Molecular basis of Refsum disease: Identification of new mutations in the phytanoyl-CoA hydroxylase cDNA

Journal of Inherited Metabolic Disease

Volumn 21, Issue 3, 1998, Pages 288-291

  Jansen, G A ^a   Ferdinandusse, S ^a   Skjeldal, O H ^b   Stokke, O ^b   De Groot, C J ^c   Jakobs, C ^d   Wanders, R J A ^a,c  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b OSLO UNIVERSITY HOSPITAL   (Norway)

^c EMMA CHILDREN S HOSPITAL   (Netherlands)

^d VU UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; PHYTANIC ACID;

CLINICAL ARTICLE; CONFERENCE PAPER; GENE MUTATION; GENETIC ANALYSIS; HETEROZYGOTE; HOMOZYGOTE; HUMAN; NUCLEOTIDE SEQUENCE; REFSUM DISEASE;

AMINO ACID SUBSTITUTION; CELLS, CULTURED; DNA, COMPLEMENTARY; FIBROBLASTS; HUMANS; MIXED FUNCTION OXYGENASES; MUTATION; REFSUM DISEASE; SEQUENCE ANALYSIS, DNA;

EID: 0031879590     PISSN: 01418955     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005388710197     Document Type: Conference Paper

References (9)

1. IJlst L, Wanders RJA, Ushikubo S, Kamijo T, Hashimoto T (1994) Molecular basis of longchain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein. Biochim Biophys Acta 1215: 347-350.
2. Jansen GA, Mihalik SJ, Watkins PA, et al (1996) Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes, and deficient in Zellweger syndrome: direct, unequivocal evidence for the new, revised pathway of phytanic acid alpha-oxidation in humans. Biochem Biophys Res Commun 229: 205-210.
3. Jansen GA, Wanders RJA, Watkins PA, Mihalik SJ (1997a) Phytanoyl-coenzyme A hydroxylase deficiency: the enzyme defect in Refsum's disease. N Engl J Med 337: 133-134.
4. Jansen GA, Ofman R, Ferdinandusse S, et al (1997b) Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nature Genet 17: 190-194.
5. Mihalik SJ, Rainville AM, Watkins PA (1995) Phytanic acid alpha-oxidation in rat liver peroxisomes. Production of alpha-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur J Biochem 232: 545-551.
6. Steinberg D (1995) Refsum disease. In Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic and Molecular Bases of Inherited Disease, 7th edn. New York: McGraw-Hill, 2351-2369.
7. ten Brink HJ, Schor DSM, Kok RM, Poll-The BT, Wanders RJA, Jakobs C (1992) Phytanic acid alpha-oxidation: accumulation of 2-hydroxyphytanic acid and absence of 2-oxophytanic acid in plasma from patients with peroxisomal disorders. J Lipid Res 33: 1449-1457.
8. Watkins PA, Howard AE, Mihalik SJ (1994) Phytanic acid must be activated to phytanoyl-CoA prior to its alpha-oxidation in rat liver peroxisomes. Biochim Biophys Acta 1214: 288-294.
9. Watkins PA, Howard AE, Gould SJ, Avigan J, Mihalik SJ (1996) Phytanic acid activation in rat liver peroxisomes is catalyzed by long-chain acyl-CoA synthetase. J Lipid Res 37: 2288-2295.