Heterozygosity for an in-frame deletion causes glutaryl-CoA dehydrogenase deficiency in a patient detected by newborn screening: Investigation of the effect of the mutant allele

Journal of Inherited Metabolic Disease

Volumn 35, Issue 5, 2012, Pages 787-796

  Bross, Peter ^a   Frederiksen, Jane B ^a   Bie, Anne S ^a   Hansen, Jakob ^a   Palmfeldt, Johan ^a   Nielsen, Marit N ^a   Duno, Morten ^b   Lund, Allan M ^b   Christensen, Ernst ^b  

^a AARHUS UNIVERSITY HOSPITAL   (Denmark)

^b Rigshospitalet   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTARYL COENZYME A DEHYDROGENASE; GLYCINE; MUTANT PROTEIN; SERINE; TETRAMER;

ALLELE; AMINO ACID SUBSTITUTION; ARTICLE; BLOOD ANALYSIS; CASE REPORT; CHEMICAL ANALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DEFICIENCY; ESCHERICHIA COLI; GENE DELETION; GENE EXPRESSION SYSTEM; GLUTARIC ACIDURIA TYPE 1; GLUTARYL COENZYME A DEHYDROGENASE DEFICIENCY; HETEROZYGOSITY; HUMAN; MALE; MUTANT; NEWBORN; NEWBORN SCREENING; NONHUMAN; PHENOTYPE; PROKARYOTE; PROMOTER REGION; PROTEIN ASSEMBLY; URINALYSIS; WILD TYPE;

ALLELES; AMINO ACID METABOLISM, INBORN ERRORS; BRAIN DISEASES, METABOLIC; CHILD, PRESCHOOL; GLUTARYL-COA DEHYDROGENASE; HETEROZYGOTE; HUMANS; INFANT, NEWBORN; MALE; NEONATAL SCREENING; SEQUENCE DELETION;

EID: 84866729240     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-011-9437-y     Document Type: Article

References (20)

1. Bross P, Andresen BS, Winter V, Kräutle F, Jensen TG, Nandy A, Kølvraa S, Ghisla S, Bolund L, Gregersen N (1993) Cooverexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E.coliexpressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochim Biophys Acta 1182:264-274
2. Bross P, Jespersen C, Jensen TG, Andresen BS, Kristensen MJ, Winter V, Nandy A, Kräutle F, Ghisla S, Bolund L, Kim JJP, Gregersen N (1995) Effects of two mutations detected in medium chain acyl-CoA dehydrogenase (MCAD)-deficient patients on folding, oligomer assembly, and stability of MCAD enzyme. J Biol Chem 270:10284-10290
3. Bross P, Corydon TJ, Andresen BS, Jørgensen MM, Bolund L, Gregersen N (1999) Protein misfolding and degradation in genetic diseases. Hum Mutat 14:186-198
4. Bross P, Naundrup S, Hansen J, Nielsen MN, Christensen JH, Kruhoffer M, Palmfeldt J, Corydon TJ, Gregersen N, Ang D, Georgopoulos C, Nielsen KL (2008) The HSP60-(P.val98ile) mutation associated with hereditary spastic paraplegia SPG13 compromises chaperonin function both in vitro and in vivo. J Biol Chem 283:15694-15700
5. Castanie MP, Berges H, Oreglia J, Prere MF, Fayet O (1997) A set of pBR322-compatible plasmids allowing the testing of chaperoneassisted folding of proteins overexpressed in Escherichia coli. Anal Biochem 254:150-152
6. Christensen E (1983) Improved assay of glutaryl-CoA dehydrogenase in cultured cells and liver: application to glutaric aciduria type I. Clin Chim Acta 129:91-97
7. Christensen E, Ribes A, Merinero B, Zschocke J (2004) Correlation of genotype and phenotype in glutaryl-CoA dehydrogenase deficiency. J Inherit Metab Dis 27:861-868
8. Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ (2004) Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochem 43:9674-9684
9. Goodman SI, Frerman FE (2001) Organic acidemias due to defects in lysine oxidation: 2-Ketoadipic acidemia and glutaric acidemia. In: Scriver CR, Beaudet al., Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B (eds) The metabolic & molecular basis of inherited disease, 8th edn. McGraw-Hill, New York, pp 2357-2365
10. Gordon N (2006) Glutaric aciduria types I and II. Brain Dev 28:136-140
11. Kölker S, Christensen E, Leonard JV, Greenberg CR, Boneh A, Burlina AB, Burlina AP, Dixon M, Duran M, Garcia CA, Goodman SI, Koeller DM, Kyllerman M, Muhlhausen C, Muller E, Okun JG, Wilcken B, Hoffmann GF, Burgard P (2011) Diagnosis and management of glutaric aciduria type I-revised recommendations. J Inherit Metab Dis 34:677-694
12. *. Orphanet J Rare Dis 6:44
13. Lossin C, George AL (2008) Myotonia congenita. Adv Genet 63:25-55
14. Miller JH (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
15. Saijo T, Welch WJ, Tanaka K (1994) Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD) - Demonstration of impaired transfer of K304E-variant MCAD from its complex with Hsp60 to the native tetramer. J Biol Chem 269:4401-4408
16. Saijo T, Tanaka K (1995) Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium chain Acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria. J Biol Chem 270:1899-1907
17. Strauss KA, Puffenberger EG, Robinson DL, Morton DH (2003) Type I glutaric aciduria, part 1: natural history of 77 patients. Am J Med Genet C Semin Med Genet 121C:38-52
18. Swigonova Z, Mohsen AW, Vockley J (2009) Acyl-CoA dehydro-genases: Dynamic history of protein family evolution. J Mol Evol 69:176-193
19. Yokota I, Saijo T, Vockley J, Tanaka K (1992) Impaired tetramer assembly of variant medium-chain acyl-coenzyme A dehydrogenase with a glutamate or aspartate substitution for lysine 304 causing instability of the protein. J Biol Chem 267:26004-26010
20. Zschocke J (2008) Dominant versus recessive: molecular mechanisms in metabolic disease. J Inherit Metab Dis 31:599-618