Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1984 Jul 1;221(1):97–104. doi: 10.1042/bj2210097

Individuals lacking the Gerbich blood-group antigen have alterations in the human erythrocyte membrane sialoglycoproteins beta and gamma.

D J Anstee, K Ridgwell, M J Tanner, G L Daniels, S F Parsons
PMCID: PMC1144007  PMID: 6466322

Abstract

Membranes from erythrocytes with a new Gerbich (Ge)-negative phenotype (Leach phenotype), as well as those from two other Ge-negative phenotypes, were examined. Whereas cells of the Leach phenotype apparently lack three minor sialoglycoproteins (beta, beta 1 and gamma), the membranes of Ge- Yus- and Ge- Yus+ erythrocytes apparently lack beta- and gamma-sialoglycoproteins but contain additional diffusely migrating components of apparent Mr 30 500-34 500 and 32 500-36 500 respectively. Immunoprecipitation experiments showed that the abnormal components of both Ge- Yus- and Ge- Yus+ erythrocytes reacted with two monoclonal antibodies, BRIC 4 and BRIC 10. These antibodies have been shown to react with sialoglycoproteins beta and beta 1 in normal erythrocytes. Cytoskeletal preparations from Ge- Yus- and Ge- Yus+ erythrocyte membranes contained the abnormal components. In contrast with cells of the Leach phenotype, which are elliptocytic, Ge- Yus- and Ge- Yus+ were of normal shape, despite their apparent lack of beta- and gamma-sialoglycoproteins. It seems likely that the abnormal components in these cells contribute to their normal shape. Ovalocytic erythrocytes were shown to incorporate more radioactivity in the sialoglycoprotein-beta 1 region than normal erythrocytes after labelling by the periodate/NaB3H4 technique. It is suggested that abnormal components in Ge- Yus- and Ge- Yus+ erythrocytes result from chromosomal misalignment with unequal crossing-over at meiosis between the genes giving rise to beta-, beta 1- and gamma-sialoglycoproteins.

Full text

PDF
97

Images in this article

Selected References

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

  1. Anstee D. J., Mawby W. J., Tanner M. J. Abnormal blood-group-Ss-active sialoglycoproteins in the membrane of Miltenberger class III, IV and V human erythrocytes. Biochem J. 1979 Nov 1;183(2):193–203. doi: 10.1042/bj1830193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anstee D. J., Parsons S. F., Ridgwell K., Tanner M. J., Merry A. H., Thomson E. E., Judson P. A., Johnson P., Bates S., Fraser I. D. Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins. Biochem J. 1984 Mar 1;218(2):615–619. doi: 10.1042/bj2180615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bennett V., Stenbuck P. J. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature. 1979 Aug 9;280(5722):468–473. doi: 10.1038/280468a0. [DOI] [PubMed] [Google Scholar]
  4. Booth P. B., McLoughlin K. The Gerbich blood group system, especially in Melanesians. Vox Sang. 1972 Jan;22(1):73–84. doi: 10.1111/j.1423-0410.1972.tb03968.x. [DOI] [PubMed] [Google Scholar]
  5. Booth P. B., Serjeantson S., Woodfield D. G., Amato D. Selective depression of blood group antigens associated with hereditary ovalocytosis among melanesians. Vox Sang. 1977;32(2):99–110. doi: 10.1111/j.1423-0410.1977.tb00612.x. [DOI] [PubMed] [Google Scholar]
  6. Cartron J. P., Andreu G., Cartron J., Bird G. W., Salmon C., Gerbal A. Demonstration of T-transferase deficiency in Tn-polyagglutinable blood samples. Eur J Biochem. 1978 Dec 1;92(1):111–119. doi: 10.1111/j.1432-1033.1978.tb12728.x. [DOI] [PubMed] [Google Scholar]
  7. Dahr W., Beyreuther K., Kordowicz M., Krüger J. N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes. Eur J Biochem. 1982 Jun 15;125(1):57–62. doi: 10.1111/j.1432-1033.1982.tb06650.x. [DOI] [PubMed] [Google Scholar]
  8. Dahr W., Beyreuther K., Steinbach H., Gielen W., Krüger J. Structure of the Ss blood group antigens, II: a methionine/threonine polymorphism within the N-terminal sequence of the Ss glycoprotein. Hoppe Seylers Z Physiol Chem. 1980;361(6):895–906. doi: 10.1515/bchm2.1980.361.1.895. [DOI] [PubMed] [Google Scholar]
  9. Daniels G. L., Banting G., Goodfellow P. A monoclonal antibody related to the human blood group Gerbich. J Immunogenet. 1983 Apr;10(2):103–105. doi: 10.1111/j.1744-313x.1983.tb01022.x. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Gratzer W. B. The red cell membrane and its cytoskeleton. Biochem J. 1981 Jul 15;198(1):1–8. doi: 10.1042/bj1980001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gunson H. H., Stratton F., Mullard G. W. An example of polyagglutinability due to the Tn antigen. Br J Haematol. 1970 Mar;18(3):309–316. doi: 10.1111/j.1365-2141.1970.tb01445.x. [DOI] [PubMed] [Google Scholar]
  13. Judd W. J., Issitt P. D., Pavone B. G., Anderson J., Aminoff D. Antibodies that define NANA-independent MN-system antigens. Transfusion. 1979 Jan-Feb;19(1):12–18. doi: 10.1046/j.1537-2995.1979.19179160260.x. [DOI] [PubMed] [Google Scholar]
  14. Kidson C., Lamont G., Saul A., Nurse G. T. Ovalocytic erythrocytes from Melanesians are resistant to invasion by malaria parasites in culture. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5829–5832. doi: 10.1073/pnas.78.9.5829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Parsons S. F., Judson P. A., Anstee D. J. BRIC 18: a monoclonal antibody with a specificity related to the kell blood group system. J Immunogenet. 1982 Dec;9(6):377–380. doi: 10.1111/j.1744-313x.1982.tb00998.x. [DOI] [PubMed] [Google Scholar]
  17. Ridgwell K., Tanner M. J., Anstee D. J. The Wrb antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells. Biochem J. 1983 Jan 1;209(1):273–276. doi: 10.1042/bj2090273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tanner M. J., Anstee D. J., Mawby W. J. A new human erythrocyte variant (Ph) containing an abnormal membrane sialoglycoprotein. Biochem J. 1980 May 1;187(2):493–500. doi: 10.1042/bj1870493. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES