Disintegrin and metalloproteinase domain-containing protein 12 (ADAM12)

Disintegrin and metalloproteinase domain-containing protein 12 (ADAM12) is a multidomain metalloprotease enzyme of the ADAM family, displaying both proteolytic and adhesive properties through its metalloproteinase and disintegrin domains, respectively[1][4]. It exists in two main isoforms: the membrane-bound ADAM12-L and the secreted, soluble ADAM12-S, with each mediating distinct roles in cell-matrix and cell-cell interactions[1][4]. ADAM12 is involved in tissue remodeling, myogenesis, bone elongation, and modulates signaling pathways such as EGFR by processing growth factor precursors[1]. It is overexpressed in numerous cancers, where it promotes migration, invasion, and therapeutic resistance, particularly in glioma and triple-negative breast cancer[2][5]. ADAM12 also serves as an early biomarker for Down syndrome in maternal serum screening and is implicated in fibrotic, cardiovascular, and inflammatory diseases[4]. Despite its therapeutic appeal, direct ADAM12-targeted drugs are not yet clinically available, though emerging data indicate that inhibition may enhance chemotherapy efficacy in certain cancers[5].

Other names

ADAM12MeltrinMeltrin-alphaMLTNMCMPMCMPMltnaADAM12-OT1MLTNACAR10UNQ346/PRO545

Proteolytic cleavage of extracellular matrix components to modulate tissue remodeling; Regulation of growth factor (EGFR) activation through ligand shedding; Modulation of tumor cell migration, invasion, and chemoresistance; Potential substrate for Src kinase; involvement in PI-3 kinase signaling[3]