Abstract
Since the discovery of the first disintegrin protein from snake venom and the following identification of a mammalian membrane-anchored metalloprotease-disintegrin implicated in fertilization, almost three decades of studies have identified additional members of these families and several biochemical mechanisms regulating their expression and activity in the cell. Most importantly, new in vivo functions have been recognized for these proteins including cell partitioning during development, modulation of inflammatory reactions, and development of cancers. In this review, we will overview the a disintegrin and metalloprotease (ADAM) family of proteases highlighting some of the major research achievements in the analysis of ADAMs’ function that have underscored the importance of these proteins in physiological and pathological processes over the years.
Highlights
The initial studies on ADAMs focused on the function of the disintegrin domain in cell-cell cell‐cell and cell-matrix interactions
In addition to mediating interactions with cell surface receptors for adhesive and fusogenic purposes, the disintegrin and cysteine domains were suggested to regulate the proteolytic function of ADAMs as shown for the shedding of interleukin-1 receptor-II by ADAM-17 [19]
By analogy to the SVMPs, that have a metalloprotease and disintegrin domain, it was suggested that some ADAMs cleave extracellular matrix components
Summary
Similarities in domain of SVMP and ADAM from the common ancestor gene [3]. Protein contain a pro‐domain, a metalloproteinase and a disintegrin and a cysteine domain. The acontain pro-domain, a metalloproteinase and a disintegrin domain,domain, and a cysteine domain The latter latter in ADAMs has cell adhesive and fusogenic potential. ADAMs contain a catalytic-Zn binding signature for metalloproteases (HExGHxxGxxHD). Known ADAMs contain a catalytic‐Zn binding signature for metalloproteases (HExGHxxGxxHD) in in their metalloprotease domain can potentially be catalytically. Those mammalian their metalloprotease domain and and can potentially be catalytically active. ADAMs contain a conserved consensus binding motif xCD in their disintegrin-like disintegrin‐like domains.
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