Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene

Research output: Contribution to journalJournal articlepeer-review

Standard

Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. / Andresen, B S; Bross, P; Vianey-Saban, C; Divry, P; Zabot, M T; Roe, C R; Nada, M A; Byskov, A; Kruse, T A; Neve, S; Kristiansen, K; Knudsen, I; Corydon, M J; Gregersen, N.

In: Human Molecular Genetics, Vol. 5, No. 4, 1996, p. 461-72.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Andresen, BS, Bross, P, Vianey-Saban, C, Divry, P, Zabot, MT, Roe, CR, Nada, MA, Byskov, A, Kruse, TA, Neve, S, Kristiansen, K, Knudsen, I, Corydon, MJ & Gregersen, N 1996, 'Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene', Human Molecular Genetics, vol. 5, no. 4, pp. 461-72. <http://www.ncbi.nlm.nih.gov/pubmed/8845838>

APA

Andresen, B. S., Bross, P., Vianey-Saban, C., Divry, P., Zabot, M. T., Roe, C. R., Nada, M. A., Byskov, A., Kruse, T. A., Neve, S., Kristiansen, K., Knudsen, I., Corydon, M. J., & Gregersen, N. (1996). Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. Human Molecular Genetics, 5(4), 461-72. http://www.ncbi.nlm.nih.gov/pubmed/8845838

Vancouver

Andresen BS, Bross P, Vianey-Saban C, Divry P, Zabot MT, Roe CR et al. Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. Human Molecular Genetics. 1996;5(4):461-72.

Author

Andresen, B S ; Bross, P ; Vianey-Saban, C ; Divry, P ; Zabot, M T ; Roe, C R ; Nada, M A ; Byskov, A ; Kruse, T A ; Neve, S ; Kristiansen, K ; Knudsen, I ; Corydon, M J ; Gregersen, N. / Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. In: Human Molecular Genetics. 1996 ; Vol. 5, No. 4. pp. 461-72.

Bibtex

@article{86f64a600fa211de8478000ea68e967b,
title = "Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene",
abstract = "Very-long-chain acyl-CoA dehydrogenase (VLCAD) is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are all nuclear encoded mitochondrial flavoproteins catalyzing the initial step in fatty acid beta-oxidation. We have used the very fast, Rapid Amplification of cDNA Ends (RACE) based strategy to obtain the sequence of cDNAs encoding human VLCAD from placenta and fibroblasts. Alignment of the predicted amino acid sequence of human VLCAD with those of the other human ACD enzymes revealed extensive sequence homology. Moreover, human VLCAD and human acyl-CoA oxidase showed extensive sequence homology corroborating the notion that these genes are evolutionarily related. Southern blot analysis of genomic DNA from hybrid cell lines was used to localize the VLCAD gene to human chromosome 17p11.2-p11.13105. Using Northern and Western blot analysis to investigate the tissue specific distribution of VLCAD mRNA and protein in several human tissues we showed that VLCAD is most abundant in heart and skeletal muscle. This agrees well with the fact that cardiac and muscle symptoms are characteristic for patients with VLCAD deficiency. Northern blot analysis and sequencing of cloned PCR amplified VLCAD cDNA from four unrelated patients with VLCAD deficiency showed that VLCAD mRNA was undetectable in one patient and that the other three have mutations in both VLCAD alleles. Western blot analysis of patient fibroblasts showed that the identified mutations result in severely reduced amounts of VLCAD protein. None of the patients harbored identical mutations suggesting that the mutational heterogeneity in VLCAD deficiency is large.",
author = "Andresen, {B S} and P Bross and C Vianey-Saban and P Divry and Zabot, {M T} and Roe, {C R} and Nada, {M A} and A Byskov and Kruse, {T A} and S Neve and K Kristiansen and I Knudsen and Corydon, {M J} and N Gregersen",
note = "Keywords: Acyl-CoA Dehydrogenase, Long-Chain; Acyl-CoA Dehydrogenases; Amino Acid Sequence; Base Sequence; Blotting, Western; Child, Preschool; Chromosome Mapping; Chromosomes, Human, Pair 17; Cloning, Molecular; DNA Primers; DNA, Complementary; Female; Humans; Infant; Infant, Newborn; Male; Molecular Sequence Data; Mutation; Sequence Homology, Amino Acid; Tissue Distribution",
year = "1996",
language = "English",
volume = "5",
pages = "461--72",
journal = "Human Molecular Genetics",
issn = "0964-6906",
publisher = "Oxford University Press",
number = "4",

