Human Blood Group Genes 2010: Chromosomal Locations and Cloning Strategies Revisited

Transfusion Medicine Reviews

Volumn 25, Issue 1, 2011, Pages 36-46

  Lögdberg, Lennart ^a   Reid, Marion E ^b   Zelinski, Teresa ^c  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NEW YORK BLOOD CENTER   (United States)

^c UNIVERSITY OF MANITOBA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C3B RECEPTOR;

AUTOSOME; BLOOD GROUP; BLOOD GROUP GENE; CHROMOSOMAL LOCALIZATION; CYTOGENETICS; DNA SEQUENCE; FLUORESCENCE IN SITU HYBRIDIZATION; GENE; HUMAN; MOLECULAR CLONING; P1PK SYSTEM; PHENOTYPE; REVIEW;

BLOOD GROUP ANTIGENS; BLOOD GROUPING AND CROSSMATCHING; CHROMOSOME MAPPING; CLONING, MOLECULAR; HUMANS; TIME FACTORS;

EID: 78649824677     PISSN: 08877963     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tmrv.2010.08.005     Document Type: Review

References (88)

1. Reid M.E., McManus K., Zelinski T. Chromosome location of genes encoding human blood groups. Transf Med Rev 1998, 12:151-161.
2. Lögdberg L., Reid M.E., Lamont R.E., et al. Human blood group genes 2004: Chromosomal locations and cloning strategies. Transf Med Rev 2005, 19:45-57.
3. Lögdberg L., Reid M.E., Miller J.L. Cloning and genetic characterization of blood group carrier molecules and antigens. Transf Med Rev 2002, 16:1-10.
4. Yamamoto F., Marken J., Tsuji T., et al. Cloning and characterization of DNA complementary to human UDP-GalNAc: Fucα1α2Galα1α3GalNAc transferase (histo-blood group A transferase) mRNA. J Biol Chem 1990, 265:1146-1151.
5. Siebert P.D., Fukuda M. Molecular cloning of a human glycophorin B cDNA: Nucleotide sequence and genomic relationship to glycophorin A. Proc Natl Acad Sci USA 1987, 84:6735-6739.
6. Keusch J.J., Manzella S.M., Nyame K.A., et al. Cloning of Gb3 synthase, the key enzyme in globo-series glycosphingolipid synthesis, predicts a family of alpha 1, 4-glycosyltransferases conserved in plants, insects, and mammals. J Biol Chem 2000, 275:25315-25321.
7. k UDP-galactose: Ga1α-4G1cα1-cer α1, 4-galactosyltransferase. Molecular genetic basis of the p phenotype. J Biol Chem 2000, 275:16723-16729.
8. Kojima Y., Fukumoto S., Furukawa K., et al. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J Biol Chem 2000, 275:15152-15156.
9. Iwamura K., Furukawa K., Uchikawa M., et al. The blood group P1 synthase gene is identical to the Gb3/CD77 synthase gene. A clue to the solution of the P1/P2/p puzzle. J Biol Chem 2003, 278:44429-44438.
10. Avent N.D., Ridgwell K., Tanner M.J.A., et al. cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh (Rhesus)-blood-group-antigen expression. Biochem J 1990, 271:821-825.
11. Le Van Kim C., Mouro I., Chérif-Zahar B., et al. Molecular cloning and primary structure of the human blood group RhD polypeptide. Proc Natl Acad Sci USA 1992, 89:10925-10929.
12. Arce M.A., Thompson E.S., Wagner S., et al. Molecular cloning of RhD cDNA derived from a gene present in RhD-positive, but not RhD-negative individuals. Blood 1993, 82:651-655.
13. Kajii E., Umenishi F., Iwamoto S., et al. Isolation of a new cDNA clone encoding an Rh polypeptide associated with the Rh blood group system. Hum Genet 1993, 91:157-162.
14. Parsons S.F., Mallinson G., Holmes C.H., et al. The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver. Proc Natl Acad Sci USA 1995, 92:5496-5500.
15. Lee S., Zambas E.D., Marsh W.L., et al. Molecular cloning and primary structure of Kell blood group protein. Proc Natl Acad Sci USA 1991, 88:6353-6357.
16. Kukowska-Latallo J.F., Larsen R.D., Nair R.P., et al. A cloned human cDNA determines expression of a mouse state-specific embryonic antigen and the Lewis blood group α(1,3/1,4)fucosyltransferase. Genes & Devel 1990, 4:1288-1303.
