Zusammenfassung
Die Glykoproteine in Erythrocytenmembranen von Individuen, die die seltenen Allele am MNSs BlutgruppenlokusMiltenberger (Mi-) III, V, M v undM k aufweisen, wurden mit Natrium-Dodecylsulfat Polyacrylamidgel elektrophoretischen Techniken untersucht. Die Ergebnisse erbringen Evidenz dafür, da\ die GeneMi-III und -V zur Synthese von Ss Sialoglykoproteinen mit verÄnderten elektrophoretischen MobilitÄten führen. Die Mi-V VerÄnderung ist zusÄtzlich durch einen verminderten MN Glykoproteingehalt charakterisiert. Das AllelM v führt zu einem verminderten Ss Glykoproteingehalt. Ergebnisse an gewöhnlichenM k undM k/Mi -III Zellen erbringen Evidenz dafür, da\ das AllelM k kein Ss Glykoprotein produziert.
Summary
The glycoproteins in erythrocyte membrane from individuals exhibiting the rare alleles at the MNSs blood group locusMiltenberger (Mi-) III, V, M v andM k were studied by sodium-dodecylsulfate polyacrylamide gel electrophoretic techniques. The results suggest that the genesMi- III and -V give rise to the formation of Ss sialoglycoproteins whose electrophoretic mobilities are altered. TheMi-V alteration is additionally associated with a decreased MN glycoprotein content. The alleleM v leads to a decreased Ss glycoprotein content. Data on ordinaryM k andM k/Mi-III red cells suggest that the gene complexM k does not give rise to the synthesis of Ss glycoprotein.
References
Cabantchik, Z.I., Balshin, M., Breuer, W., Markus, H., Rothstein, A.: A comparison of intact human red cells and resealed and leaky ghosts with respect to their interactions with surface labelling agents and proteolytic enzymes. Biochim. Biophys. Acta382, 621–633 (1975)
Crossland, J.D., Pepper, M.D., Giles, C.M., Ikin, E.W.: A British family possessing two variants of the MNSs blood group system, Mk and a new class within the Miltenberger complex. Vox Sang.18, 407–413 (1970)
Dahr, W., Uhlenbruck, G., Wagstaff, W., Leikola, J.: Studies on the membrane glycoprotein defect of En(a-) erythrocytes. II. MN antigenic properties of En(a-) erythrocytes. J. Immunogenet.3, 383–393 1976)
Dahr, W., Uhlenbruck, G., Janssen, E., Schmalisch, R.: Heterogeneity of human erythrocyte membrane sialoglycoproteins. Blut32, 171–184 (1976)
Dahr, W., Uhlenbruck, G., Schmalisch, R., Janssen, E.: Ss blood group associated PASstaining polymorphism of glycoprotein 3 from human erythrocyte membranes. Hum. Genet.32, 121–132 (1976)
Dahr, W., Uhlenbruck, G., Janssen, E., Schmalisch, R.: Different N-terminal amino acids in the MN glycoprotein fromMM andNN erythrocytes. Hum. Genet.35, 335–343 (1977)
Dahr, W., Uhlenbruck, G., Leikola, J., Wagstaff, W.: Studies on the membrane glycoprotein defect of En(a-) erythrocytes. III. N-terminal amino acids of sialoglycoproteins from normal and En(a-) red cells. J. Immunogenet.5, in press (1978)
Dahr, W., Issitt, P. D., Uhlenbruck, G.: New concepts of the MNSs blood group system. In: Human blood groups. Mohn J. F. (ed.). Basel S. Karger 1977
Dahr, W., Uhlenbruck, G., Knott, H.: The defect of Mk erythrocytes as revealed by sodiumdodecylsulfate polyacrylamide gel electrophoresis. J. Immunogenet.4, 191–200 (1977)
Furthmayr, H., Tomita, M., Marchesi, V.T.: Fractionation of the major sialoglycopeptides of the human red cell membrane. Biochem. biophys. Res. Commun.65, 113–121 (1975)
Fujita, S., Cleve, H.: Isolation and partial characterization of two minor glycoproteins from human erythrocyte membranes. Biochim. biophys. Acta382, 172–180 (1075)
Gahmberg, C.G., Hakomori, S.: External labelling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes. J. biol. Chem.248, 4311–4317 (1973)
Gahmberg, C.G., MyllylÄ, G., Leikola, J., Pirkola, A., Nordling, S.: Absence of the major sialoglycoprotein in the membrane of human En(a-) erythrocytes and increased glycosylation of band 3. J. biol. Chem.251, 6108–6116 (1976)
Hamaguchi, H., Cleve, H.: Solubilization of erythrocyte membrane glycoproteins and separation of the MN glycoprotein from a glycoprotein with I, S and A activity. Biochem. biophys. Acta278, 271–280 (1972)
Laemmli, U.K.: Cleavage of structual proteins during the assembly of the head of bacteriophage T4. Nature Lond.227, 680–685 (1970)
Lunner, S.J., Sturgeon, P., Szkarek, D., McQuiston, T.: Cell electrophoretic, membrane sialic acid and quantitative hemagglutination studies on some MN variants. Vox Sang.29, 440–449 (1975)
Mueller, T.J., Dow, A.W., Morrison, M.: Heterogeneity of the sialoglycoproteins of the normal human erythrocyte membrane. Biochem. biophys. Res. Commun.72, 94–99 (1976)
Metaxas, M.N., Metaxas-Bühler, M., Heiken, A., Vamosi, M., Ikin, E.W., Bull, W.: Further examples of Miltenberger cell class V, one of them inherited with a depressed M antigen. Vox Sang.23, 420–428 (1972)
Steck, T., Dawson, G.: Topographical distribution of complex carbohydrates in the erythrocyte membrane. J. biol. Chem.249, 2135–2142 (1974)
Sturgeon, P., Metaxas-Bühler, M., Metaxas, M.N., Tippett, P., Ikin, E.W.: An erroneous exclusion of paternity in a Chinese family exhibiting the rare MNSs gene complexes Mk and MsIII. Vox Sang.18, 395–406 (1970)
Tanner, M.T.A., Anstee, D.J.: The membrane change in En(a-) human erythrocytes. Absence of the major erythrocyte sialoglycoprotein. Biochem. J.153, 217–277 (1976)
Wasniowska, K., Drzeniek, Z., Lisowska, E.: The amino acids of M and N blood group glycopeptides are different. Biochem. biophys. Res. Commun.76, 385–390 (1977)
Weber, K., Osborn, M.: The reliability of Molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. biol. Chem.244, 4406–4412 (1969)
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Dedicated to Professor Dr. R. Gross on the occasion of his 60th birthday. Part of the work described in the present paper was presented at the 7th International Congress of the Society for Forensic Haematogenetics, Hamburg, September 25-29, 1977
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Dahr, W., Longster, G., Uhlenbruck, G. et al. Studies on Miltenberger class III, V, Mv and Mk red cells. Blut 37, 129–138 (1978). https://doi.org/10.1007/BF00996762
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DOI: https://doi.org/10.1007/BF00996762