Metalloprotease-Disintegrins: Links to Cell Adhesion and Cleavage of TNFα and Notch

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A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions (2016, background): “For this reason these domains are referred to as “disintegrin‐like” domains [8].”
The ADAM metalloproteinases (2008, background): “Our knowledge of the remarkable mammalian ADAM family has come a long way since the discovery of the first members as sperm-associated proteins in the early 1990s (Blobel, 1997) .”
ADAM 23/MDC3, a Human Disintegrin That Promotes Cell Adhesion via Interaction with the αvβ3 Integrin through an RGD-independent Mechanism (2000, unknown): “These recent findings have stimulated the search for new ADAMs potentially associated with some of the conditions involving cell– cell interactions or extracellular matrix degradation taking place during both normal or pathological conditions (Blobel, 1997; Werb, 1997; Wolfsberg and White, 1997).”
Molecular mechanisms in intimal hyperplasia (2000, background): “Many ADAMs have a classical metalloproteinase active site and members are capable of degrading extracellular matrix components, cell surface receptors, and extracellular proteins [122].”
TNFα Shedding in Mechanically Stressed Cardiomyocytes is Mediated by Src Activation of TACE (2015, background): “The pro-TNFa is cleaved and TNFa is shed (secreted) as a 17 kDa protein by TACE, a member of the ADAM family of disintegrin metalloproteinases (also known as ADAM17) [Blobel, 1997; Moss et al., 1997].”