Assignment of Human Glutaryl-CoA Dehydrogenase Gene (GCDH) to the Short Arm of Chromosome 19 (19p13.2) by in Situ Hybridization and Somatic Cell Hybrid Analysis

Greenberg, Cheryl R.; Duncan, Alessandra M.V.; Gregory, Carolyn; Singal, Rupinder; Goodman, Stephen I.

doi:10.1006/geno.1994.1264

Cited by 39 publications

(17 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Multiple neurologic abnormalities, including choreoathetosis, quadriplegia, and dystonic posturing, persist on recovery from the acute phase . The human GCDH gene (GCDH) consists of 11 exons spanning about 7 kb and maps to chromosome 19p11.2 [Biery et al, 1996;Greenberg et al, 1994]. At least 18 different mutations in GCDH have been identified in GA-I patients [Anikster et al, 1996;Biery et al, 1996;Greenberg et al, 1995].…”

Section: Introductionmentioning

confidence: 99%

Novel mutations of the glutaryl-CoA dehydrogenase gene in two Japanese patients with glutaric aciduria type I

et al. 1998

View full text Add to dashboard Cite

We identified three different point mutations in the glutaryl-CoA dehydrogenase (GCDH) gene in two unrelated Japanese patients with glutaric aciduria type I (GA-I). One patient was a homozygote for Arg355His and the other a compound heterozygote for Ser305Leu and Met339Val. Arg355His and Met339Val are mutations hitherto undescribed, and all three mutations are predicted to alter the secondary structure of GCDH. Molecular analysis is useful for definite diagnosis and/or prenatal diagnosis of GA-I.

show abstract

Section: Introductionmentioning

confidence: 99%

Novel mutations of the glutaryl-CoA dehydrogenase gene in two Japanese patients with glutaric aciduria type I

et al. 1998

View full text Add to dashboard Cite

show abstract

“…The responsible GCDH gene (OMIM*608801) is localised on chromosome 19 (19p13.2) (2), spans approximately 7 kb and contains 12 exons, but the fi rst exon is noncoding. GCDH gene encodes a fl avin adenine dinucleotide (FAD)-dependent mitochondrial matrix fl avoprotein, which catalyses dehydrogenation and decarboxylation of glutaryl-CoA to crotonyl-CoA in the common degradative pathway of L-lysine, L-hydroxylysine and Ltryptophan (3,4).…”

Section: Introductionmentioning

confidence: 99%

GAI – distinct genotype and phenotype characteristics in reported Slovak patients

Lisyová¹,

Petrovič²,

Juříčková³

et al. 2017

BLL

View full text Add to dashboard Cite

OBJECTIVES: The clinical, biochemical and genetic fi ndings in two Slovak patients with glutaric aciduria type I (GAI) are presented. BACKGROUND: GAI is a rare autosomal recessive neuro-metabolic disorder caused by defi ciency of glutarylCoA dehydrogenase, which is involved in the catabolic pathways of lysine, hydroxylysine and tryptophan. This enzymatic defect gives rise to elevated levels of glutaric acid (GA), 3-hydroxyglutaric acid (3-OH-GA) and glutarylcarnitine (C5DC) in body fl uids. METHODS: Biochemical and molecular-genetic tests were performed. Urinary organic acids were analysed by Gas Chromatography/Mass Spectrometry (GC/MS) and the entire coding region of the GCDH gene, including fl anking parts, was sequenced. RESULTS: We found the presence of typical metabolic profi le and novel causal pathogenic variants in both GAI patients. CONCLUSION: We present the fi rst report of two Slovak patients with GAI, which differed in the clinical and biochemical phenotype signifi cantly. They were diagnosed by two distinct approaches -selective and newborn screening. Their diagnosis was complexly confi rmed by biochemical and later on molecular-genetic examinations. Though we agreed with a thesis that early diagnostics might positively infl uenced patientʼs health outcome, contradictory facts should be considered. Supposed extremely low prevalence of GAI patients in the general population and/or the existence of asymptomatic individuals with a questionable benefi t of the applied therapeutic intervention for them lead to doubts whether the inclusion of disease into the newborn screening programme is justifi ed well enough (Tab. 1, Fig. 3

show abstract

“…This disorder is characterized by the accumulation of glutaric and 3-hydroxyglutaric acids as well as glutarylcarnitine in body¯uids. The human GCDH gene has been mapped to chromosome 19p 13.2 (Greenberg et al, 1994), spans about 7 Kb and comprises 11 exons and 10 introns. The genomic structure and most of the intronic sequences have been published Biery et al, 1996;Schwartz et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Prenatal molecular diagnosis of glutaric aciduria type I by direct mutation analysis

Busquets¹,

Coll²,

Merinero

et al. 2000

Prenat. Diagn.

View full text Add to dashboard Cite

Various biochemical strategies are followed for the prenatal diagnosis of glutaric aciduria type I (GA I). However, since the description of patients with normal excretion of glutarate and significant residual activity, the difficulties of prenatal biochemical diagnosis are obvious. The characterization of the glutaryl‐CoA dehydrogenase (GCDH) gene has allowed us to develop a single strand conformation polymorphism (SSCP) screening method, followed by direct sequencing, to identify the disease causing mutations in patients with GA I. Here we report the first prenatal diagnoses based on DNA analysis in chorionic villi biopsy or cultured amniotic fluid cells in three families at risk for GA I. Our results show that this strategy provides a fast and reliable method for prenatal diagnosis. In addition we report two new mutations (1209–1210ins G and R161W) in the GCDH gene that occurred at hypermutable loci. Copyright © 2000 John Wiley & Sons, Ltd.

show abstract

Assignment of Human Glutaryl-CoA Dehydrogenase Gene (GCDH) to the Short Arm of Chromosome 19 (19p13.2) by in Situ Hybridization and Somatic Cell Hybrid Analysis

Cited by 39 publications

References 0 publications

Novel mutations of the glutaryl-CoA dehydrogenase gene in two Japanese patients with glutaric aciduria type I

Novel mutations of the glutaryl-CoA dehydrogenase gene in two Japanese patients with glutaric aciduria type I

GAI – distinct genotype and phenotype characteristics in reported Slovak patients

Prenatal molecular diagnosis of glutaric aciduria type I by direct mutation analysis

Contact Info

Product

Resources

About