A Disintegrin and Metalloproteinase (ADAM) is a family of proteolytic enzymes that regulate shedding of membrane-bound proteins, growth factors, cytokines, ligands and receptors [ PUBMED:30905657 ]. This group of proteins are fundamental to many control processes in development and homeostasis, and they are linked to … expand

A Disintegrin and Metalloproteinase (ADAM) is a family of proteolytic enzymes that regulate shedding of membrane-bound proteins, growth factors, cytokines, ligands and receptors [ PUBMED:30905657 ]. This group of proteins are fundamental to many control processes in development and homeostasis, and they are linked to pathological states [ PUBMED:18762209 ].

ADAM is a transmembrane protein that contains a disintegrin and metalloprotease domain (MEROPS peptidase family M12B). All members of the ADAM family display a common domain organisation -a pro-domain, the metalloprotease, disintigrin, cysteine-rich, epidermal-growth factor like, and transmembrane domains and a C-terminal cytoplasmic tail. They possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signalling. ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour.They are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain [ PUBMED:11193153 PUBMED:12514095 ].

The ADAM cysteine-rich domain is not found in plant, archaeal, bacterial or viral proteins. The cysteine-rich domain complements the binding capacity of the disintegrin domain, and perhaps imparts specificity to disintegrin domain-mediated interactions. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity [ PUBMED:12460986 ].