The molecular defects in the
catalase gene, levels of m-
RNA and properties of the residual
catalase studied by scientists are reviewed in human (Japanese, Swiss and Hungarian) and non-human (mouse and beagle dog)
acatalasemia with reference to the bioinformatics. Japanese
acatalasemia-I, the G to A transition at the fifth position of intron 4 of the
catalase gene, limited the correct splicing of the
mRNA and synthesized trace
catalase with normal properties. Hungarian
acatalasemia type C showed a splicing mutation. In the Japanese
acatalasemia II and the type A and B of Hungarian
acatalasemia, the deletion or insertion of
nucleotides was observed in the coding regions, and the frame shift altered downstream amino acid sequences and formed truncated
proteins. In the Hungarian
acatalasemia D, the substitution of a
nucleotide in the exon was found. In mouse and beagle dog
acatalasemia, the substitution of
nucleotides in the coding regions was also observed. Studies of residual
catalase in Swiss, mouse and beagle dog
acatalasemia showed that aberrant
catalase protein degrades more quickly than normal
catalase in cells. The experimental research in genetic toxicology concerning the effect of oxidative stressors (
nitrogen monoxide,
nitrogen dioxide and so on) on Japanese acatalasemic blood and acatalasemic mice is described. The clinical features of Japanese and Hungarian acatalasemic subjects are also described.