Serpin family B member 2 (SERPINB2) (SERPINB2)

Serpin family B member 2 (SERPINB2), also known as Plasminogen Activator Inhibitor-2 (PAI-2), is a serine protease inhibitor that primarily functions to inhibit urokinase-type plasminogen activator (uPA), thereby regulating fibrinolysis and extracellular matrix remodeling (UniProt: P05115). The specific regulatory axis involving exosomal miR-146a-5p targeting SERPINB2 mRNA is a critical pathway in modulating inflammatory responses and cellular senescence, particularly in chronic obstructive pulmonary disease (COPD) and wound healing (PubMed: 31203480). In this mechanism, miR-146a-5p is packaged into exosomes and delivered to recipient cells, where it binds to the 3' untranslated region (UTR) of SERPINB2 mRNA, leading to its degradation or translational repression (PubMed: 28235144). This interaction acts as a feedback inhibitor to dampen overactive immune responses by reducing SERPINB2 levels, which otherwise promote pro-inflammatory cytokine secretion. While SERPINB2 is not currently a target for FDA-approved small molecule drugs, its regulation via miRNA-based therapies or exosomal delivery systems represents a significant area of research in regenerative medicine and oncology. Dysregulation of this axis is also a notable biomarker in pregnancy-related disorders like preeclampsia and various malignancies.

Other names

Plasminogen activator inhibitor 2PAI-2Monocyte arginine-serpinPAI2Planh2hsa-miR-146a-5pMicroRNA 146a

Post-transcriptional silencing of SERPINB2 mRNA by miR-146a-5p to modulate the uPA/uPAR signaling pathway and inflammatory cytokine production.