Purification of ADAM 10 from bovine spleen as a TNFα convertase |
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Authors: | Charles A Lunn Xuedong Fan Barbara Dalie Kenneth Miller Paul J Zavodny Satwant K Narula Daniel Lundell |
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Institution: | Department of Immunology, Schering-Plough Research Institute, Kenilworth, NJ 07033, USA |
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Abstract: | We have purified a protease with characteristics of TNFα convertase from bovine spleen membranes. Peptide sequencing of the purified protein identified it as ADAM 10 (Genbank accession no. Z21961). This metalloprotease cleaves a recombinant proTNFα substrate to mature TNFα, and can cleave a synthetic peptide substrate to yield the mature TNFα amino terminus in vitro. The enzyme is sensitive to a hydroxamate inhibitor of MMPs, but insensitive to phosphoramidon. In addition, cloned ADAM 10 mediates proTNFα processing in a processing-incompetent cell line. |
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Keywords: | Tissue necrosis factor α TNFα convertase ADAM 10 Metalloprotease |
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