Refsum disease is caused by mutations in the phytanoyl-coa hydroxylase gene

Nature Genetics

Volumn 17, Issue 2, 1997, Pages 193-

  Jansen, Gerbert A ^a   Ofman, Rob ^a   Ferdinandusse, Sacha ^a   Ijlst, Lodewijk ^a   Muijsers, Anton O ^b   Stokke, Oddvar ^c   Jakobs, Cornells ^d   Besley, Guy T N ^e   Wraith, J E ^e   Wanders, Ronald J A ^a,b  

^a Department of Clinical Biochemistry ^*  (Netherlands)

^b UNIVERSITY OF AMSTERDAM   (Netherlands)

^c OSLO UNIVERSITY HOSPITAL   (Norway)

^d VU UNIVERSITY MEDICAL CENTER   (Netherlands)

^e ROYAL MANCHESTER CHILDREN S HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MIXED FUNCTION OXIDASE; PHYH PROTEIN, HUMAN; PHYH PROTEIN, RAT; PRIMER DNA;

ADULT; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CASE CONTROL STUDY; CASE REPORT; ENZYMOLOGY; FEMALE; GENE DELETION; GENE EXPRESSION; GENETICS; HUMAN; INFANT; ISOLATION AND PURIFICATION; LIVER; MALE; MICROBODY; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; POINT MUTATION; POLYMERASE CHAIN REACTION; RAT; REFSUM DISEASE;

ADULT; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CASE-CONTROL STUDIES; DNA PRIMERS; DNA, COMPLEMENTARY; FEMALE; GENE EXPRESSION; HUMANS; INFANT; LIVER; MALE; MICROBODIES; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; MUTATION; POINT MUTATION; POLYMERASE CHAIN REACTION; RATS; REFSUM DISEASE; SEQUENCE DELETION;

EID: 84984777129     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1097-190     Document Type: Article

References (22)

1. Refsum, S. Heredopathia atactica polyneuritiformis. Acta Psychiatr. Scand. (Suppl.) 38, 9-303(1946).
2. Steinberg, D. Refsum disease, in The Metabolic and Molecular Basis of Inherited Disease, 7th ed. (eds Scriver, C.R., Beaudet, A.L, Sly, W.S. & Valle, D.) 2351- 2369 (McGraw-Hill, New York, 1995).
3. Skjeldal, O.H., Stokke, O., Refsum, S., Norseth, J. & Petit H. Clinical and biochemical heterogeneity in conditions with phytanic acid accumulation. J. Neurol. Sci. 77, 87-96(1987).
4. Mihalik, S.J., Rainville, A.M. & Watkins, P.A. Phytanic acid α-oxidation in rat liver peroxisomes: Production of α-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur. J. Biochem. 232, 545-551 (1995).
5. Jansen, G.A. et al. 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 α-oxidation in humans. Biochem. Biophys. Res. Commun. 229, 205-210 (1996).
6. 2, cofactor requirements, subcellular localization and formation of a 2-hydroxy-3-methylacyl-CoA intermediate. Fur. J. Biochem. 240, 674-683 (1996).
7. Jansen, G.A. et al. Phytanoyl-CoA hydroxylase is not only deficient in classical Refsum disease but also in rhizomelic chondrodysplasia punctata. J. Inherited Metab. Dis. 20, 444-446 (1997).
8. Jansen, G.A., Wanders, R.J.A., Watkins, P.A. & Mihalik, S.J. Phytanoyl-coenzyme A hydroxylase deficiency—the enzyme defect in Refsum’s disease. N. Engl. J. Med. 337, 133-134(1997).
9. Lazarow, P.B. & Moser H.W. Disorders of peroxisome biogenesis, in The Metabolic and Molecular Basis of Inherited Disease, 7th ed. (eds Scriver, C.R., Beaudet A.L, Sly, W.S. & Valle, D.) 2287-2324 (McGraw-Hill, New York, 1995).
10. Motley, A.M. et al. Rhizomelic chondrodysplasia punctata is a peroxisomal protein targeting disease caused by a non-functional PTS2 receptor. Nature Genet. 15, 377-380(1997).
11. Purdue, P.E., Zhang, J.W., Skoneczny, M. & Lazarow, P.B. Rhizomelic chondrodysplasia punctata is caused by deficiency of human PEX7, a homologue of the yeast PTS2 receptor. Nature Genet. 15, 381-384 (1997).
12. Braverman, N. et al. Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata. Nature Genet. 15, 369-375(1997).
13. Waterham, H.R. & Cregg, J.M. Peroxisome biogenesis. Bioessays 19, 57-66 (1997).
14. Subramani, S. PEXgenes on the rise. Nature Genet. 15, 331-333 (1997).
15. Purdue, P.E. & Lazarow, P.B. Peroxisomal biogenesis: Multiple pathways of protein import. J Biol. Chem. 269, 30065-30068(1994).
16. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. & Lipman, D.J. Basic local alignment search tool. J. Mol. Biol. 215, 403-410 (1990).
17. Kozak, M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 12, 857-872 (1984).
18. Swinkels, B.W., Gould, S.J., Bodnar, A.G., Rachubinski, R.A. & Subramani, S. A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoAthiolase. EMBO J. 10, 3255-3262 (1991).
19. DeVet, E.C.J.M., Zomer, A.W.M., Lahaut G.J.H.T.J. & van den Bosch, H. Polymerase chain reaction-based cloning of alkyl-dihydroxyacetonephosphate synthase complementary DNA from guinea pig liver. J. Biol. Chem. 272, 798-803 (1997).
20. Osumi, T. et al. Amino-terminal presequence of the precursor of peroxisomal 3-ketoacyl-CoA thiolase is a cleavable signal peptide for peroxisomal targeting. Biochem. Biophys. Res. Commun. 181, 947-954 (1991).
21. Krawczak, M., Reiss, J. & Cooper, D.N. The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: Causes and consequences. Hum. Genet 90, 41-54 (1992).
22. Ijlst, L., Wanders, R.J.A., Ushikubo, S., Kamijo, T. & Hashimoto, T. Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: Identification of the major disease-causing mutation in the α-subunit of the mitochondrial trif unctional protein. Biochim. Biophys. Acta 1215, 347-350(1994).