Details

Autor(en) / Beteiligte

• Moss, Marcia L
• Jin, S.-L. Catherine
• Milla, Marcos E
• Burkhart, William
• Carter, H. Luke
• Chen, Wen-Ji
• Clay, William C
• Didsbury, John R
• Hassler, Daniel
• Hoffman, Christine R
• Kost, Thomas A
• Lambert, Millard H
• Leesnitzer, M. Anthony
• McCauley, Philip
• McGeehan, Gerard
• Mitchell, Justin
• Moyer, Mary
• Pahel, Gregory
• Rocque, Warren
• Overton, Laurie K
• Schoenen, Frank
• Seaton, Theresa
• Su, Jui-Lan
• Warner, Janet
• Willard, Derril
• Becherer, J. David

Titel

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

Ist Teil von

• Nature (London), 1997-02, Vol.385 (6618), p.733-736

Ort / Verlag

London: Nature Publishing

Erscheinungsjahr

1997

Quelle

MEDLINE

Beschreibungen/Notizen

• Tumour-necrosis factor-alpha (TNF-alpha) is a cytokine that contributes to a variety of inflammatory disease states. The protein exists as a membrane-bound precursor of relative molecular mass 26K which can be processed by a TNF-alpha-converting enzyme (TACE), to generate secreted 17K mature TNF-alpha. We have purified TACE and cloned its complementary DNA. TACE is a membrane-bound disintegrin metalloproteinase. Structural comparisons with other disintegrin-containing enzymes indicate that TACE is unique, with noteable sequence identity to MADM, an enzyme implicated in myelin degradation, and to KUZ, a Drosophila homologue of MADM important for neuronal development. The expression of recombinant TACE (rTACE) results in the production of functional enzyme that correctly processes precursor TNF-alpha to the mature form. The rTACE provides a readily available source of enzyme to help in the search for new anti-inflammatory agents that target the final processing stage of TNF-alpha production.