Variants of citrullinaemia.

Wick, H; Bachmann, C.; Baumgartner, René; Brechbühler, T.; Colombo, J. P.; Wiesmann, Ulrich; Mihatsch, Michael J.; Ohnacker, H.

doi:10.1136/adc.48.8.636

Cited by 41 publications

(17 citation statements)

References 15 publications

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“…The incidence is estimated to be 1:57,000 (Maestri et al 1995;Brusilow and Horwich 2001). Patients only mildly affected with citrullinemia and asymptomatic patients have also been described (Wick et al 1973;Whelan et al 1976). Recently, citrullinemia was discovered in patients with mild clinical symptoms, in some of their asymptomatic siblings, and in asymptomatic neonates detected by newborn screening with tandem mass spectrometry (Bakker et al 1998;J.…”

Section: Introductionmentioning

confidence: 87%

Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia

et al. 2002

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Deficiency of argininosuccinate synthetase (ASS) causes citrullinemia, an autosomal recessive inherited defect of the urea cycle. Most patients described so far have presented with the classical form of the disease. There are also patients with a mild form of citrullinemia in whom the exact molecular basis and clinical relevance are uncertain. Mutations in the human ASS gene have not yet been described in mildly affected or asymptomatic patients with citrullinemia. The genomic sequence of the human ASS gene is not precisely known making mutation analysis difficult. Here, the entire genomic DNA sequence and mutations in the ASS gene of patients with the classical and mild form of the disease are described. The mutations c.1168G-->A (G390R) and IVS13+5 G-->A and the novel mutation c.323G-->T (R108L) have been found to be associated with classical citrullinemia, whereas the novel mutations c.535T-->G (W179R), and c.1085G-->T (G362V) have been detected on alleles of the mildly affected patients. Thus, mutations found in the human ASS gene of asymptomatic children with biochemical abnormalities and in some cases enzymatically proven citrullinemia have allowed us to classify these cases as ASS-deficient patients. The elucidation of the structure of the human ASS gene has made possible the use of intronic primers for molecular analysis of patients with mild disease and the classical form, and provides another option for prenatal diagnostics in affected families with the severe type.

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Section: Introductionmentioning

confidence: 87%

Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia

et al. 2002

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“…Among the small number of cases of citrullinaemia so far described, the range of clinical severity is wide (Wick et al, 1973;Scott-Emuakpor, Higgins, and Kohrman, 1972). The 5 acutely ill newbom babies so far described with this disease have all died despite energetic treatment (Wick et al, 1973;Okken, Van der Blij, and Hommes, 1973).…”

Section: Severe Neonatal Citrullinaemiamentioning

confidence: 99%

“…The 5 acutely ill newbom babies so far described with this disease have all died despite energetic treatment (Wick et al, 1973;Okken, Van der Blij, and Hommes, 1973). The patient described here was investigated from birth because 2 sibs had died of undiagnosed illness on the third day of life.…”

Section: Severe Neonatal Citrullinaemiamentioning

confidence: 99%

Severe neonatal citrullinaemia.

Danks¹,

Tippett²,

Zentner³

1974

Archives of Disease in Childhood

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“…Plasma and urinary amino acids were screened by high-voltage electrophoresis and quantitated by ion-exchange column chromatography as described previously [31]. Blood ammonia was determined by a microliter modification of the technique of Seligson and Hirahara [26] in patient B.M.…”

Section: Methodsmentioning

confidence: 99%

Congenital Methylmalonic Acidemia: a Variant of the B ‘Non-Responsive’ Form with Evidence for Reduced Affinity of Methylmalonyl-CoA Mutase for its B(12)-Coenzyme

Er¹,

Bachmann²,

Wick³

1976

Enzyme

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Methylmalonate metabolism was investigated in fibroblasts and leukocytes of two unrelated patients with a B(12)-nonresponsive type of congenital methylmalonic acidemia. Intact fibroblasts from both patients showed a defective metabolism of methyl^-14 C-malonate to 14C0(2), whereas no such defect was found in their intact peripheral leukocytes. In disrupted fibroblasts, the conversion of methylmalonyl coenzyme A to succinyl coenzyme A was markedly reduced but was completely normalized by the addition of 5'-deoxyadenosylcobalamin (AdoCbl; 10^-5 mol/l), the specific coenzyme of methylmalonyl coenzyme A mutase. Assays with decreasing concentrations of AdoCbl (10^-5-10^-11 mol/l) suggested a reduced affinity of the mutase apoenzyme for its coenzyme, implicating yet another variant of this heterogeneous disease.

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Variants of citrullinaemia.

Cited by 41 publications

References 15 publications

Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia

Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia

Severe neonatal citrullinaemia.

Congenital Methylmalonic Acidemia: a Variant of the B ‘Non-Responsive’ Form with Evidence for Reduced Affinity of Methylmalonyl-CoA Mutase for its B(12)-Coenzyme

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