Abstract:
:Numerous proteins are cleaved or "shed" from their membrane-bound form. One such protein, tumour necrosis factor alpha (TNF-alpha), is synthesized as a type 2 transmembrane protein. Recently, a human protease responsible for this shedding, the TNF-alpha converting enzyme (TACE/ADAM17), was isolated. TACE/ADAM17 is a member of the adamalysin class of zinc-binding metalloproteases or ADAM (a disintegrin and metalloprotease). We report the isolation and characterization of the mouse TACE/ADAM17 cDNA and gene. Mouse TACE/ADAM17 has a 92% amino-acid identity with the human protein and was ubiquitously expressed. A recombinant form of the protease is found to cleave a peptide representing the cleavage site of precursor mouse TNF-alpha. An alternatively spliced form of mouse TACE/ADAM17 was found that would produce a soluble protein. The gene for TACE/ADAM17 is approximately 50 kb and contains 19 exons. Chromosomal mapping places TACE/ADAM17 on mouse chromosome 12 and human chromosome 2p25.
journal_name
Cytokinejournal_title
Cytokineauthors
Cerretti DP,Poindexter K,Castner BJ,Means G,Copeland NG,Gilbert DJ,Jenkins NA,Black RA,Nelson Ndoi
10.1006/cyto.1998.0466keywords:
subject
Has Abstractpub_date
1999-08-01 00:00:00pages
541-51issue
8eissn
1043-4666issn
1096-0023pii
S1043-4666(98)90466-5journal_volume
11pub_type
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