Matrix metallopeptidase 23B (MMP23B)

Matrix metallopeptidase 23B (MMP23B) is a member of the matrix metalloproteinase family, enzymes characterized by their zinc- and calcium-dependent proteolytic activity involved in the breakdown and remodeling of extracellular matrix components. Uniquely, MMP23B has a type-II transmembrane domain, an atypical pro-domain (lacking the classical cysteine-switch motif), a central catalytic domain with zinc-binding sites, a toxin-like domain, and an immunoglobulin-like cell adhesion molecule (IgCAM) domain in place of the common hemopexin domain found in other MMPs[1][2]. MMP23B modulates the trafficking and function of voltage-gated potassium channels (notably Kv1.3), is strongly expressed in ovarian tissue and heart, and is involved in tissue remodeling associated with reproduction and possibly inflammation[1][2][3]. In disease, MMP23B may play roles in cancer, particularly as a non-invasive urinary biomarker in bladder cancer risk assessment, and in inflammatory disorders[2]. Its clinical significance as a therapeutic target or drug-interacting protein remains under investigation, and no drugs targeting MMP23B are currently approved or well-characterized[1][2].

Other names

Matrix metalloproteinase-23MMP23AMMP22MMP-23MMP-22MMP-21MIFRMIFR-1FemalysinMatrix metalloproteinase in the female reproductive tract