Matrix metallopeptidase 28 (MMP28)

Matrix metallopeptidase 28 (MMP28, also known as epilysin) is a member of the matrix metalloproteinase family of zinc-dependent endopeptidases that play essential roles in the degradation and remodeling of extracellular matrix (ECM) components[1][2][3]. Unlike many MMPs, MMP28 is constitutively expressed in a range of normal tissues such as skin, lung, heart, and nervous system, and is highly inducible during processes including wound healing, development, and tissue regeneration[1][2][3][4]. MMP28 can induce epithelial-to-mesenchymal transition (EMT) via TGF-beta signaling, promote changes in cell adhesion, and modulate cell migration and ECM composition[1][3][4]. Increased MMP28 expression has been documented in various cancers, osteoarthritis, demyelinating diseases, and after tissue injury, supporting roles both in disease and normal physiological processes[1][3][4]. No specific clinical drugs directly targeting MMP28 are currently approved or in widespread use[2]. Modulation of MMP28, up or down, could have significant consequences for inflammation, tissue remodeling, and potentially cancer progression or metastasis[1][3][4].

Other names

Matrix metalloproteinase-28MMP-28EpilysinMM28MMP25UNQ1893/PRO4339

Enzymatic degradation of ECM proteins, including casein, Nogo-A, and neural cell adhesion molecule-1\nPromotion or inhibition of EMT via TGF-beta pathway modulation\nModulation of collagen cross-linking and fibronectin-1 expression\nUpregulation of other MMPs (such as MMP2), and TIMPs (tissue inhibitors of metalloproteinases)