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
Science. 1998 282 (5392): 1281-4

PMID: 9812885 · DOI:10.1126/science.282.5392.1281

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.

MeSH Terms (22)

ADAM17 Protein ADAM Proteins 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

Connections (1)

This publication is referenced by other Labnodes entities:

Links