Characterization of the cDNA and gene for mouse tumour necrosis factor α converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25

Kurt Poindexter, Beverly J. Castner, Gary Means, Neal G. Copeland, Debra J. Gilbert, Nancy A. Jenkins, Roy A. Black, Nicole Nelson

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Numerous proteins are cleaved or 'shed' from their membrane-bound form. One such protein, tumour necrosis factor α (TNF-α), is synthesized as a type 2 transmembrane protein. Recently, a human protease responsible for this shedding, the TNF-α 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-α. 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.

Original languageEnglish (US)
Pages (from-to)541-551
Number of pages11
JournalCytokine
Volume11
Issue number8
DOIs
StatePublished - Aug 1999

Keywords

  • Converting enzyme
  • Disintegrin
  • TNF-α
  • Zinc metalloprotease

ASJC Scopus subject areas

  • Endocrinology
  • Molecular Biology
  • Immunology
  • Immunology and Allergy

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