Genomic and mutational analysis of the mitochondrial trifunctional protein β-subunit (HADHB) gene in patients with trifunctional protein deficiency

Human Molecular Genetics

Volumn 6, Issue 8, 1997, Pages 1215-1224

  Orii, Kenji E ^a,b   Aoyama, Toshifumi ^b   Wakui, Keiko ^b   Fukushima, Yoshimitsu ^b   Miyajima, Hiroaki ^c   Yamaguchi, Seiji ^d   Orii, Tadao ^e   Kondo, Naomi ^a   Hashimoto, Takashi ^b  

^a GIFU UNIVERSITY   (Japan)

^b SHINSHU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c HAMAMATSU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^d SHIMANE UNIVERSITY   (Japan)

^e CHUBU GAKUIN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; ACETYL COENZYME A ACYLTRANSFERASE; ENOYL COENZYME A HYDRATASE; MITOCHONDRIAL ENZYME;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENCEPHALOMYOPATHY; ENZYME ACTIVITY; ENZYME DEFICIENCY; ENZYME SUBUNIT; FIBROBLAST; GENE INSERTION; GENE MUTATION; HEPATIC ENCEPHALOPATHY; HETEROZYGOTE; HOMOZYGOTE; HUMAN; HUMAN CELL; HYPERTROPHIC CARDIOMYOPATHY; LIVER FAILURE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; RNA SPLICING; SUDDEN INFANT DEATH SYNDROME;

ANIMALS; BASE SEQUENCE; CHO CELLS; CHROMOSOME MAPPING; CRICETINAE; DNA MUTATIONAL ANALYSIS; DNA, COMPLEMENTARY; GENE EXPRESSION; HUMANS; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES;

ANIMALIA;

EID: 0030856404     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/6.8.1215     Document Type: Article

References (46)

