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An essential role for ectodomain shedding in mammalian development.
Peschon JJ, Slack JL, Reddy P, Stocking KL, Sunnarborg SW, Lee DC, Russell WE, Castner BJ, Johnson RS, Fitzner JN, Boyce RW, Nelson N, Kozlosky CJ, Wolfson MF, Rauch CT, Cerretti DP, Paxton RJ, March CJ, Black RA
(1998) Science 282: 1281-4
MeSH Terms: ADAM Proteins, ADAM17 Protein, Amino Acid Sequence, Animals, Catalytic Domain, Cell Membrane, Cells, Cultured, Crosses, Genetic, Embryonic and Fetal Development, L-Selectin, Ligands, Membrane Proteins, Metalloendopeptidases, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Mutation, Phenotype, Protein Processing, Post-Translational, Receptors, Tumor Necrosis Factor, Transforming Growth Factor alpha, Tumor Necrosis Factor-alpha
Show Abstract · Added December 10, 2013
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.
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