Abstract
The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-alpha converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-alpha (TNFalpha) 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, the L-selectin adhesion molecule, and transforming growth factor-alpha (TGFalpha). The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ADAM Proteins
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ADAM17 Protein
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Amino Acid Sequence
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Animals
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Catalytic Domain
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Cell Membrane / metabolism*
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Cells, Cultured
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Crosses, Genetic
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Embryonic and Fetal Development*
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L-Selectin / metabolism
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Ligands
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Membrane Proteins / metabolism*
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Metalloendopeptidases / chemistry
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism*
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Mice
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Mice, Inbred C57BL
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Molecular Sequence Data
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Mutation
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Phenotype
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Protein Processing, Post-Translational
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Receptors, Tumor Necrosis Factor / metabolism
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Transforming Growth Factor alpha / metabolism
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Tumor Necrosis Factor-alpha / metabolism*
Substances
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Ligands
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Membrane Proteins
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Receptors, Tumor Necrosis Factor
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Transforming Growth Factor alpha
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Tumor Necrosis Factor-alpha
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L-Selectin
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ADAM Proteins
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Metalloendopeptidases
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ADAM17 Protein
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Adam17 protein, mouse