Have a personal or library account? Click to login
JMH blood group system: a review Cover
By: S.T. Johnson  
Paid access
|Oct 2019

References

  1. Rolih SD. High-titer, low-avidity (HTLA) antibodies and antigens: a review. Transfus Med Rev 1989;3:128–39.10.1016/S0887-7963(89)70074-2
  2. Issitt PD. Applied blood group serology. 4th ed. Durham, NC: Montgomery Scientific Publications, 1998.
  3. Issitt PD. Applied blood group serology. 2nd ed. Oxnard, CA: Spectra Biologicals, 1975.
  4. Sabo B, Moulds JJ, McCreary J. Anti-JMH: another high titer-low avidity antibody against a high frequency antigen (abstract). Transfusion 1978;18:387.
  5. Baldwin ML, Ness PM, Barrasso C, et al. In vivo studies of the long-term 51Cr red cell survival of serologically incompatible red cell units. Transfusion 1985;25:34–8.10.1046/j.1537-2995.1985.25185116499.x3969699
  6. Daniels GL, Green C, Lomas C, Tippet P. Monoclonal antibodies recognizing high-frequency RBC antigens, including type 2H and JMH (abstract). Transfusion 1981:21;612.
  7. Daniels GL, Knowles RW. A monoclonal antibody to the high frequency red cell antigen JMH. J Immunogenet 1982;9:57–9.10.1111/j.1744-313X.1982.tb00783.x
  8. Moulds JJ, Levene C, Zimmernam S. Serological e vidence for heterogeneity among antibodies compatible with JMH-negative red cells (abstract). Abstracts of the Joint Meeting of the 19th Congress of the International Society of Haematology and the 17th Congress of the International Society of Blood Transfusion. 1982:287.
  9. Telen MJ, Rosse WF, Parker CJ, Moulds MK, Moulds JJ. Evidence that several high-frequency human blood group antigens reside on phosphatidylinositol-linked erythrocyte membrane proteins. Blood 1990;75:1404–7.10.1182/blood.V75.7.1404.1404
  10. Bobolis KA, Moulds JJ, Telen MJ. Isolation of the JMH antigen on novel phosphatidylinositol-linked human membrane protein. Blood 1992;79:1574–81.10.1182/blood.V79.6.1574.1574
  11. Mudud R, Rao N, Angelisova P, Horejsi V, Telen MJ. Evidence that CDw108 membrane protein bears the JMH blood group antigen. Transfusion 1995;35:566–70.10.1046/j.1537-2995.1995.35795357878.x7631388
  12. Yamada A, Kubo K, Takeshita T, et al. Molecular cloning of a glycosylphosphatidylinositol-anchored molecule CDw108. J Immunol 1999;162:4094–100.
  13. Daniels GL, Anstee DJ, Cartron JP, et al. International Society of Blood Transfusion Working Party on Terminology for Red Cell Surface Antigens. Vox Sang 2001;80:193–7.10.1046/j.1423-0410.2001.00024.x11449960
  14. Seltsam A, Strigens S, Levene C, et al. The molecular diversity of Sema7A, the semaphorin that carries the JMH blood group antigens. Transfusion 2007;47:133–46.10.1111/j.1537-2995.2007.01076.x17207242
  15. Richard M, St-Laurent J, Perreault J, Long A, St-Louis M. A new SEMA7A variant found in Native Americans with alloantibody. Vox Sang 2011;100:322–6.10.1111/j.1423-0410.2010.01413.x20854351
  16. Daniels G, Flegel WA, Fletcher A, et al. International Society of Blood Transfusion Committee on Terminology for Red Cell Surface Antigens: Cape Town report. Vox Sang 2007;92: 250–3.10.1111/j.1423-0410.2007.00887.x17348875
  17. Storry JR, Castilho L, Daniels G, et al. International Society of Blood Transfusion Working Party on red cell immunogenetics and blood group terminology: Berlin report. Vox Sang 2011; 101:77–82.10.1111/j.1423-0410.2010.01462.x549784821401621
  18. Suzuki K, Okuno T, Yamamoto M, et al. Semaphorin 7A initiates T-cell-mediated inflammatory responses through alpha1beta1 integrin. Nature 2007;446:680–4.10.1038/nature0565217377534
  19. Kikutani H, Kumanogh A. Semaphorins in interactions between T cells and antigen-presenting cells. Nat Rev Immunol 2003;3:159–67.10.1038/nri100312563299
  20. Yazdani U, Terman JR. The semaphorins. Genome Biol 2006; 7:211.10.1186/gb-2006-7-3-211155774516584533