1. Izai, K., Uchida, Y., Orii, T., Yamamoto, S., and Hashimoto, T. (1992) Novel fatty acid β-oxidation enzymes in rat liver mitochondria, I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem., 267, 1027-1033.
2. Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K., and Hashimoto, T. (1995) Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J. Clin. Invest., 95, 2465-2473.
3. Aoyama, T., Ueno, I., Kamijo, T., and Hashimoto, T. (1994) Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in long-chain fatty acid β-oxidation system. J. Biol. Chem., 269, 19088-19094.
4. Carpenter, K., Pollitt, R.J., and Middleton, B. (1992) Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membranebound beta-oxidation enzyme of mitochondria. Biochem. Biophys. Res. Commun., 183, 443-448.
5. Uchida, Y., Izai, K., Orii, T., and Hashimoto, T. (1992) Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein. J. Biol. Chem., 267, 1034-1041.
6. Kamijo, T., Aoyama, T., Miyazaki, J., and Hashimoto, T. (1993) Molecular cloning of the cDNA for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex: structural and functional relationships to other milochondrial and peroxisomal β-oxidation enzymes. J. Biol. Chem., 268, 26452-26460.
7. Wanders, R.J.A., Duran, M., IJlst, L., de Jager,J.P., van Gennip, A.H., Jakobs, C., Dorland, L., and Van Sprang, F.J. (1989) Sudden infant death and long-chain 3-hydroxyacyl-CoA dehydrogenase. Lancet, i, 52-53.
8. IJlst, L., Ushikubo, S., Kamijo, T., Hashimoto, T., Ruiter, J.P.N., de Klerk, J.B.C., and Wanders, R.J.A. (1995) Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: high frequency of the G1528C mutation with no apparent correlation with the clinical phenotype. J. Inher. Metab. Dis., 18, 241-244.
9. Sewell, A.C., Bender, S.W., Wirth, S., Münterfering, H., IJlst, L., and Wanders, R.J. A. (1994) Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: a severe fatty acid oxidation disorder. Eur. J. Pediatr., 153, 745-750.
10. Jackson, S., Kler, R.S., Bartlett, K., Briggs, H., Bindoff, L.A., Pourtarzam, M., Gardner-Medwin, D., and Tumbull. D. M. (1992) Combined enzyme defect of mitochondrial fatty acid oxidation. J. Clin. Invest., 90, 1219-1225.
11. Kamijo, T., Wanders, R.J.A., Saudubray, J.M., Aoyama, T., Komiyama, A., and Hashimoto, T. (1994) Mitochondrial trifunctional protein deficiency: catalytic heterogeneity of the mutant enzyme in two patients. J. Clin. Invest., 93, 1740-1747.
12. Wanders, R.J.A., IJlst, L., Poggi, F., Bonnefont, J.P., Munnich, A., Brivet, M., Rabier, D., and Saudubray, J.M. (1992) Human trifunctional protein deficiency: a new disorder of mitochondrial fatty acid β-oxidation. Biochem. Biophys. Res. Commun., 188, 1139-1145.
13. IJlst, L., Wanders, R.J.A., Ushikubo, S., Kamijo, T., and Hashimoto, T. (1994) Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the α-subunit of the mitochondrial trifunctional protein. Biochim. Biophys. Acta, 1215, 347-350.
14. IJlst, L., Ruiter, J.P.N., Vreijling, J., and Wanders, R.J.A. (1996) Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: a new method to identify the G1528C mutation in genomic DNA showing its high frequency (∼90%) and identification of a new mutation (T2198C). J. Inher. Metab. Dis., 19, 165-168.
15. Isaacs, J.D., Sims, H.F., Powell, C.K., Bennett, M.J., Hale, D.E.,Treem, W.R., and Strauss, A.W. (1996) Maternal acute fatty liver of pregnancy associated with fetal trifunctional protein deficiency: Molecular characterization of a novel maternal mutant allele. Pediatr. Res., 40, 393-398.
16. Sims, H.F., Brackett, J.C., Powell, C.K., Treem, W.R., Hale, D.E., Bennett, M.J., Gibson, B., Shapiro, S., and Strauss, A.W. (1995) The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy. Proc. Natl. Acad. Sci. USA, 92, 841-845.
17. Brackett, J.C., Sims, H.F., Rinaldo, P., Shapiro, S., Powell, C.K., Bennett, M.J., and Strauss, A.W. (1995) Two α subunit donor splice site mutations cause human trifunctional protein deficiency. J. Clin. Invest., 95, 2076-2082.
18. Ushikubo, S., Aoyama,T., Kamijo, T., Wanders, R.J.A., Rinaldo, P., Vockley, J., and Hashimoto, T. (1996) Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both α- and β-subunits. Am. J. Hum. Genet., 58, 979-988.
19. Dionisi-Vici, C., Garavaglia, B., Burlina, A.B., Bertini, E., Saponara, I., Sabetta, G., and Taroni, F. (1996) Hypoparathyroidism in mitochondrial trifunctional protein deficiency. J. Pediatr., 129, 159-162.
