Literature DB >> 10826695

Cloning and sequencing of feline and canine ice-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides.

S Taylor1, L Hanlon, C McGillivray, E A Gault, D J Argyle, D E Onions, L Nicolson.   

Abstract

Caspases are cysteine proteases which have important roles in the activation of cytokines and in apoptosis. The ICE subfamily of caspases comprise peptides closely related to caspase-1, or interleukin-1beta (IL-1beta) converting enzyme (ICE), which promotes maturation of interleukin IL-1beta and interleukin-18 (IL-18) by proteolytic cleavage of precursor forms to generate biologically active peptides. Other members of this subfamily include caspase-4, -5, -13 and isoforms of these proteins. We report the cloning and sequencing of two feline and canine ICE-related cDNAs amplified by RT-PCR. The predicted proteins are 410 and 404 amino acids in length respectively and are most closely related to caspase-1 sequences across the N-terminal 115 amino acids and to human caspase-13 across the C-terminal sequence.

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Year:  2000        PMID: 10826695     DOI: 10.3109/10425170009015606

Source DB:  PubMed          Journal:  DNA Seq        ISSN: 1026-7913


  1 in total

Review 1.  Lipopolysaccharide detection by the innate immune system may be an uncommon defence strategy used in nature.

Authors:  Anna E Gauthier; Randi D Rotjan; Jonathan C Kagan
Journal:  Open Biol       Date:  2022-10-05       Impact factor: 7.124

  1 in total

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