Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1979 Nov 1;183(2):193–203. doi: 10.1042/bj1830193

Abnormal blood-group-Ss-active sialoglycoproteins in the membrane of Miltenberger class III, IV and V human erythrocytes.

D J Anstee, W J Mawby, M J Tanner
PMCID: PMC1161547  PMID: 230820

Abstract

1. We have studied the inherited changes occurring in the sialoglycoproteins of membranes from erythrocytes of type Miltenberger Class III (Mi.III), Miltenberger Class IV (Mi.IV) and Miltenberger Class V (Mi.V) by using sodium dodecyl sulphate/polyacrylamide gel electrophoresis and lactoperoxidase radioiodination. 2. Mi.III erythrocytes lack the normal blood-group-Ss-active sialoglycoprotein but contain an unusual s-active sialoglycoprotein of higher apparent molecular weight. A similar abnormal S-active sialoglycoprotein appears to occur in Mi.IV erythrocytes. 3. The Mi.V condition is associated with the hemizygous absence of both the normal blood-group-MN-active sialoglycoprotein and the normal Ss-active sialoglycorprotein. However, a new sialoglycoprotein component is present in these cells that has properties characteristic of both the MN-active and Ss-active sialoglycoproteins. 4. Our results suggest that the new sialoglycorportein present in Mi.V erythrocytes is a hybrid of the normal MN sialoglycoprotein and an s-active sialoglycoprotein that has properties similar to the s-active sialoglycoprotein found in Mi.III erythrocytes. We suggest that the unusual Mi.V sialoglycoprotein is derived from chromosomal misalignment with unequal crossing-over between the genes for the MN- and Ss-active sialoglycoproteins in a manner similar to that which gives rise to haemoglobin Lepore. 5. Further studies of S-s-erythrocytes confirm that these cells lack normal Ss-active sialoglycoprotein, but contain an unusual component that shows some of the properties of the normal Ss-active sialoglycoprotein. 6. Analysis of erythrocytes of type Mk/Mi.III confirms that, in addition to the known hemizygous lack of the MN-active sialoglycoprotein, the Mk condition is also associated with a loss of the Ss-active sialoglycoprotein. 7. In order to facilitate discussion of the complex changes that occur in these variant erythrocytes, a new unified nomenclature is used for the erythrocyte sialoglycoproteins.

Full text

PDF
193

Images in this article

195Fig. 1.
on p.195
196Fig. 2.
on p.196
197Fig. 4.
on p.197
198Fig. 5.
on p.198
200Fig. 7.
on p.200
202Fig. 9.
on p.202