20. Zhang, Q.X., and Baldwin, G.S. (1994) Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene. Biochim. Biophys. Acta, 1219, 567-575.
21. IJlst, L., Ruiter, J.P.N., Hoovers, J.M.N., Jakobs, M.E., and Wanders, R.J.A. (1996) Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein α subunit gene. J. Clin. Invest., 98, 1028-1033.
22. Shapiro, M.B., and Senapathy, P. (1987) RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucleic Acids Res., 15, 7155-7174.
23. Kamijo, T., Aoyama, T., Komiyama, A., and Hashimoto, T. (1994) Structural analysis of cDNA for subunits of human mitochondrial fatty acid β-oxidation trifunctional protein. Biochem. Biophys. Res. Commun., 199, 818-825.
24. Yang, B-Z., Heng, H.H.Q., Ding, J-H., and Roe C.R. (1996) The genes for the α and βsubunits of the mitochondrial trifunctional protein are both located in the same region of the human chromosome 2p23. Genomics, 37, 141-143.
25. Niwa, H., Yamamura, K., and Miyazaki, J. (1991) Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene, 108, 193-200.
26. Newton, C.R., Graham, A., Heptinstall, L.E., Powell, S.J., Summers, C., Kalsheker, N., Smith, J.C., and Markham, A.F. (1989) Analysis of any point mutation in DNA. The amplification refractory mutation system (ARMS). Nucleic Acids Res., 17, 2503-2516.
27. Jackson, S., Schaefer, J., Middleton, B., and Turnbull, D.M. (1995) Characterization of a novel enzyme of human fatty acid β-oxidation: a matrix-associated, mitochondrial 2-enoyl-CoA hydratase. Biochem. Biophys. Res. Commun., 214, 247-253.
28. Shaefer, J., Jackson, S., Dick, D.J., and Tumbull, D.M. (1996) Trifunctional enzyme deficiency: adult presentation of a usually fatal β-oxidation defect. Ann.. Neurol., 40, 597-602.
29. Miyajima, H., Orii, K.E., Shindo, Y., Hashimoto, T., Shinka, T., Kuhara, T., Matsumoto, T., Shimizu, H., and Kaneko, E. (1997) Mitochondrial trifunctional protein deficiency associated with recurrent myoglobinuria in adolescence. Neurology, in press.
30. Humphrey, M.B., Bryan, J., Cooper, T.A., and Berget, S.M. (1995) A 32-nucleotide exon-splicing enhancer regulates usage of competing 5′ splice sites in a differential internal exon. Mol Cell. Biol., 15, 3979-3988.
31. Tanaka, K., Watakabe, A., and Shimura, Y. (1994) Polypurine sequences within a downstream exon function as a splicing enhancer. Mol. Cell, Biol., 14, 1347-1354.
32. Orii, K.E., Aoyama, T., Souri, M., Jiang, L.L., Orii, K.O., Hayashi, S., Yamaguchi, S., Kondo, N., Orii, T., and Hashimoto, T. (1996) Formation of the enzyme complex in mitochondria is required for function of trifunctional β-oxidation protein. Biochem. Biophys. Res. Commun., 219, 773-777.
33. Wieland, T., and Rueff, L. (1953) Synthese von S-β-oxybutyryl- und S-acetacelyl-coenzyme A. Angew. Chem., 65, 186-187.
34. Imamura, S., Ueda, S., Mizugaki, M., and Kawaguchi, A. (1990) Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of the fatty acid oxidation system. J. Biochem., 107, 184-189.
35. Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA, 74, 5463-5467.
36. Aoyama, T., Wakui, K., Fukushima, Y., Orii, K.O., and Hashimoto, T. (1996) Assignment of the human mitochondrial very-long-chain acyl-CoA dehydrogenase gene (LCACD) to 17p13 by in situ hybridization. Genomics, 37, 144-145.
37. KIP2 and its reduced expression in Wilms' tumors. Hum Mol. Genet., 5, 783-788.
38. Furuta, S., Miyazawa, S., Osumi, T., Hashimoto, T., and Ui, N.(1980) Properties of mitochondrial and peroxisomal enoyl-CoA hydratases from rat liver. J. Biochem., 88, 1059-1070.
39. Osumi, T., and Hashimoto, T. (1979) Occurrence of two 3-hydroxyacyl-CoA dehydrogenases in rat liver. Biochim. Biophys. Acta, 574, 258-267.
40. Osumi, T., and Hashimoto, T. (1980) Purification and properties of milochondrial and peroxisomal 3-hydroxyacyl-CoA dehydrogenase from rat liver. Arch. Biochem. Biophys., 203, 372-383.
41. Markwell, M.A., Haas, S.M., Bieber, L.L., and Tolbert, N.B. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem., 87, 206-210.
42. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275.
43. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
44. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA, 76, 4350-4354.
45. Chomczynski, P., and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem., 162, 156-159.
46. Graham, F.L., and van der Eb, A.J. (1973) A new technique for the assay of infectivity of human adenovirus IV DNA. Virology, 52, 456-467.