17. Chaudhuri A., Polyakova J., Zbrzezna V., et al. Cloning of glycoprotein D cDNA, which encodes the major subunit of the duffy blood group system and the receptor for the Plasmodium vivax malaria parasite. Proc Natl Acad Sci USA 1993, 90:10793-10797.
18. Olivès B., Mattei M.G., Huet M., et al. Kidd blood group and urea transport function of human erythrocytes are carried by the same protein. J Biol Chem 1995, 270:15607-15610.
19. Lux S.E., John K.M., Kopito R.R., et al. Cloning and characterization of band 3, the human erythrocyte anion- exchange protein (AE1). Proc Natl Acad Sci USA 1989, 86:9089-9093.
20. a) blood group antigen. Biochem J 1992, 288:713-716.
21. Li Y., Camp S., Rachinsky T.L., et al. Gene structure of mammalian acetylcholinesterase: Alternative exons dictate tissue-specific expression. J Biol Chem 1991, 266:23083-23090.
22. Bartels C.F., Zelinski T., Lockridge O. Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism. Am J Hum Genet 1993, 52:928-936.
23. Ellis N.A., Ye T.Z., Patton S., et al. Cloning of PBDX, an MIC2-related gene that spans the pseudoautosomal boundary on chromosome Xp. Nature Genet 1994, 6:394-400.
24. Ellis N.A., Tippett P., Petty A., et al. PBDX is the XG blood group gene. Nature Genet 1994, 8:285-290.
25. Xu H., Foltz L., Sha Y., et al. Cloning and characterization of human erythroid membrane-associated protein, human ERMAP. Genomics 2001, 76:2-4.
26. Su Y.Y., Gordon C.T., Ye T.Z., et al. Human ERMAP: An erythroid adhesion/receptor transmembrane protein. Blood Cells Mol Dis 2001, 27:938-949.
27. Wagner F.F., Poole J., Flegel W.A. The Scianna antigens including Rd are expressed by ERMAP. Blood 2003, 101:752-757.
28. Gubin A.N., Njoroge J.M., Wojda U., et al. Identification of the Dombrock blood group glycoprotein as a polymorphic member of the ADP-ribosyltransferase gene family. Blood 2000, 96:2621-2627.
29. Preston G.M., Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family. Proc Natl Acad Sci USA 1991, 88:11110-11114.
30. Bailly P., Hermand P., Callebaut I., et al. The LW blood group glycoprotein is homologous to intercellular adhesion molecules. Proc Natl Acad Sci USA 1994, 91:5306-5310.
31. Yu C.Y. The complete exon-intron structure of a human complement component C4A gene. DNA sequences, polymorphism, and linkage to the 21-hydroxylase gene. J Immunol 1991, 146:1057-1066.
32. Kelly R.J., Ernst L.K., Larsen R.D., et al. Molecular basis for H blood group deficiency in Bombay (Oh) and para-Bombay individuals. Proc Natl Acad Sci USA 1994, 91:5843-5847.
33. Ho M., Chelly J., Carter N., et al. Isolation of the gene for McLeod syndrome that encodes a novel membrane transport protein. Cell 1994, 77:869-880.
34. Colin Y., Rahuel C., London J., et al. Isolation of cDNA clones and complete amino acid sequence of human erythrocyte glycophorin C. J Biol Chem 1986, 261:229-233.
35. Medof M.E., Lublin D.M., Holers V.M., et al. Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement. Proc Natl Acad Sci USA 1987, 84:2007-2011.
36. Spring F.A., Judson P.A., Daniels G.L., et al. A human cell-surface glycoprotein that carries Cromer-related blood group antigens on erythrocytes and is also expressed on leucocytes and platelets. Immunology 1987, 62:307-313.
37. Telen M.J., Hall S.E., Green A.M., et al. Identification of human erythrocyte blood group antigens on decay-accelerating factor (DAF) and an erythrocyte phenotype negative for DAF. J Exp Med 1988, 167:1993-1998.
38. Moulds J.M., Nickells M.W., Moulds J.J., et al. The C3b/C4b receptor is recognized by the Knops, McCoy, Swain-Langley, and York blood group antisera. J Exp Med 1991, 173:1159-1163.
39. Stamenkovic I., Aruffo A., Amiot M., et al. The hematopoietic and epithelial forms of CD44 are distinct polypeptides with different adhesion potentials for hyaluronate-bearing cells. EMBO J 1991, 10:343-348.
