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Hemagglutination by Lectins in Friedreich's Ataxia

Published online by Cambridge University Press:  18 September 2015

M.S. Steinberg ,
J. Magnani ,
N. Czarkowski ,
M.B. Coccia  and
A. Barbeau
M.S. Steinberg
Affiliation:
Department of Biology, Princeton University, Princeton, New Jersey and the Department of Neurobiology, Clinical Research Institute of Montreal
J. Magnani
Affiliation:
Department of Biology, Princeton University, Princeton, New Jersey and the Department of Neurobiology, Clinical Research Institute of Montreal
N. Czarkowski
Affiliation:
Department of Biology, Princeton University, Princeton, New Jersey and the Department of Neurobiology, Clinical Research Institute of Montreal
M.B. Coccia
Affiliation:
Department of Biology, Princeton University, Princeton, New Jersey and the Department of Neurobiology, Clinical Research Institute of Montreal
A. Barbeau
Affiliation:
Department of Biology, Princeton University, Princeton, New Jersey and the Department of Neurobiology, Clinical Research Institute of Montreal
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Coded erythrocyte samples from ten individuals with Friedreich*š ataxia, from parents of five of these individuals, and from five unrelated control individuals were subjected to lecţin agglutination tests at three temperatures; before and after trypsinization; and before and after treatment with echinocyte-producing sodium salicylate and stornato^ cyte-pröducing tetracaine followed by shape-fixation with glutaraldehyde. The aġglutinins tested were the polycationic poly-L-lysirie (PLL) and four lectins with different saccharide specificities: soybean agglutinin, wheat germ agglutinin, Ufex europeus agglutinin (VEA) and concana-valin A. Altogether, over 45,000 individual test wells were scored, the status of each blood donor with respect to diagnosis being disclosed to the experimenters only after all results were tabulated.

The majority of these tests revealed no significant difference among the three groups of blood samples. A few tests did reveal statistically valid (p<0.0l) differences between groups, the most significant of which were the following: Trypsin ized control RBC were more sensitive, on average, to agglutination by VEA (fucose-inhibited) than were RBC of ataxies or their parents. Non-trypsinized control “stomatocytes” were less sensitive, on average, to agglutination by PLL than were those of ataxies or their parents. Trypsinization appeared, on average, to sensitive control but not ataxia or parent RBC to PLL-agglutination. Other differences of borderline (p-0.01-0.025) or near borderline (p = 0.025-0.05) significance were also noted. None of the statistically significant, Friedreich's ataxia-telated differences in median agglutination titers were large, the greatest being about threefold, and in every case the ranges of individual titers within the differing groups overlapped. Thus, none of these tests at present offers a method of pre clinic al diagnosis or carrier detection, and only further tests can establish whether even the differences observed in the present series of tests are reproducible.

Type
Research Article
Information
Canadian Journal of Neurological Sciences , Volume 6 , Issue 2 , May 1979 , pp. 299 - 309
Copyright
Copyright © Canadian Neurological Sciences Federation 1979

