Shedding light on ADAM metalloproteinases

ADAM metalloproteinase disintegrins have emerged as the major proteinase family that mediates ectodomain shedding, the proteolytic release of extracellular domains from their membrane-bound precursors. Recent gene-manipulation studies have established the role of ADAM-mediated shedding in mammalian...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2005-07, Vol.30 (7), p.413-422
Main Authors: Huovila, Ari-Pekka J., Turner, Anthony J., Pelto-Huikko, Markku, Kärkkäinen, Iivari, Ortiz, Rebekka M.
Format: Article
Language:English
Subjects:
Amyloid beta-Protein Precursor - metabolism
Animals
Humans
Membrane Proteins - metabolism
Metalloendopeptidases - genetics
Metalloendopeptidases - physiology
Mitogen-Activated Protein Kinases - metabolism
Receptors, Notch
Signal Transduction - physiology
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Summary:ADAM metalloproteinase disintegrins have emerged as the major proteinase family that mediates ectodomain shedding, the proteolytic release of extracellular domains from their membrane-bound precursors. Recent gene-manipulation studies have established the role of ADAM-mediated shedding in mammalian physiology and, in addition, raised the issue of functional redundancy among ADAM sheddases. ADAM sheddases activate, for example, growth factors and cytokines, thus regulating signalling pathways that are important in development and pathological processes such as cancer. The recent studies have also begun to elucidate the substrate specificity and the mechanisms that control ADAM-mediated shedding events that regulate, for example, growth-factor and Notch signalling, and the processing of the amyloid precursor protein.
ISSN:0968-0004
1362-4326
DOI:10.1016/j.tibs.2005.05.006