}

RIS

TY - JOUR

T1 - Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene

AU - Andresen, B S

AU - Bross, P

AU - Vianey-Saban, C

AU - Divry, P

AU - Zabot, M T

AU - Roe, C R

AU - Nada, M A

AU - Byskov, A

AU - Kruse, T A

AU - Neve, S

AU - Kristiansen, K

AU - Knudsen, I

AU - Corydon, M J

AU - Gregersen, N

N1 - Keywords: Acyl-CoA Dehydrogenase, Long-Chain; Acyl-CoA Dehydrogenases; Amino Acid Sequence; Base Sequence; Blotting, Western; Child, Preschool; Chromosome Mapping; Chromosomes, Human, Pair 17; Cloning, Molecular; DNA Primers; DNA, Complementary; Female; Humans; Infant; Infant, Newborn; Male; Molecular Sequence Data; Mutation; Sequence Homology, Amino Acid; Tissue Distribution

PY - 1996

Y1 - 1996

N2 - Very-long-chain acyl-CoA dehydrogenase (VLCAD) is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are all nuclear encoded mitochondrial flavoproteins catalyzing the initial step in fatty acid beta-oxidation. We have used the very fast, Rapid Amplification of cDNA Ends (RACE) based strategy to obtain the sequence of cDNAs encoding human VLCAD from placenta and fibroblasts. Alignment of the predicted amino acid sequence of human VLCAD with those of the other human ACD enzymes revealed extensive sequence homology. Moreover, human VLCAD and human acyl-CoA oxidase showed extensive sequence homology corroborating the notion that these genes are evolutionarily related. Southern blot analysis of genomic DNA from hybrid cell lines was used to localize the VLCAD gene to human chromosome 17p11.2-p11.13105. Using Northern and Western blot analysis to investigate the tissue specific distribution of VLCAD mRNA and protein in several human tissues we showed that VLCAD is most abundant in heart and skeletal muscle. This agrees well with the fact that cardiac and muscle symptoms are characteristic for patients with VLCAD deficiency. Northern blot analysis and sequencing of cloned PCR amplified VLCAD cDNA from four unrelated patients with VLCAD deficiency showed that VLCAD mRNA was undetectable in one patient and that the other three have mutations in both VLCAD alleles. Western blot analysis of patient fibroblasts showed that the identified mutations result in severely reduced amounts of VLCAD protein. None of the patients harbored identical mutations suggesting that the mutational heterogeneity in VLCAD deficiency is large.

AB - Very-long-chain acyl-CoA dehydrogenase (VLCAD) is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are all nuclear encoded mitochondrial flavoproteins catalyzing the initial step in fatty acid beta-oxidation. We have used the very fast, Rapid Amplification of cDNA Ends (RACE) based strategy to obtain the sequence of cDNAs encoding human VLCAD from placenta and fibroblasts. Alignment of the predicted amino acid sequence of human VLCAD with those of the other human ACD enzymes revealed extensive sequence homology. Moreover, human VLCAD and human acyl-CoA oxidase showed extensive sequence homology corroborating the notion that these genes are evolutionarily related. Southern blot analysis of genomic DNA from hybrid cell lines was used to localize the VLCAD gene to human chromosome 17p11.2-p11.13105. Using Northern and Western blot analysis to investigate the tissue specific distribution of VLCAD mRNA and protein in several human tissues we showed that VLCAD is most abundant in heart and skeletal muscle. This agrees well with the fact that cardiac and muscle symptoms are characteristic for patients with VLCAD deficiency. Northern blot analysis and sequencing of cloned PCR amplified VLCAD cDNA from four unrelated patients with VLCAD deficiency showed that VLCAD mRNA was undetectable in one patient and that the other three have mutations in both VLCAD alleles. Western blot analysis of patient fibroblasts showed that the identified mutations result in severely reduced amounts of VLCAD protein. None of the patients harbored identical mutations suggesting that the mutational heterogeneity in VLCAD deficiency is large.

M3 - Journal article

C2 - 8845838

VL - 5

SP - 461

EP - 472

JO - Human Molecular Genetics

JF - Human Molecular Genetics

SN - 0964-6906

IS - 4

ER -

ID: 11253676