40. b blood group antigens are located on a glycoprotein of 80,000 MW (the CDw44 glycoprotein) whose expression is influenced by the In(Lu) gene. Immunology 1988, 64:37-43.
41. Kasinrerk W., Fiebiger E., Stefanova I., et al. Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule. J Immunol 1992, 149:847-854.
42. Biswas C., Zhang Y., DeCastro R., et al. The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res 1995, 55:434-439.
43. a blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues. Eur J Immunol 1997, 27:891-897.
44. Fitter S., Tetaz T.J., Berndt M.C., et al. Molecular cloning of cDNA encoding a novel platelet-endothelial cell tetra-span antigen, PETA-3. Blood 1995, 86:1348-1355.
45. Crew V.K., Green C.A., Daniels G., et al. Renal failure associated with an inactivating mutation in the human CD151 gene of three individuals lacking the MER2 blood group. Blood 2003, 102:4a. (abstr).
46. Crew V.K., Burton N., Kagan A., et al. CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood 2004, 104:2217-2223.
47. Yamada A., Kubo K., Takeshita T., et al. Molecular cloning of a glycosylphosphatidylinositol-anchored molecule CDw108. J Immunol 1999, 162:4094-4100.
48. Bierhuizen M.F., Mattei M.G., Fukuda M. Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family. Genes Dev 1993, 7:468-478.
49. Yu L.C., Twu Y.C., Chang C.Y., et al. Molecular basis of the adult I phenotype and the gene responsible for the expression of the human blood group I antigen. Blood 2001, 98:3840-3845.
50. Yu L.C., Twu Y.C., Chou M.L., et al. The molecular genetics of the human I locus and molecular background explaining the partial association of the adult I phenotype with congenital cataracts. Blood 2003, 101:2081-2087.
51. Inaba N., Hiruma T., Togayachi A., et al. A novel I-branching β-1,6-N-acetylglucosaminyltransferase involved in human blood group I antigen expression. Blood 2003, 101:2870-2876.
52. Okajima T., Nakamura Y., Uchikawa M., et al. Expression cloning of human globoside synthase cDNAs. Identification of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta 1,3-N-acetylgalactosaminyltransferase. J Biol Chem 2000, 275:40498-40503.
53. k blood group phenotype. Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: Globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene. J Biol Chem 2002, 277:29455-29459.
54. Inase N., Fushimi K., Ishibashi K., et al. Isolation of human aquaporin 3 gene. J Biol Chem 1995, 270:17913-17916.
55. Roudier N., Ripoche P., Gane P., et al. AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL. J Biol Chem 2002, 277:45854-45859.
56. Ridgwell K., Spurr N.K., Laguda B., et al. Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression. Biochem J 1992, 287:223-228.
57. Daniels G., Castilho L., Flegel W.A., et al. International society of blood transfusion committee on terminology for red cell surface antigens: Macao report. Vox Sang 2009, 96:153-156.
58. Tilley L., Green C., Poole J., et al. A new blood group system, RHAG: Three antigens resulting from amino acid substitutions in the Rh-associated glycoprotein. Vox Sang 2010, 98:151-159.
59. An International System for Human Cytogenetic Nomenclature (1985 ISCN (1985) 1985, Basel, S. Karger. H.P. Standing Committee on Human Cytyogenetic Nomenclature, Klinger (Eds.).
60. Ensembl Genome Browser. http://www.ensembl.org.
61. Blood Group Antigen Gene Mutation Database. http://bioc.aecom.yu.edu/bgmut/index.htm.
62. UCSC Genome Bioinformatics. http://genome.ucsc.org.
63. National Center for Biotechnology Information. http://www.ncbi.nlm.nih.gov.
64. Moore S., Green C. The identification of specific Rhesus polypeptide blood group ABH-active glycoprotein complexes in the human red-cell membrane. Biochem J 1987, 244:735-741.
