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Purification of ADAM 10 from bovine spleen as a TNFalpha convertase
1Department of Immunology, Schering-Plough Research Institute, Kenilworth, NJ 07033, USA. charles.lunn@spcorp.com
FEBS Letters
|January 6, 1997
Abstract:
We have purified a protease with characteristics of TNFalpha 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 proTNFalpha substrate to mature TNFalpha, and can cleave a synthetic peptide substrate to yield the mature TNFalpha amino terminus in vitro. The enzyme is sensitive to a hydroxamate inhibitor of MMPs, but insensitive to phosphoramidon. In addition, cloned ADAM 10 mediates proTNFalpha processing in a processing-incompetent cell line.