Hostname: page-component-54dcc4c588-5q6g5 Total loading time: 0 Render date: 2025-10-13T14:34:48.476Z Has data issue: false hasContentIssue false
  • English
  • Français

Leukocyte Valine Dehydrogenase Activity in Friedreich’s Ataxia

Published online by Cambridge University Press:  18 September 2015

A. Barbeau ,
T. Cloutier  and
M. Charbonneau
A. Barbeau*
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
T. Cloutier
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
M. Charbonneau
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
*
Clinical Research Institute of Montreal, 110 Pine Avenue West, Montréal, Quebec, Canada, H2W 1R7
Rights & Permissions [Opens in a new window]

Summary:

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

We studied the activity of valine dehydrogenase (VDH) in leukocytes of 14 Friedreich’s ataxia patients and of 14 normal control subjects. There was a significant 26% mean decrease in enzyme activity in the patients, a finding which could be responsible for the chronic accumulation of some α-keto acids with toxic metabolic consequences in that disease. However the deficiency was not present in all patients with the typical symptoms, nor was its magnitude sufficient to be considered the primary genetic defect in Friedreich’s A taxia.

Information

Type
Research Article
Information
Canadian Journal of Neurological Sciences , Volume 9 , Issue 2 , May 1982 , pp. 235 - 238
Copyright
Copyright © Canadian Neurological Sciences Federation 1982

