J. Zou et al., Molecular cloning of interleukin 1 beta from rainbow trout Oncorhynchus mykiss reveals no evidence of an ice cut site, CYTOKINE, 11(8), 1999, pp. 552-560
The complete coding sequence of rainbow trout IL-1 beta has been obtained.
The gene contains a short 5' UTR (97 bp), a 780 bp open reading frame and a
466 6p 3' UTR, which includes a polyadenylation signal, 7 ATTTA motifs and
an 18 bp poly ii tail. The predicted amino acid sequence (260 amino acids)
contains 3 potential glycosylation sites, with a predicted molecular weigh
t of 29 kDa, and show's between 49 and 56% amino acid similarity to mammali
an IL-1 beta s and 57% similarity to carp IL-1 beta, Greatest homology was
apparent within the secondary structure of the gene, with few of the amino
acids known to bind to the IL-1 receptor being conserved. No ICE cut site w
as apparent but multiple alignment with mammalian sequences allowed a putat
ive mature peptide of 166 amino acids to be identified, in which Ala(95) wo
uld be the amino terminus. Northern blot analysis showed that whilst no IL-
1 beta expression was detectable in head kidney leukocytes immediately afte
r isolation, expression could be induced by stimulation with LPS for 4 h in
culture. Similarly, with isolated head kidney macrophages expression was s
ignificantly increased following stimulation with LPS. (C) 1999 Academic Pr
ess.