A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells

@article{Black1997AMD,
  title={A metalloproteinase disintegrin that releases tumour-necrosis factor-$\alpha$ from cells},
  author={Roy A. Black and Charles T. Rauch and Carl J. Kozlosky and Jacques J. Peschon and Jennifer L. Slack and Martin F. Wolfson and Beverly J. Castner and Kim L. Stocking and Pranitha Reddy and Subhashini Srinivasan and Nicole Nelson and Norman Boiani and Kenneth Schooley and Mary J. Gerhart and Raymond Davis and Jeffrey N. Fitzner and Richard S. Johnson and Raymond J. Paxton and Carl J. March and Douglas Pat Cerretti},
  journal={Nature},
  year={1997},
  volume={385},
  pages={729-733}
}
Mammalian cells proteolytically release (shed) the extracellular domains of many cell-surface proteins1. Modification of the cell surface in this way can alter the cell's responsiveness to its environment2 and release potent soluble regulatory factors3. The release of soluble tumour-necrosis factor-α (TNF-α) from its membrane-bound precursor4,5 is one of the most intensively studied shedding events because this inflammatory cytokine is so physiologically important6,7. The inhibition of TNF… 
Pro-Tumor Necrosis Factor-α Processing Activity Is Tightly Controlled by a Component That Does Not Affect Notch Processing*
TLDR
Biochemical evidence shows that the component that controls TACE is different from protein kinase C, the only known activator of protein ectodomain shedding, and that this component does not affect biosynthesis or processing of TACE or other metalloprotease disintegrins.
Involvement of a disintegrin and metalloproteinase 10 and 17 in shedding of tumor necrosis factor-alpha.
TLDR
Both ADAM10 and ADAM17 can be a TNF-alpha sheddase and that their significance could be determined by their expression levels and the abundance of tissue inhibitor of metalloproteinases.
The ADAM metalloproteinases
Inhibition of the Metalloproteinase Domain of Mouse TACE
TLDR
Preliminary results suggest that TACE is not involved in the degradation of the ECM proteins tested and does not indirectly participate in ECM degradation by activating MMP-2 or M MP-9.
Functional Analysis of the Domain Structure of Tumor Necrosis Factor-α Converting Enzyme*
TLDR
It is found that TACE must be expressed with its membrane-anchoring domain for phorbol ester-stimulated shedding of TNF, p75 TNFR, and IL-1R-II, but that the cytoplasmic domain is not required for the shedding of these substrates.
Proteasome inhibition activates the transport and the ectodomain shedding of TNF-α receptors in human endothelial cells
TLDR
Evidence is provided that proteasome inhibitors increase TACE-dependent TNFR-shedding in endothelial cells, supporting the use of these molecules in inflammatory disorders and enhancing the sensitivity to the proapoptotic effect of recombinant TNF-α.
Processing of tumor necrosis factor by the membrane-bound TNF-alpha-converting enzyme, but not its truncated soluble form.
TLDR
It is suggested that binding of the membrane-anchored but not the soluble form of TACE to TNF-alpha results in efficient ectodomain shedding, and that FasL secretase is a metalloproteinase similar, but not identical, to TACE.
Tumor Necrosis Factor-α-converting Enzyme Mediates the Inducible Cleavage of Fractalkine*
TLDR
It is reported that tumor necrosis factor-α-converting enzyme (TACE) is primarily responsible for the inducible cleavage of FK, and a potentially important link between local generation of potent cytokines and control of the balance between the cell adhesion and chemotactic properties of Fk is identified.
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