Abstract
ADAMs contain adhesive and metalloprotease domains. As major ectodomain sheddases, they release a variety of cell-surface proteins, including growth factors, cytokines, cell adhesion molecules and receptors. ADAMs can also cleave and remodel components of the extracellular matrix. Hence, ADAMs are emerging as key modulators of cell-cell and cell-matrix interactions. Important questions, including if and how ADAM adhesive domains promote ADAM protease function, are currently being addressed.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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ADAM Proteins
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ADAM10 Protein
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ADAM12 Protein
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Amyloid Precursor Protein Secretases
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Animals
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Cell Communication / physiology*
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Disintegrins / metabolism*
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Extracellular Matrix / metabolism*
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Growth Substances / metabolism
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Heparan Sulfate Proteoglycans / metabolism
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Integrins / metabolism
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Membrane Proteins / metabolism*
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Metalloendopeptidases / metabolism*
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Protein Binding
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Protein Structure, Tertiary
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Xenopus / metabolism
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Xenopus Proteins / metabolism
Substances
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Disintegrins
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Growth Substances
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Heparan Sulfate Proteoglycans
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Integrins
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Membrane Proteins
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Xenopus Proteins
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Amyloid Precursor Protein Secretases
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ADAM Proteins
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ADAM12 Protein
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ADAM12 protein, human
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ADAM15 protein, human
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ADAM33 protein, Xenopus
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ADAM9 protein, human
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Metalloendopeptidases
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ADAM10 Protein
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ADAM10 protein, human