Hostname: page-component-745bb68f8f-5r2nc Total loading time: 0 Render date: 2025-01-26T06:17:48.327Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein Kinase Activity of Human Erythrocyte Membranes in Friedreich's Ataxia

Published online by Cambridge University Press:  18 September 2015

P. Wong  and
A. Barbeau
P. Wong
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
A. Barbeau*
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
*
Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal, 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.

Proteins of human erythrocyte membranes of Friedrich's ataxia patients and controls were examined by SDS-polyacrylamide gel electrophoresis before and after reduction withβ-mercaptoethanol. No difference could be detected in the composition of their state of aggregation. The protein kinase activity of human erythrocyte membranes of eleven Friedreich's ataxia patients and six controls was determined. No difference in their protein kinase activity could be detected. These results are discussed with respect to an involvement of a generalized membrane defect in Friedreich's ataxia.

Type
Quebec Cooperative Study of Friedreich's Ataxia
Information
Canadian Journal of Neurological Sciences , Volume 7 , Issue 4 , November 1980 , pp. 425 - 427
Copyright
Copyright © Canadian Neurological Sciences Federation 1980

References

REFERENCES

Bureau, M.A., Berthiaume, Y., Begin, R., Shapcott, D., Lemieux, B. and Côté, M. (1978). Oxygen transport in patients with Friedreich’s Ataxia. Can. J. Neur. Sci., 5: 97–99.CrossRefGoogle ScholarPubMed
Butterfield, D.A., Leung, P.K., Markenberg, W.R. and Barbeau, A. (1979). Evidence for an altered physical state of membrane proteins in erythrocytes in Friedreich’s Ataxia. Can. J. Neurol. Sci., 6: 295–298.CrossRefGoogle ScholarPubMed
Draper, P., Huang, Y.S., Shapcott, D., Lemieux, B., Breman, M., Barbeau, A. and Davignon, J. (1979). Erythrocyte membrane lipids in Friedreich’s Ataxia. Can. J. Neurol. Sci., 6: 291–294.CrossRefGoogle ScholarPubMed
Dzandu, J.K. and Johnson, R.M. (1980). Membrane protein phosphorylation in intact normal and sickle cells erythrocytes. J. Biol. Chem., 255: 6382–6382.CrossRefGoogle Scholar
Fairbanks, G., Steck, T.L., Wallach, and , D.F.H. (1971). Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry, 10, 2606–2617.CrossRefGoogle ScholarPubMed
Hanahan, D.J., Ekholm, J. and Hildenbrandt, G. (1973). Biochemical variability of human erythrocyte membranes preparations, as demonstrated by sodium-potassium-magnesium and calcium adenosine triphosphatase activities. Biochemistry, 12: 1374–1387.CrossRefGoogle ScholarPubMed
Hosey, M.M. and Tao, M. (1976). Altered erythrocyte membrane phosphorylation in sickle cell disease. Nature, 263: 424–425.CrossRefGoogle ScholarPubMed
Lowry, O.H., Rosenbough, N.J., Farr, A.L. and Randall, R.J. (1951). Protein measurements with the Folin phenol reagent. J. Biol. Chem., 193: 265–275.CrossRefGoogle ScholarPubMed
Roses, A.D. and Appel, S.H. (1973). Protein kinase activity in erythrocyte ghosts of patients with myotonic muscular dystrophy. Proc. Nat. Acad. Sci. U.S.A., 70: 1855–1859.CrossRefGoogle ScholarPubMed
Roses, A.D., Herbstreith, M.A. and Appel, S.H. (1975). Membrane protein kinase alteration in Duchenne muscular dystrophy. Nature, 254: 350–351.CrossRefGoogle ScholarPubMed
Roses, A.D. and Appel, S.H. (1975). Phosphorylation of component a of the human erythrocyte membrane in myotonic muscular dystrophy. J. Membrane Biol., 20: 51–58.CrossRefGoogle ScholarPubMed
Weber, K. and Osborn, M. (1969). The reliability of molecular weight determinations by dodecyl sulfate polyacrylamide gel electrophoresis. J. Biol. Chem., 224: 4406–4412.CrossRefGoogle Scholar
Wong, P. and Roses, A.D. (1979). Isolation of an abnormally phosphorylated erythrocyte membrane Band 3 glycoprotein from patients with myotonic muscular dystrophy. J. Membrane Biol., 45: 147–166.CrossRefGoogle ScholarPubMed