Further genetic heterogeneity in acatalasemia

Abstract

A T-deletion at position 10 of exon 4 for catalase gene was reported as a novel mutation, causing a new genetic type of acatalasemia in Japan. This mutation, destroying a Hinf1 recognition site, was searched for in Hungarian acatalasemic (2) and hypocatalasemic (22) patients and in controls (27) by Hinf1 digestion and sequence analyses of a 203 bp polymerase chain reaction (PCR) product containing the entire exon 4. The Hinf1 polymorphism did not reveal any difference between controls and hypocatalasemic as well as acatalasemic patients. These results were confirmed by sequence analyses showing the T nucleotide for the two acatalasemic and for one unrelated hypocatalasemic patient, as well as for two controls. These findings represent further evidence that acatalasemia is heterogeneous at the DNA level.

Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus

“…In contrast, none of the 66 normocatalasemic family members suffered from diabetes mellitus [13,14]. Genetic analysis of these families showed that the known types of Japanese acatalasemia (2) were not found in the Hungarian families [15,16].…”

A novel catalase mutation detected by polymerase chain reaction-single strand conformation polymorphism, nucleotide sequencing, and Western blot analyses is responsible for the type C of Hungarian acatalasemia

“…We have reported on two acatalasemic sisters in the first Hungarian acatalasemic family [9] and nine hypocatalasemic families [10] with 37 hypocatalasemics including the biochemical markers of lipid and carbohydrate metabolism in acatalasemia and hypocatalasemia [11]. In Hungarian acatalasemic and hypocatalasemic patients, we could not detect the mutations responsible for the defect catalase synthesis in Japanese patients [12,13]. For the acatalasemic and three hypocatalasemic families, we found a GA insertion at position 138 of exon 2.…”

Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair

“…In step two, compound I oxidizes a second peroxide molecule to molecular oxygen and releases the ferryl oxygen species as water. Several catalase crystal structures have been determined, aiding our understanding of reactive oxygen control by defining the reaction and inhibition mechanisms (Goth, 1997). These studies include the definition of the chemistry of the human catalase, through structures of the resting-state enzyme and complexes of a catalase bound to cyanide and 3AT inhibitors (Putnam et al, 2000).…”