An Essential Role for Ectodomain Shedding in Mammalian Development
- 13 November 1998
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 282 (5392), 1281-1284
- https://doi.org/10.1126/science.282.5392.1281
Abstract
The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-α converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-α (TNFα) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, thel-selectin adhesion molecule, and transforming growth factor-α (TGFα). The phenotype of mice lacking TACE suggests an essential role for soluble TGFα in normal development and emphasizes the importance of protein ectodomain shedding in vivo.Keywords
This publication has 34 references indexed in Scilit:
- A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cellsNature, 1997
- Diverse Cell Surface Protein Ectodomains Are Shed by a System Sensitive to Metalloprotease InhibitorsOnline Journal of Public Health Informatics, 1996
- Metalloproteinase-mediated Regulation of L-selectin Levels on LeucocytesOnline Journal of Public Health Informatics, 1996
- Proteolytic Release of Membrane-Bound Angiotensin-Converting Enzyme: Role of the Juxtamembrane Stalk SequenceBiochemistry, 1996
- ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.The Journal of cell biology, 1995
- Mutational analysis of the membrane-proximal cleavage site of L-selectin: relaxed sequence specificity surrounding the cleavage site.The Journal of Experimental Medicine, 1995
- Strain-Dependent Epithelial Defects in Mice Lacking the EGF ReceptorScience, 1995
- Biosynthesis and Processing by Phorbol Ester of the Cell Surface-Associated Precursor Form of Heparin-Binding EGF-like Growth FactorBiochemical and Biophysical Research Communications, 1994
- A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusionNature, 1992
- Overexpression of TGFα in transgenic mice: Induction of epithelial hyperplasia, pancreatic metaplasia, and carcinoma of the breastCell, 1990