Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease
Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease
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DOI:
10.1093/hmg/9.8.1195
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发表时间:
2000-05-01
影响因子:
3.5
通讯作者:
Wanders, RJA
中科院分区:
文献类型:
--
作者:
Jansen, GA;Hogenhout, EM;Wanders, RJA
Refsum's disease (RD) is an inherited neurological syndrome biochemically characterized by the accumulation of phytanic acid in plasma and tissues. Patients with RD are unable to degrade phytanic acid due to a deficient activity of phytanoyl-CoA hydroxylase (PhyH), a peroxisomal enzyme catalysing the first step of phytanic acid alpha-oxidation. To enable mutation analysis of RD at the genome level, we have elucidated the genomic organization of the PHYH gene. The gene is similar to 21 kb and contains nine exons and eight introns. Mutation analysis of PHYH cDNA from 22 patients with RD revealed 14 different missense mutations, a 3 bp insertion, and a 1 bp deletion, which were all confirmed at the genome level. A 111 bp deletion identified in the PHYH cDNA of several patients with RD was due to either one of two different mutations in the same splice acceptor site, which result in skipping of exon 3. Six mutations, including a large in-frame deletion and five missense mutations, were expressed in the yeast Saccharomyces cerevisiae to study their effect on PhyH activity. The results showed that all these mutations lead to an enzymatically inactive PhyH protein.