65. Avent N., Judson P.A., Parsons S.F., et al. Monoclonal antibodies that recognize different membrane proteins that are deficient in Rhnull human erythrocytes. One group of antibodies reacts with a variety of cells and tissues whereas the other group is erythroid-specific. Biochem J 1988, 251:499-505.
66. Avent N.D., Ridgwell K., Mawby W.J., et al. Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane. Biochem J 1988, 256:1043-1046.
67. Chérif-Zahar B., Matassi G., Raynal V., et al. Rh-deficiency of the regulator type caused by splicing mutations in the human RH50 gene. Blood 1998, 92:2535-2540.
68. Chérif-Zahar B., Raynal V., Gane P., et al. Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency. Nature Genet 1996, 12:168-173.
69. mod syndrome: A family study of the translation-initiator mutation in the Rh50 glycoprotein gene. Am J Hum Genet 1999, 64:108-117.
70. null disease. J Biol Chem 1998, 273:2207-2213.
71. null syndrome: Identification of three new missense mutations in the Rh50 glycoprotein gene. Am J Hematol 1999, 62:25-32.
72. 279→Glu missense mutation in the conserved transmembrane segment. Blood 1998, 92:1776-1784.
73. null blood donor of the regulator type. Blood 1998, 91:1458-1463.
74. null phenotype. Ann Hum Genet 1998, 62:107-113.
75. Lin Y., Pavenski K., Saidenberg E., et al. Blood group antigens and normal red blood cell physiology: A Canadian blood services research and development symposium. Transfus Med Rev 2009, 23:292-309.
76. Habibi B., Fouillade M.T., Duedari N., et al. The antigen Duclos. A new high frequency red cell antigen related to Rh and U. Vox Sang 1978, 34:302-309.
77. Kornstad L. A rare blood group antigen, Ola (Oldeide), associated with weak Rh antigens. Vox Sang 1986, 50:235-239.
78. Daniels G.L., Anstee D.J., Cartron J.P., et al. Blood group terminology 1995. ISBT working party on terminology for red cell surface antigens. Vox Sang 1995, 69:265-279.
79. Reid M.E., Lomas-Francis C. Blood Group Antigen FactsBook 2003, Academic Press, San Diego. 2nd ed.
80. Daniels G.L., Cartron J.P., Fletcher A., et al. international society of blood transfusion committee on terminology for red cell surface antigens: Vancouver report. Vox Sang 2003, 84:244-247.
81. Hellberg A., Chester M.A., Olsson M.L. Two previously proposed P1/P2-differentiating and nine novel polymorphisms at the A4GALT (Pk) locus do not correlate with the presence of the P1 blood group antigen. BMC Genet 2005, 6:49.
82. Tilley L., Green C., Daniels G. Sequence variation in the 5' untranslated region of the human A4GALT gene is associated with, but does not define, the P1 blood-group polymorphism. Vox Sang 2006, 90:198-203.
83. 2 histo-blood groups made possible by identification of a novel A4GALT exon. Transfusion 2009, 49(Suppl):48A. (abstr).
84. Lee S., Debnath A.K., Redman C.M. Active amino acids of the Kell blood group protein and model of the ectodomain based on the structure of neutral endopeptidase 24.11. Blood 2003, 102:3028-3034.
85. Neote K., Mak J.Y., Kolakowski L.F., et al. Functional and biochemical analysis of the cloned Duffy antigen: Identity with the red blood cell chemokine receptor. Blood 1994, 84:44-52.
86. Horuk R., Chitnis C.E., Darbonne W.C., et al. A receptor for the malarial parasite Plasmodium vivax: The erythrocyte chemokine receptor. Science 1993, 261:1182-1184.
87. Chaudhuri A., Zbrzezna V., Polyakova J., et al. Expression of the Duffy antigen in K562 cells. Evidence that it is the human erythrocyte chemokine receptor. J Biol Chem 1994, 269:7835-7838.
88. Darbonne W.C., Rice G.C., Mohler M.A., et al. Red blood cells are a sink for interleukin 8, a leukocyte chemotaxin. J Clin Invest 1991, 88:1362-1369.