JMH Antigen

  • Helmut Schenkel-Brunner


The John Milton Hagen antigen JMH is a high-incidence serological character [7](1). It is expressed on erythrocytes and weakly on peripheral blood lymphocytes [2,3] as well as on a series of non-haematopoietic human tissues, such as neurons of the central nervous system and in respiratory epithelium [5].


Erythrocyte Membrane Respiratory Epithelium Blood Group Antigen Erythrocyte Membrane Protein Intact Erythrocyte 


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  1. 1.
    Bobolis, K. A., Moulds, J. J. & Telen, M. J. (1992): Isolation of the JMH antigen on a novel phosphatidylinositol-linked human membrane protein. Blood 79, 1574–1581.PubMedGoogle Scholar
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    Daniels, G. L. & Knowles, R. W. (1982): A monoclonal antibody to the high frequency red cell antigen JMH. J. Immunogenet. 9, 57–62.PubMedCrossRefGoogle Scholar
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    Moulds, J. J., Levene, C. & Zimmernman, S. (1982): Serological evidence for heterogeneity among antibodies compatible with JMH-negative red cells. 17th Congress of the International Society of Blood Transfusion, Budapest, Hungary 1982, Abstract 287.Google Scholar
  5. 5.
    Mudad, R., Rao, N., Angelisova, P., Horeji, V. & Telen, M. J. (1995): Evidence that CDwl08 membrane protein bears the JMH blood group antigen. Transfusion 35, 566–570.PubMedCrossRefGoogle Scholar
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    Mudad, R., Rao, N., Issitt, P. D., Roy, R. B., Combs, M. R. & Telen, M. J. (1995): JMH variants: serologic, clinical, and biochemical analyses in two cases. Transfusion 35, 925–930.PubMedCrossRefGoogle Scholar
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    Sabo, B., Moulds, J. J. & Mccreary, J. (1978): Anti-JMH: another high titer low avidity antibody against a high frequency antigen. Transfusion 18, 387–389.Google Scholar
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    Schlossman, S. R, Boumsell, L., Gllks, W., Harlan, J. M., Klshimoto, T., Morimoto, C., Rltz, J., Shaw, S., Silverstein, R. L., Springer, T. A., Tedder, T. F. & Todd, R. F. (1994): CD antigens 1993. Blood 83, 879–880.PubMedGoogle Scholar
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    Telen, M. J., Rosse, W. F., Parker, C. J., Moulds, M. K. & Moulds, J. J. (1990): Evidence that several high-frequency human blood group antigens reside on phosphatidylinositol-linked erythrocyte membrane proteins. Blood 75, 1404–1407.PubMedGoogle Scholar
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    Yamada, A., Kubo, K., Takeshita, T., Harashima, N., Kawano, K., Mine, T., Sagawa, K., Sugamura, K. & Itoh, K. (1999): Molecular cloning of a glycosylphosphatidylinositol-anchored molecule CDw108. J. Immunol. 162, 4094–4100.PubMedGoogle Scholar

Copyright information

© Springer-Verlag Wien 2000

Authors and Affiliations

  • Helmut Schenkel-Brunner
    • 1
  1. 1.Institut für Medizinische BiochemieUniversität WienViennaAustria

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