  21. Holmes S, Downs AM, Fosberry A, et al. Sema7A is a potent monocyte stimulator. Scand J Immunol 2002;56:270–5.10.1046/j.1365-3083.2002.01129.x12193228
  22. Gras C, Eiz-Vesper B, Seltsam A, Immenschuh S, Blasczyk R, Figueiredo. Semaphorin 7A protein variants differentially regulate T-cell activity. Transfusion 2013;53:270–83.10.1111/j.1537-2995.2012.03812.x22845496
  23. Koh J-M, Oh B, Lee JY, et al. Association study of semaphorin 7a (sema7a) polymorphisms with bone mineral density and fracture risk in postmenopausal Korean women. J Hum Genet 2006;51:112–17.10.1007/s10038-005-0331-z16372136
  24. Kang H-R, Lee CG, Homer RJ, Elias JA. Semaphorin 7A plays a critical role in TGF-beta1-induced pulmonary fibrosis. J Exp Med 2007;204:1083–93.10.1084/jem.20061273211857517485510
  25. Anstee DJ. The functional importance of blood group-active molecules in human red blood cells. Vox Sang 2011;100:140–9.10.1111/j.1423-0410.2010.01388.x21175664
  26. Bartholdson SJ, Bustamente LY, Crosnier C, et al. Semaphorin-7A is an erythrocyte receptor for P. falciparum merozoite-specific TRAP homolog, MTRAP. PLoS Pathog 2012; 8:e1003031.10.1371/journal.ppat.1003031349958323166499
  27. Kollmar M, South SF, Tregellas WM. Evidence of a genetic mechanism for the production of the JMH negative phenotype (abstract). Transfusion 1981;21:612.
  28. Daniels G. Human blood groups. 3rd ed. Wiley-Blackwell, 2013:467.10.1002/9781118493595
  29. Stroka-Lee AH, Halverson GR. Collecting GPI-negative RBCs from patients with paroxysmal nocturnal hemoglobinuria for use in serological investigations (abstract). Transfusion 2010;50(Suppl):167A.
  30. Whitsett CF, Moulds M, Pierce JA, Hare V. Anti-JMH identified in serum and eluate from red cells of a JMH-negative man. Transfusion 1983;23:344–5.10.1046/j.1537-2995.1983.23483276874.x6410552
  31. Tregellas WM, Pierce SR, Harding JT, Beck ML. Anti-JMH: IgG subclass composition and clinical significance (abstract). Transfusion 1980;20:628.
  32. Garratty G, Arndt P, Nance S. IgG subclass of blood group alloantibodies to high frequency antigens (abstract). Transfusion 1996;36(Suppl 9S):50S.
  33. Pope J, Lubenko A, Lai WYY. A survey of the IgG subclasses of antibodies to high frequency red cell antigens (abstract). Transf Med 1991;1(Suppl 2):58.
  34. Geisland J, Corgan M, Hillard B. An example of anti-JMH with characteristics of a clinically significant antibody. Immunohematology 1990;6:9–11.10.21307/immunohematology-2019-1031
  35. Seltsam A, Agaylan A, Grueger D, Meyer O, Blasczyk R, Salama A. Rapid detection of JMH antibodies with recombinant Sema7A (CD108) protein and the particle gel immunoassay. Transfusion 2008;48:1151–5.10.1111/j.1537-2995.2008.01660.x18422858
  36. Baldwin ML, Ness PM, Barrasso C, et al. In vivo studies of the long-term 51Cr red cell survival of serologically incompatible red cell units. Transfusion 1985;25:34–8.10.1046/j.1537-2995.1985.25185116499.x3969699
  37. Mudad R, Rao N, Issitt PD, Roy RB, Combs MR, Telen MJ. JMH variants: serologic, clinical, and biochemical analyses in two cases. Transfusion 1995;35:925–30.10.1046/j.1537-2995.1995.351196110897.x8604490
  38. Hoppe B, Pastucha L, Seltsam A, Greinacher A, Salama A. Acute haemolytic transfusion reactions due to weak antibodies that in vitro did not seem to be clinically significant. Vox Sang 2002;82:207–10.10.1046/j.1423-0410.2002.00171.x12047515
DOI: https://doi.org/10.21307/immunohematology-2019-094 | Journal eISSN: 1930-3955 | Journal ISSN: 0894-203X
Language: English
Page range: 18 - 23
Published on: Oct 29, 2019
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year

© 2019 S.T. Johnson, published by American National Red Cross
This work is licensed under the Creative Commons License.