family E member 1 (SERPINE1) mRNA 3′ untranslated region (3′UTR) is a critical regulatory segment of the messenger RNA encoding Plasminogen Activator Inhibitor-1 (PAI-1) (NIH/PMC). PAI-1 serves as the primary physiological inhibitor of tissue-type and urokinase-type plasminogen activators (tPA and uPA), thereby acting as a central regulator of fibrinolysis and extracellular matrix remodeling (NIH/PMC, Maayanlab). The 3′UTR contains multiple binding sites for microRNAs, such as miR-30a, miR-143, and miR-642a, as well as RNA-binding proteins like SERBP1 and p53, which dictate mRNA stability and translation efficiency (ResearchGate, bioRxiv). Dysregulation of PAI-1 expression, often mediated by 3′UTR-dependent mechanisms, is associated with various pathologies including thrombosis, tissue fibrosis, cardiovascular disease, and cancer progression (NIH/PMC). Therapeutic strategies targeting the SERPINE1 mRNA 3′UTR, such as antisense oligonucleotides (ASOs) like IONIS-PAI-1Rx, aim to reduce PAI-1 levels by promoting mRNA degradation or blocking regulatory interactions (Biojx). This approach offers a potential treatment for conditions characterized by hypofibrinolysis or excessive fibrosis, though challenges include managing the risk of bleeding and ensuring tissue-specific delivery (Ionis Pharmaceuticals, ResearchGate).

Other names

PAI-1 mRNA 3′UTRPlasminogen activator inhibitor-1 mRNA 3′UTRPLANH1 mRNA 3′UTRSerpin E1 mRNA 3′UTRSERPINE1 3′ untranslated region

Antisense oligonucleotides (ASOs) target the 3′UTR to recruit RNase H for mRNA degradation or to sterically block the binding of microRNAs and RNA-binding proteins (e.g., p53, SERBP1), thereby modulating mRNA stability and translation.