References

REFERENCES

Barbeau, A. (1980). Friedreich’s Ataxia, 1980 – An overview of the physiopathology. Can. J. Neurol. Sci. 7: 455–468.CrossRefGoogle ScholarPubMed
Barbeau, A., Butterworth, R.F., Ngo, T., Breton, G., Melancon, S., Shapcott, D., Geoffroy, G. and Lemieux, B. (1976). Pyruvate metabolism in Friedreich’s Ataxia. Can. J. Neurol. Sci. 3:379–397.CrossRefGoogle ScholarPubMed
Blass, J.P., Kark, R.A.P. and Menon, N.K. (1976). Low activities of the pyruvate and oxoglutarate dehydrogenase complexes in five patients with Friedreich’s Ataxia. New Engl. J. Med. 295:62–67.CrossRefGoogle ScholarPubMed
Bowden, J.A. and Connelly, J.L. (1968). Branched chain α-keto acid metabolism. II. Evidence for the common identify of α -ketoisocaproic acid and α-keto-methyl-valeric acid dehydrogenases. J. Biol. Chem. 243: 3526–3531.CrossRefGoogle Scholar
Bowden, J.A., Mcarthur, C.L. and Fried, M. (1971). The inhibition of pyruvate decarboxylation in rat brain by -α ketoisocaproic acid. Biochem. Med. 5: 101–108.CrossRefGoogle Scholar
Buffington, C.K., De Buysere, M.S. and Olson, M.S. (1979). Studies on the regulation of the branched chain α -keto acid dehydrogenase in the perfused rat heart. J. Biol. Chem. 254: 10453–10458.CrossRefGoogle ScholarPubMed
Connelly, J.I., Danner, D.J. and Bowden, J.A. (1968). Branched chain α-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver α -keto isocaproic: α -ketomethyl-valeric acid dehydrogenase. J. Biol. Chem. 243: 1198–1203.CrossRefGoogle Scholar
Dancis, J., Hutzler, J. and Levitz, M. (1963). The diagnosis of Maple Syrup Urine disease (branched chain keto aciduria) by in in vitro study of the peripheral leucocyte. Pediatrics 32: 234–238.CrossRefGoogle Scholar
Dancis, J., Hutzler, J., Levitz, M. (1965). Detection of the heterozygote in Maple Syrup Urine Disease. J. of Pediat. 66: 595–603.CrossRefGoogle ScholarPubMed
Dancis, J., Hutzler, J., Synderman, S.E. and Cox, R.P. (1972). Enzyme activity in classical and variant forms of Maple Syrup Urine Disease. J. of Pediat. 81: 312–320.CrossRefGoogle ScholarPubMed
Dancis, J., Hutzler, J., Tada, K., Wada, Y., Morikawa, T. and Arakawa, T. (1967). Hypervalinemia – A defect in valine transamination. Pediatrics 39:813–817.CrossRefGoogle ScholarPubMed
Danner, D.J., Lemmon, S.K., Besharse, J.C. and Elsas, L.J. (1979). Purification and characterization of branched chain α -keto acid dehydrogenase from bovine liver mitochondria. J. Biol. Chem. 254: 5522–5526.CrossRefGoogle ScholarPubMed
Frick, G.P. and Goodman, H.M. (1980). Insulin regulation of branched-chain α -keto acid dehydrogenase in adipose tissue. J. Biol. Chem. 255:6186–6192.CrossRefGoogle ScholarPubMed
Geoffroy, G., Barbeau, A., Breton, G., Lemieux, B., Aube, M., Leger, C. and Bouchard, J.P. (1976). Clinical description and Roentgenologic evaluation of patients with Friedreich’s Ataxia. Can. J. Neurol. Sci. 3: 279–286.CrossRefGoogle ScholarPubMed
Johnson, W.A. and Connelly, J.L. (1972). Cellular localization and characterization of bovine liver branched chain α-keto acid dehydrogenase. Biochem. 11: 1967–1970.CrossRefGoogle Scholar
Kark, R.A.P. and Rodriguez-Budelli, M.M. (1979). Clinical correlations of partial deficiency of lipoamide dehydrogenase. Neurology 29: 1006–1013.CrossRefGoogle ScholarPubMed
Kean, E.A. and Morrison, E.Y. STA. (1979). Isolation of a branched chain α-keto-acid decarboxylase from rat liver. Biochem. Biophys. Acta 567: 12–17.Google ScholarPubMed
Livingstone, I.R., Mastaglia, F.L., and Pennington, R.J.T. (1980). An investigation of pyruvate metabolism in patients with cerebellar and spino-cerebellar degeneration. J. Neurol. Sci. 48: 123–132.CrossRefGoogle Scholar
Melancon, S.B., Potier, M., Dallaire, L., Fontaine, G., Grenier, B., Lemieux, B., Geoffroy, G. and Barbeau, A. (1978). Lipoamide dehydrogenase in Friedreich’s Ataxia fibroblasts. Can. J. Neurol. Sci. 5: 115–118.CrossRefGoogle ScholarPubMed
Menkes, J.H., Hurst, P.L. and Craig, J.M. (1954). New syndrome: Progressive familial infantile cerebral dysfunction associated with an unusual urinary substance. Pediatrics 14: 462–468.CrossRefGoogle ScholarPubMed
Patrick, A.D. (1961). Maple Syrup Urine Disease. Archs. Dis. Childhood 36: 269–272.CrossRefGoogle ScholarPubMed
Pettit, F.H., Yeaman, S.J. and Reed, L.J. (1978). Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. U.S.A. 75: 4881–4885.CrossRefGoogle ScholarPubMed
Rüdiger, H.W., Langenbeck, U., Schulze-Schencking, M. and Goedde, H.W. (1972). Defective decarboxylase in branched chain ketoacid oxidase multienzyme complex in classic type of Maple Syrup Urine Disease. Humangenetik 14: 257–263.Google ScholarPubMed
Scriver, C.R., Mackenzie, S., Clow, C.L. and Delvin, E. (1971). Thiamineresponsive Maple Syrup Urine Disease. Lancet 1:310–312.CrossRefGoogle ScholarPubMed
Snyderman, S.E., Norton, P.M., Roitman, S. and Holt, L.E. (1964). Maple Syrup Urine Disease, with particular reference to dietotherapy. Pediatrics 34: 454–472.CrossRefGoogle ScholarPubMed
Sternowsky, H.J., Roboz, J., Hutterer, F. and Gaull, G. (1973). Determination of α-keto acids as silylated oxines in urine and serum by combined gas chromatography-mass spectrometry. Clin. Chim. Acta 47: 371–379.CrossRefGoogle Scholar
Sullivan, S.G., Potter, D.A., Krauss, M.R., Dancis, J. and Cox, R.P. (1979). Differential alterations in branched chain amino-acid decarboxylation in liver of hypophysectomized rats. Experientia 35: 1043–1044.CrossRefGoogle ScholarPubMed
Tashian, R.E. (1961). Inhibition of brain glutamic acid decarboxylase by phenylalanine, valine and leucine derivatives: a suggestion concerning the etiology of the neurological defect in Phenylketonuria and branched chain ketonuria. Metabolism 10: 393–402.Google ScholarPubMed
Westall, R.G., Dancis, J. and Miller, S. (1957). Maple Sugar Urine Disease. Am. J. Dis. Child 94: 571–575.Google Scholar