Matrix metalloproteinase 9 (MMP-9) (MMP-9)

Matrix metalloproteinase 9 (MMP-9), also known as gelatinase B, is a zinc-dependent endopeptidase that plays a critical role in degrading extracellular matrix (ECM) components, particularly type IV collagen and gelatin [UniProt: P14780]. In the skin, MMP-9 is produced by various cells including fibroblasts and keratinocytes, where its expression is tightly regulated during processes like wound healing and basement membrane remodeling [PMID: 25605932]. Pathologically, elevated MMP-9 levels are associated with cancer progression, where it facilitates tumor invasion and angiogenesis, as well as chronic inflammatory conditions and non-healing wounds [PubMed: 28273103]. Therapeutic targeting of MMP-9 has involved small molecule inhibitors and highly specific monoclonal antibodies like andecaliximab, aimed at reducing tissue destruction and tumor metastasis [ClinicalTrials.gov: NCT02545504]. However, clinical development has been hampered by the challenge of achieving selectivity over other MMP isoforms to avoid side effects such as musculoskeletal toxicity.

Other names

Gelatinase B92 kDa type IV collagenase92 kDa gelatinaseCLG4BMMP9

Inhibition of the proteolytic activity of MMP-9 to prevent the degradation of extracellular matrix components and the activation of pro-inflammatory cytokines.