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Molecular biology of blood groups: cloning the Kell gene

1992; Wiley; Volume: 32; Issue: 2 Linguagem: Inglês

10.1046/j.1537-2995.1992.32292180158.x

1537-2995

W. Marsh,

Glycosylation and Glycoproteins Research

TransfusionVolume 32, Issue 2 p. 98-101 Free Access Molecular biology of blood groups: cloning the Kell gene William Laurence Marsh PhD, FIBiol, FRCPartl, FIMLS, William Laurence Marsh PhD, FIBiol, FRCPartl, FIMLS Senior Immunohematologist The Lindsley F. Kimball Research Institute of The New York Blood Center 310 East 76th Street New York, NY 10021Search for more papers by this author William Laurence Marsh PhD, FIBiol, FRCPartl, FIMLS, William Laurence Marsh PhD, FIBiol, FRCPartl, FIMLS Senior Immunohematologist The Lindsley F. Kimball Research Institute of The New York Blood Center 310 East 76th Street New York, NY 10021Search for more papers by this author First published: February 1992 https://doi.org/10.1046/j.1537-2995.1992.32292180158.xCitations: 6AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S.. Cloning and characterization of DNA complementary to human UDP-GalNAc: Fucα1→2Galαl→3 GalNAc transferase (histo-blood group A transferase) mRNA. J Biol Chem 1990; 265: 1146– 51. 2 Yamamoto F., Clausen H., White T., Marken J., Hakomori S.. Molecular genetic basis of the histo-blood group ABO system. Nature 1990; 345: 229– 33. 3 Larsen RD, Ernst LK, Nair RP, Lowe JB. Molecular cloning, sequence, and expression of a human GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc Natl Acad Sci U S A 1990; 87: 6674– 8. 4 Cherif-Zahar B., Bloy C., Le Van Kim C., et al. Molecular cloning and protein structure of a human blood group Rh polypeptide. Proc Natl Acad Sci U S A 1990; 87: 6243– 7. 5 Avent ND, Ridgwell K., Tanner JA, Anstee DJ. cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh (Rhesus)-blood-group-antigen expression. Biochem J 1990; 271: 821– 5. 6 Siebert PD, Fukuda M.. Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucotide approach: nucleotide sequence and mRNA structure. Proc Natl Acad Sci U S A 1986; 83: 1665– 9. 7 Siebert PD, Fukuda M.. Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and genomic relationship to glycophorin A. Proc Natl Acad Sci U S A 1987; 84: 6735– 9. 8 Tate G., Tanner MGA. Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta. Biochem J 1988; 254: 743– 50. 9 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– 33. 10 Awdch ZL, Alper CA. Inherited structural polymorphism of the fourth component of human complement. Proc Natl Acad Sci U S A 1980; 77: 3576– 80. 11 Belt KT, Carroll MC, Porter RR. The structural basis of the multiple forms of human complement component C4. Cell 1984; 36: 907– 14. 12 Tilley CA, Romans DG, Crookston MC. Localisation of Chido and Rodgers determinants to the C4d fragment of human C4. Nature 1978; 276: 713– 5. 13 Caras IW, Davitz MA, Rhee L., Weddell G., Martin DW, Nussenzweig V.. Cloning of decay-accelerating factor suggests novel use of splicing to generate two proteins. Nature 1987; 325: 545– 9. 14 Medof ME, Lublin DM, Holers VM, et al. Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement. Proc Natl Acad Sci U S A 1987; 84: 2007– 11. 15 Lee S., Zambas ED, Marsh WL, Redman CM. Molecular cloning and primary structure of Kell blood group protein. Proc Natl Acad Sci U S A 1991; 88: 6353– 7. 16 Coombs RRA, Mourant AE, Race RR. New test for the detection of weak and "incomplete" Rh agglutinins. Br J Exp Pathol 1945; 26: 255– 66. 17 Marsh WL, Redman CM. Recent developments in the Kell blood group system. Transfus Med Rev 1987; 1: 4– 20. 18 Redman CM, Marsh WL, Mueller KA, Avellino GP, Johnson CL. Isolation of Kell-active protein from the red cell membrane. Transfusion 1984; 24: 176– 8. 19 Redman CM, Avellino G., Pfeffer SR, et al. Kell blood group antigens are part of a 93,000-dalton red cell membrane protein. J Biol Chem 1987; 261: 9521– 5. 20 Branch DR, Petz LD. A new reagent (ZZAP) having multiple applications in immunohematology. Am J Clin Pathol 1982; 78: 161– 7. 21 Branch DR, Muensch HA, Hian Sy Siok AL, Petz LD. Disulfide bonds are a requirement for Kell and Cartwright (Yta) blood group integrity. Br J Haematol 1983; 54: 573– 8. 22 Advani H., Zamor J., Judd WG, Johnson CL, Marsh WL. Inactivation of Kell blood group antigens by 2-aminoethylisothiouronium bromide. Br J Haematol 1982; 51: 107– 15. 23 Masouredis SP, Sudora E., Mahan LC, Victoria EJ. Immunoelectron microscopy of Kell and Cellano antigens on red cell ghosts. Haematology (Budap) 1980; 13: 59– 64. 24 Hughes-Jones NL, Gardner B.. The Kell system studied with radioactively-labelled anti-K. Vox Sang 1971; 21: 154– 8. 25 Greenbury CL, Moore DH, Nunn LAC. Reaction of 7S and 19S components of immune rabbit antisera with human group A and AB red cells. Immunology 1963; 6: 421– 33. 26 Economidou J., Hughes-Jones NC, Gardner B.. Quantitative measurements concerning A and B antigen sites. Vox Sang 1967; 12: 321– 8. 27 Rochna E., Hughes-Jones NC. The use of purified 125I-labelled anti-γ globulin in the determination of the number of D antigen sites on red cells of different phenotypes. Vox Sang 1965; 10: 675– 86. 28 Letarte M., Vera C., Tran R., et al. Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. J Exp Med 1988; 168: 1247– 53. 29 Shipp MA, Vijayaraghavan J., Schmidt EV, et al. Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): direct evidence by cDNA transfection analysis. Proc Natl Acad Sci U S A 1989; 86: 297– 301. 30 Malfroy B., Schofield PR, Kuang WJ, Seeburg PH, Mason AJ, Henzel WJ. Molecular cloning and amino acid sequence of rat enkephalinase. Biochem Biophys Res Commun 1987; 144: 59– 66. 31 Devault A., Lazure C., Nault C., et al. Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complimentary DNA. EMBO J 1987; 6: 1317– 22. 32 Marsh WL, Redman CM. Kell blood group glycoprotein in normal and Ko cell (abstract). Transfusion 1985; 25: 470. 33 Taswell HF, Lewis JC, Marsh WL, Wimer BM, Pineda AA, Brzica SM. Erythrocyte morphology in genetic defects of the Rh and Kell blood group systems. Mayo Clic Proc 1977; 52: 157– 9. 34 Poschmann A., Fischer K., Seidl S., Spielmann W.. ABH receptors and red cell survival in "Bombay" blood. Immunofluorescence studies by phytohemagglutinins and Helix agglutinins. Vox Sang 1974; 27: 338– 46. Citing Literature Volume32, Issue2February 1992Pages 98-101 ReferencesRelatedInformation