References

Birchmeier, W. and Singer, S. J. (1977). On the mechanism of ATP-induced shape changes in human erythrocyte membranes. II. The role of ATP. J. Cell Biol., 73, 647–659.CrossRefGoogle ScholarPubMed
Deuticke, B. (1968). Transformation and restoration of biconcave shape of human erythrocytes induced by amphi-philic agents and changes of ionic environment. Biochim. Biophys. Acta, 75, 494–500.CrossRefGoogle Scholar
Fisher, R. A. (1934). “Statistical Methods for Research Workers” (5th Ed.), sec. 21.02. Oliver and Boyd, Edinburgh.Google Scholar
Fowler, V. and Branton, D. (1977). Lateral mobility of human erythrocyte integral membrane proteins. Nature, 268, 23–26.CrossRefGoogle ScholarPubMed
Goldstein, J. L. and Brown, M. S. (1977). The low-density lipoprotein pathway and its relation to atherosclerosis. Ann. Rev. Biochem., 46, 897–930.CrossRefGoogle ScholarPubMed
Gordon, J. A. and Marquardt, M. D. (1974). Factors affecting hemagglutination by cocanavalin A and soybean agglutinin. Biochim. Biophys. Acta, 332, 136–144.CrossRefGoogle Scholar
Gordon, J. A. and Marquardt, M. D. (1975). Erythrocyte morphology and clustering of fluorescent anti-A immunoglo-bulin. Nature, 259, 346–347.CrossRefGoogle Scholar
Huang, Y. S., Nestruck, A. C., Barbeau, A., Bouchard, J. P. and Davignon, J. (1978). Plasma lipids and lipoproteins in Fried reich's ataxia and familial spastic ataxia — Evidence for an abnormal composition of high density lipoproteins. Can. J. Neurol. Sci., 5, 149–156.CrossRefGoogle Scholar
Hui, D. Y., and Harmony, J. A. K. (1978). Low density lipoprotein-induced alterations of the erythrocyte membrane. Abstr. 7th Ann. ICN-UCLA Symposium: Normal and abnormal red cell membranes. J. Supramol. Struct. Suppl. 2, 208.Google Scholar
Inbar, M., Huet, C., Oseroff, A. R., Ben-Bassat, H., and Sachs, L. (1973). Inhibition of lectin agglutinability by fixation of the cell surface membrane. Biochim. Biophys. Acta, 311, 594–599.CrossRefGoogle ScholarPubMed
Katchalsky, A., Dannon, D., Nevo, A., and Devries, A. (1959). Interactions of basic polyelectrolytes the red blood cell. II. Agglutination of red blood cells by polymeric bases. Biochim. Biophys. Acta, 33, 120–138.Google ScholarPubMed
Kury, P. G. and McConnell, H. M. (1975). Regulation of membrane flexibility in human erythrocytes. Biochemistry, 14, 2798–2803.CrossRefGoogle ScholarPubMed
Kury, P. G., Ramwell, P. W. and McConnell, H. M. (1974). The effect of prostaglandins E, and E2 on the human erythrocyte as monitored by spin labels. Biochem. Biophys. Res. Commun., 56, 478–483.CrossRefGoogle Scholar
Lis, H. and Sharon, N. (1973). The biochemistry of plant lectins (phytohemagglu-tinins.). Ann. Rev. Biochem., 42, 541–574.CrossRefGoogle Scholar
Marikovsky, Y., Brown, C. S., Weinstein, R. S. and Wortis, H. H. (1976). Effects of lysolecithin on the surface properties of human erythrocytes. Exptl. Cell Res., 98, 313–324.CrossRefGoogle ScholarPubMed
Meyers, M. B. and Swislocki, N. I. (1974). Conformational changes in erythrocyte membranes by prostaglandins as measured by circular dichroism. Arch. Biochem. Biophys., 164; 544–550.CrossRefGoogle ScholarPubMed
Nicolson, G. L. (1974). The interaction of lectins with animal cell surfaces. Int. Rev. Cytol., 39, 89–190.CrossRefGoogle ScholarPubMed
Noonan, K. D. and Burger, M. M. (1973). The relationship of concanavalin A binding to lectin-initiated cell agglutination. J. Cell Biol., 59, 134–142.CrossRefGoogle ScholarPubMed
Peters, R., Peters, J., Tews, K. H. and Bahr, W. (1974). A microfluorimetric study of translational diffusion in erythrocyte membranes. Biochim. Biophys. Acta, 367, 282–294.CrossRefGoogle ScholarPubMed
Schnebli, H. P. and Bachi, T. (1975). Reactions of lectins with human erythrocytes. I. Factors governing the agglutination reaction. Exptl. Cell Res., 91, 175–183.Google ScholarPubMed
Schnebli, H. P., Roeder, C., and Tarcsay, L. (1976). Reactions of lectins with human erythrocytes. III. Surface charge density and agglutination. Exptl. Cell Res., 98, 273–276.Google ScholarPubMed
Sheetz, M. P. and Singer, S. J. (1974). Biological membranes as bilayer couples. A molecular mechanism of drug erythrocyte interactions. Proc. Nat. Acad. Sci. (U.S.). 71, 4457–4461.Google ScholarPubMed
Shotton, D., Thompson, K., Wofsy, L. and Branton, D. (1978). Appearance and distribution of surface proteins of the human erythrocyte membrane. An electron microscope and immunochemical labelling study. J. Cell Biol., 76, 512–531.Google ScholarPubMed
Siegel, S. (1956). “Nonparametric Statistics for the Behavioral Sciences.” pp. 111–116. McGraw-Hill, N.Y.Google Scholar
Spielmann, W. and Seidl, S. (1973). Summary of clinical experiences in Germany with preservative-anticoagulant solutions with newer additives.In: “The Human Red Cell in Vitro”, Grune and Stratton, N.Y. and London (edited by Greenwalt, T. and Jamieson, G. A.), pp. 255–275.Google Scholar
Ukena, T. E. and Karnovsky, M. J. (1977). The role of microvilli in the agglutination of cells by concanavalin A. Exptl. Cell Res., 106, 309–325.CrossRefGoogle ScholarPubMed
Vlodavsky, J., Inbar, M. and Sachs, L. (1972). Temperature-sensitive agglutinability of human erythrocytes by lectins. Biochim. Biophys. Acta., 274, 364–369.CrossRefGoogle ScholarPubMed
Weltzien, H. U. (1975). Effects of lysolecithin and synthetic analogs on concanavalin A induced agglutination of chicken, human and bovine erythrocytes. Exptl. Cell Res., 92, 111–121.CrossRefGoogle ScholarPubMed
Willingham, M. C. and Pastan, L. (1975). Cyclic AMP modulates microvillus formation and agglutinability in transformed and normal mouse fibroblasts. Proc. Nat. Acad. Sci. (U.S.), 72, 1263–1267.CrossRefGoogle ScholarPubMed