ReviewMethods in molecular biology (Clifton, N.J.)2026
An Overview of ADAMTS Proteases.
Review in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The ADAMTS superfamily comprises 19 secreted metalloproteases (ADAMTS proteases) and seven structurally related secreted proteins without catalytic activity (ADAMTS-like proteins). Members of both families participate in diverse and numerous processes in a variety of tissues and organs during embryo development and in connective tissue maintenance and hemostasis in the adult. The functional relationships between the two families are unclear, although most ADAMTS roles can be attributed to proteolytic actions and most ADAMTS-like roles to their functions as matricellular proteins. ADAMTS proteases are implicated in human and animal Mendelian disorders and are key participants in acquired disease pathways, including inflammatory and degenerative conditions. Several spontaneous mutations and genetically engineered invertebrate and mammalian (mostly mouse) models have been used to uncover ADAMTS biological roles in organogenesis and to define their cellular impact and underlying mechanisms. Despite their profound biological and medical importance, detailed knowledge about ADAMTS molecular structures, substrates, or binding partners and biochemical mechanisms is still limited. ADAMTS2, ADAMTS5, and ADAMTS13 have previously been extensively investigated because of their obvious clinical relevance, but much less is known about other ADAMTS proteases and most ADAMTS-like proteins. Here, the essential background and concepts relevant to this superfamily of proteins are discussed.
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