Molecular characterization of mouse and rat CPP32β gene encoding a cysteine protease resembling interleukin-1β converting enzyme and CED-3

Todd S.C. Juan, Ian K. McNiece, Nancy A. Jenkins, Debra J. Gilbert, Neal G. Copeland, Frederick A. Fletcher

Research output: Contribution to journalArticle

47 Scopus citations

Abstract

Interleukin-1β converting enzyme (ICE) defines a new class of mammalian cysteine protease that shares strong homology with the Caenorhabditis elegans death gene ced-3, Both ICE and CED-3, when introduced into cultured cells, induce apoptosis, indicating that this type of cysteine protease may play an important role in the process of programmed cell death. Here, we report the cloning of a mouse and rat gene encoding a novel cysteine protease, The putative proteins encoded by these cDNAs contain the conserved sequence (QACRG) necessary for covalent linkage to the substrate as well as the three amino acids responsible for substrate binding and catalysis in ICE. Amino acid sequence analysis indicates that this rodent cysteine protease is the homolog of human CPP32β. Mouse CPP32β mRNA is highly expressed in spleen, and to a lesser degree in brain, lung, liver, and kidney. The mouse CPP32β genomic locus spans a region of approximately 20 kb, including seven exons and six introns. Mouse interspecific backcross mapping allowed localization of CPP32β to the central region of mouse chromosome 8, linked to Scvr, Lpl, Jund1 and Mlr.

Original languageEnglish (US)
Pages (from-to)749-755
Number of pages7
JournalOncogene
Volume13
Issue number4
StatePublished - Sep 30 1996

Keywords

  • Apoptosis
  • CED-3
  • Cysteine protease
  • Gene structure

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

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