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AMINOFF D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem J. 1961 Nov;81:384–392. doi: 10.1042/bj0810384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aminoff D., Bell W. C., Fulton I., Ibgebrigtsen N. Effect of sialidase on the viability of erythrocytes in circulation. Am J Hematol. 1976;1(4):419–432. doi: 10.1002/ajh.2830010407. [DOI] [PubMed] [Google Scholar]
  3. Anstee D. J., Tanner M. J. Genetic variants involving the major membrane sialoglycoprotein of human erythrocytes. Studies on erythrocytes of type Mk, Miltenberger class V and Mg. Biochem J. 1978 Oct 1;175(1):149–157. doi: 10.1042/bj1750149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Anstee D. J., Tanner M. J. Separation of ABH, I, Ss antigenic activity from the MN-active sialoglycoprotein of the human erythrocyte membrane. Vox Sang. 1975;29(5):378–389. doi: 10.1111/j.1423-0410.1975.tb00522.x. [DOI] [PubMed] [Google Scholar]
  5. Boxer D. H., Jenkins R. E., Tanner M. J. The organization of the major protein of the human erythrocyte membrane. Biochem J. 1974 Mar;137(3):531–534. doi: 10.1042/bj1370531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chandanayingyong D., Pejrachandra S., Poole J. Three antibodies of the MNSs system and their association with the Miltenberger Complex of antigens. I. Anek serum. Vox Sang. 1977;32(5):272–273. doi: 10.1111/j.1423-0410.1977.tb00643.x. [DOI] [PubMed] [Google Scholar]
  7. Chandanayingyong D., Pejrachandra S. Separable anti-Hut which is specific for class II of the Miltenberger complex. Vox Sang. 1975;28(2):149–151. doi: 10.1111/j.1423-0410.1975.tb02752.x. [DOI] [PubMed] [Google Scholar]
  8. Cleghorn T. E. A memorandum on the Miltenberger blood groups. Vox Sang. 1966 Mar-Apr;11(2):219–222. doi: 10.1111/j.1423-0410.1966.tb04226.x. [DOI] [PubMed] [Google Scholar]
  9. Crossland J. D., Pepper M. D., Giles C. M., Ikin E. W. A British family possessing two variants of the MNSs blood group system, Mv and a new class within the Miltenberger complex. Vox Sang. 1970 May;18(5):407–413. doi: 10.1111/j.1423-0410.1970.tb01478.x. [DOI] [PubMed] [Google Scholar]
  10. Dahr W., Uhlenbruck G., Janssen E., Schmalisch R. Heterogeneity of human cell membrane sialoglycoproteins. Blut. 1976 Mar;32(3):171–184. doi: 10.1007/BF00995910. [DOI] [PubMed] [Google Scholar]
  11. Dahr W., Uhlenbruck G., Knott H. The defect of Mk erythrocytes as revealed by sodium dodecylsulphate--polyacrylamide gel electrophoresis. J Immunogenet. 1977 Jun;4(3):191–200. doi: 10.1111/j.1744-313x.1977.tb00901.x. [DOI] [PubMed] [Google Scholar]
  12. Dahr W., Uhlenbruck G., Leikola J., Wagstaff W., Landfried K. Studies on the membrane glycoprotein defect of En(a-) erythrocytes. I. Biochemical aspects. J Immunogenet. 1976 Oct;3(5):329–346. doi: 10.1111/j.1744-313x.1976.tb00592.x. [DOI] [PubMed] [Google Scholar]
  13. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  14. Furthmayr H., Marchesi V. T. Subunit structure of human erythrocyte glycophorin A. Biochemistry. 1976 Mar 9;15(5):1137–1144. doi: 10.1021/bi00650a028. [DOI] [PubMed] [Google Scholar]
  15. Furthmayr H. Structural comparison of glycophorins and immunochemical analysis of genetic variants. Nature. 1978 Feb 9;271(5645):519–524. doi: 10.1038/271519a0. [DOI] [PubMed] [Google Scholar]
  16. Furthmayr H., Tomita M., Marchesi V. T. Fractionation of the major sialoglycopeptides of the human red blood cell membrane. Biochem Biophys Res Commun. 1975 Jul 8;65(1):113–121. doi: 10.1016/s0006-291x(75)80068-4. [DOI] [PubMed] [Google Scholar]
  17. Gahmberg C. G., Myllyla 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. 1976 Oct 10;251(19):6108–6116. [PubMed] [Google Scholar]
  18. Giles C. M., Chandanayingong D., Webb A. J. Three antibodies of the MNSs system and their association with the Miltenberger complex of antigens. III. Anek, Raddon and Lane antisera in relation to each other and the Miltenberger complex. Vox Sang. 1977;32(5):277–279. doi: 10.1111/j.1423-0410.1977.tb00645.x. [DOI] [PubMed] [Google Scholar]
  19. Hamaguchi H., Cleve H. Solubilization of human erythrocyte membrane glycoproteins and separation of the MN glycoprotein from a glycoprotein with I, S, and A activity. Biochim Biophys Acta. 1972 Sep 29;278(2):271–280. doi: 10.1016/0005-2795(72)90232-2. [DOI] [PubMed] [Google Scholar]
  20. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  21. Luner S. J., Sturgeon P., Szklarek D., McQuiston D. T. Cell electrophoretic, membrane sialic acid and quantitative hemagglutination studies on some MN variants. Vox Sang. 1975;29(6):440–449. doi: 10.1111/j.1423-0410.1975.tb00590.x. [DOI] [PubMed] [Google Scholar]
  22. Marton L. S., Garvin L. E. Subunit structure of the major human erythrocytes glycoprotein: depolymerization by heating ghosts with sodium dodecyl sulfate. Biochem Biophys Res Commun. 1973 Jun 19;52(4):1457–1462. doi: 10.1016/0006-291x(73)90664-5. [DOI] [PubMed] [Google Scholar]
  23. 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 inerited with a depressed M antigen. Vox Sang. 1972;23(5):420–428. doi: 10.1111/j.1423-0410.1972.tb03829.x. [DOI] [PubMed] [Google Scholar]
  24. Mueller T. J., Dow A. W., Morrison M. Heterogeneity of the sialoglycoproteins of the normal human erythrocyte membrane. Biochem Biophys Res Commun. 1976 Sep 7;72(1):94–99. doi: 10.1016/0006-291x(76)90965-7. [DOI] [PubMed] [Google Scholar]
  25. Mueller T. J., Morrison M. The transmembrane proteins in the plasma membrane of normal human erythrocytes. J Biol Chem. 1974 Dec 10;249(23):7568–7573. [PubMed] [Google Scholar]
  26. Steck T. L. The organization of proteins in the human red blood cell membrane. A review. J Cell Biol. 1974 Jul;62(1):1–19. doi: 10.1083/jcb.62.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. 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 Ms3. Vox Sang. 1970 May;18(5):395–406. doi: 10.1111/j.1423-0410.1970.tb01477.x. [DOI] [PubMed] [Google Scholar]
  28. Tanner M. J., Anstee D. J. A method for the direct demonstration of the lectin-binding components of the human erythrocyte membrane. Biochem J. 1976 Feb 1;153(2):265–270. doi: 10.1042/bj1530265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Tanner M. J., Anstee D. J., Judson P. A. A carbohydrate-deficient membrane glycoprotein in human erythrocytes of phenotype S-s-. Biochem J. 1977 Jul 1;165(1):157–161. doi: 10.1042/bj1650157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Tanner M. J., Anstee D. J. The membrane change in En(a-) human erythrocytes. Absence of the major erythrocyte sialoglycoprotein. Biochem J. 1976 Feb 1;153(2):271–277. doi: 10.1042/bj1530271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2964–2968. doi: 10.1073/pnas.72.8.2964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Tuech J. K., Morrison M. Human erythrocyte membrane sialoglycoproteins: a study of interconversion. Biochem Biophys Res Commun. 1974 Jul 10;59(1):352–360. doi: 10.1016/s0006-291x(74)80214-7. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES