Four novel mutations identified in Norwegian patients result in intermittent maple syrup urine disease when combined with the R301C mutation

Molecular Genetics and Metabolism

Volumn 100, Issue 4, 2010, Pages 324-332

  Brodtkorb, Else ^a   Strand, Janne ^a   Backe, Paul Hoff ^a   Lund, Anne Marie ^b   Bjørås, Magnar ^a   Rootwelt, Terje ^b   Rootwelt, Helge ^b   Woldseth, Berit ^b   Eide, Lars ^a  

^a UNIVERSITY OF OSLO   (Norway)

^b OSLO UNIVERSITY HOSPITAL   (Norway)

Author keywords

Branched chain ketoacid dehydrogenase; E2; MUSD

Indexed keywords

2 OXOACID DEHYDROGENASE; ACYLTRANSFERASE; BRANCHED CHAIN AMINO ACID; MESSENGER RNA; DIHYDROLIPOAMIDE ACYLTRANSFERASE; PROTEIN SUBUNIT;

3' UNTRANSLATED REGION; ALLELE; ARTICLE; ATAXIA; CHILD; CLINICAL ARTICLE; CLINICAL FEATURE; COMPLEX FORMATION; CONTROL GROUP; CONTROLLED STUDY; DNA EXTRACTION; ENZYME ACTIVITY; FIBROBLAST; GENE MUTATION; GENE SEQUENCE; GENE STRUCTURE; GENETIC CODE; HETEROZYGOTE; HUMAN; INFORMED CONSENT; LETHARGY; MAPLE SYRUP URINE DISEASE; MISSENSE MUTATION; NEUROLOGICAL COMPLICATION; NONSENSE MUTATION; NORWAY; PRESCHOOL CHILD; PRIORITY JOURNAL; PROTEIN DOMAIN; RNA EXTRACTION; SCHOOL CHILD; AMINO ACID SUBSTITUTION; CHEMISTRY; DECARBOXYLATION; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; INFANT; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PATHOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN SUBUNIT;

ALLELES; AMINO ACID SUBSTITUTION; AMINO ACIDS, BRANCHED-CHAIN; BASE SEQUENCE; CHILD; CHILD, PRESCHOOL; DECARBOXYLATION; DNA MUTATIONAL ANALYSIS; FIBROBLASTS; GENE EXPRESSION REGULATION; HETEROZYGOTE; HUMANS; INFANT; MAPLE SYRUP URINE DISEASE; MOLECULAR SEQUENCE DATA; MUTATION; MUTATION, MISSENSE; NORWAY; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; ACYLTRANSFERASES;

ACER;

EID: 77954657516     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2010.04.017     Document Type: Article

References (30)

1. Chuang D.T., Chuang J.L., Wynn R.M. Lessons from genetic disorders of branched-chain amino acid metabolism. J. Nutr. 2006, 136:243S-249S.
2. Mamer O.A., Reimer M.L. On the mechanisms of the formation of l-alloisoleucine and the 2-hydroxy-3-methylvaleric acid stereoisomers from l-isoleucine in maple syrup urine disease patients and in normal humans. J. Biol. Chem. 1992, 267:22141-22147.
3. Schadewaldt P., Bodner-Leidecker A., Hammen H.W., Wendel U. Significance of l-alloisoleucine in plasma for diagnosis of maple syrup urine disease. Clin. Chem. 1999, 45:1734-1740.
4. Islam M.M., Wallin R., Wynn R.M., Conway M., Fujii H., Mobley J.A., Chuang D.T., Hutson S.M. A novel branched-chain amino acid metabolon: protein-protein interactions in a supramolecular complex. J. Biol. Chem. 2007, 282:11893-11903.
5. Obayashi M., Sato Y., Harris R.A., Shimomura Y. Regulation of the activity of branched-chain 2-oxo acid dehydrogenase (BCODH) complex by binding BCODH kinase. FEBS Lett. 2001, 491:50-54.
6. Lu G., Sun H., She P., Youn J.Y., Warburton S., Ping P., Vondriska T.M., Cai H., Lynch C.J., Wang Y. Protein phosphatase 2Cm is a critical regulator of branched-chain amino acid catabolism in mice and cultured cells. J. Clin. Invest. 2009, 119:1678-1687.
7. Joshi M., Jeoung N.H., Popov K.M., Harris R.A. Identification of a novel PP2C-type mitochondrial phosphatase. Biochem. Biophys. Res. Commun. 2007, 356:38-44.
8. Shimomura Y., Obayashi M., Murakami T., Harris R.A. Regulation of branched-chain amino acid catabolism: nutritional and hormonal regulation of activity and expression of the branched-chain alpha-keto acid dehydrogenase kinase. Curr. Opin. Clin. Nutr. Metab. Care 2001, 4:419-423.
9. Chang C.F., Chou H.T., Chuang J.L., Chuang D.T., Huang T.H. Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. J. Biol. Chem. 2002, 277:15865-15873.
10. Chang C.F., Chou H.T., Lin Y.J., Lee S.J., Chuang J.L., Chuang D.T., Huang T.H. Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex. J. Biol. Chem. 2006, 281:28345-28353.
11. Kato M., Wynn R.M., Chuang J.L., Brautigam C.A., Custorio M., Chuang D.T. A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex. EMBO J. 2006, 25:5983-5994.
12. Chuang J.L., Cox R.P., Chuang D.T. Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences. Am. J. Hum. Genet. 1996, 58:1373-1377.
13. Schadewaldt P., Wendel U. Comparison of the catabolism of branched-chain l-amino acids in cultured human skin fibroblasts. Pediatr. Res. 1987, 22:591-594.
14. Jellum E., Kvittingen E.A., Thoresen O., Guldal G., Horn L., Seip R., Stokke O. Systematic laboratory diagnosis of human metabolic disorders. Scand. J. Clin. Lab. Invest. Suppl. 1986, 184:11-20.
15. Chuang D.T., Shih V.E. Maple Syrup Urine Disease (Branched-Chain Ketoaciduria). The Metabolic and Molecular Bases of Inherited Disease 2001, Mc Graw Hill, pp. 1971-1989.
16. D.T. Chuang, R.M. Wynn, V. Shih, Maple syrup urine disease (branched-chain ketoaciduria). Valle, Beaudet, Vogelstein, Kinzler, Antonarakis, Ballabio, The Online Metabolic and Molecular Bases of Inherited Diseases, vol. 87, McGraw Hill 2008. Available from: http://www.ommbid.com.
17. Bota D.A., Davies K.J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 2002, 4:674-680.
18. Tatsuta T. Protein quality control in mitochondria. J. Biochem. 2009, 146:455-461.
19. Honda K., Ono K., Mori T., Kochi H. Both induction and activation of the branched-chain 2-oxo acid dehydrogenase complex in primary-cultured rat hepatocytes by clofibrate. J. Biochem. 1991, 109:822-827.
20. Kuokkanen M., Enattah N.S., Oksanen A., Savilahti E., Orpana A., Jarvela I. Transcriptional regulation of the lactase-phlorizin hydrolase gene by polymorphisms associated with adult-type hypolactasia. Gut 2003, 52:647-652.
21. Ingram C.J., Mulcare C.A., Itan Y., Thomas M.G., Swallow D.M. Lactose digestion and the evolutionary genetics of lactase persistence. Hum. Genet. 2009, 124:579-591.
22. Sai L.S., Agrawal S. piRNABank: a web resource on classified and clustered Piwi-interacting RNAs. Nucleic Acids Res. 2008, 36:D173-D177.
23. Mersey B.D., Jin P., Danner D.J. Human microRNA (miR29b) expression controls the amount of branched chain alpha-ketoacid dehydrogenase complex in a cell. Hum. Mol. Genet. 2005, 14:3371-3377.
24. Quental S., edo-Ribeiro S., Matos R., Vilarinho L., Martins E., Teles E.L., Rodrigues E., Diogo L., Garcia P., Eusebio F., Gaspar A., Sequeira S., Furtado F., Lanca I., Amorim A., Prata M.J. Molecular and structural analyses of maple syrup urine disease and identification of a founder mutation in a Portuguese Gypsy community. Mol. Genet. Metab. 2008, 94:148-156.
25. Simon E., Flaschker N., Schadewaldt P., Langenbeck U., Wendel U. Variant maple syrup urine disease (MSUD) - the entire spectrum. J. Inherit. Metab. Dis. 2006, 29:716-724.
26. Kiil R., Rokkones T. Late manifesting variant of branched-chain ketoaciduria (maple syrup urine disease). Acta Paediatr. 1964, 53:356-364.
27. Danner D.J., Doering C.B. Human mutations affecting branched chain alpha-ketoacid dehydrogenase. Front. Biosci. 1998, 3:d517-d524.
28. Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C., Snyderman S.E., Diaz G.A. Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population. Am. J. Hum. Genet. 2001, 69:863-868.
29. Wynn R.M., Chuang J.L., Sansaricq C., Mandel H., Chuang D.T. Biochemical basis of type IB (E1beta) mutations in maple syrup urine disease. A prevalent allele in patients from the Druze kindred in Israel. J. Biol. Chem. 2001, 276:36550-36556.
30. Chi C.S., Tsai C.R., Chen L.H., Lee H.F., Mak B.S., Yang S.H., Wang T.Y., Shu S.G., Chen C.H. Maple syrup urine disease in the Austronesian aboriginal tribe Paiwan of Taiwan: a novel DBT (E2) gene 4.7kb founder deletion caused by a nonhomologous recombination between LINE-1 and Alu and the carrier-frequency determination. Eur. J. Hum. Genet. 2003, 11:931-936.