Disintegrin and metalloproteinase domain-containing protein 8 (ADAM8)

Disintegrin and metalloproteinase domain-containing protein 8 (ADAM8) is a multidomain, membrane-anchored metalloproteinase enzyme implicated in diverse biological processes including extracellular proteolysis, cell adhesion, cell–cell and cell–matrix interaction, and regulation of immune cell extravasation and inflammatory responses[1][2][3][4]. It contains a prodomain, a metalloproteinase domain, a disintegrin domain, a cysteine-rich region, a transmembrane domain, and a cytoplasmic tail[1][4]. ADAM8 is capable of autocatalytic activation and is involved in shedding a range of cell surface proteins, including cytokines and adhesion molecules[1]. It is overexpressed in several types of cancer, is involved in tissue remodeling, and contributes to both cancer progression and inflammation[1][3]. ADAM8 has also been suggested as a therapeutic target in asthma and other inflammatory diseases[3].

Other names

ADAM metallopeptidase domain 8MS2CD156aCD156Cell surface antigen MS2Human leukocyte differentiation antigen

Inhibition of ADAM8 enzymatic (metalloproteinase) activity, leading to reduced extracellular matrix breakdown and cell signaling