THE BIOCHEMISTRY OF BLOOD GROUP ANTIGENS ‐ SOME RECENT ADVANCES

Name: THE BIOCHEMISTRY OF BLOOD GROUP ANTIGENS ‐ SOME RECENT ADVANCES
Uploaded: 1994-07-01

David J. Anstee; Gary Mallinson

Basic Information

ID: W2076746819
Title: THE BIOCHEMISTRY OF BLOOD GROUP ANTIGENS ‐ SOME RECENT ADVANCES
Abstract: Vox SanguinisVolume 67, Issue s3 p. 1-6 THE BIOCHEMISTRY OF BLOOD GROUP ANTIGENS - SOME RECENT ADVANCES DAVID J. ANSTEE, DAVID J. ANSTEE International Blood Group Reference Laboratory Southmead Road Bristol BS10 5ND United KingdomSearch for more papers by this authorGARY MALLINSON, GARY MALLINSON International Blood Group Reference Laboratory Southmead Road Bristol BS10 5ND United KingdomSearch for more papers by this author DAVID J. ANSTEE, DAVID J. ANSTEE International Blood Group Reference Laboratory Southmead Road Bristol BS10 5ND United KingdomSearch for more papers by this authorGARY MALLINSON, GARY MALLINSON International Blood Group Reference Laboratory Southmead Road Bristol BS10 5ND United KingdomSearch for more papers by this author First published: July 1994 https://doi.org/10.1111/j.1423-0410.1994.tb04536.xCitations: 9AboutPDF 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 onEmailFacebookTwitterLinkedInRedditWechat References 1 Lowe, JB: The blood group-specific human glycosyltransferases: in MJA Tanner and DJ Anstee (eds): Baille res Clinical Haematology, Oxford, 1993 vol 6.2 pp 465–492. 2 Giles, CM: An update on Rodgers and Chido, the antigenic determinants of human C4. Immunohaematology 1989; 5: 1–6. 3 Fukuda, M: Molecular genetics of the Glycophorin A gene cluster. Semin Hematol 1993; 30: 138–151. 4 Cartron, J-P, Le van Kim, C, Colin, Y: Glycophorin C and related glycoproteins: structure, function and regulation. Semin Hematol 1993; 30: 152–168. 5 Mourant, AE, Kopec, AC, Domaniewska-Sobczak, K: The distribution of human blood groups and other polymorphisms, 2nd edn, Oxford University Press, London 1976, pp 20–24. 6 Spring, FA, Bruce, LJ, Anstee, DJ and Tanner, MJA: A red cell band 3 variant with altered stilbene disulphonate binding is associated with the Diego (Dia) blood group antigen. Biochem J 1992; 288: 713–716. 7 Yannoukakos, D, Vasseur, C, Driancourt, C, Blouquit, Y, Delauney, J, Wajcman, H and Bursaux, E: Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56 Glu) by protein chemistry methods. Blood 1991; 78: 117–1120. 8 Hsu, L and Morrison, M: A new variant of the anion transport protein in human erythrocyte. Biochemistry 1985; 24: 3086–3090. 9 Bruce, LJ, Anstee, DJ, Spring, FA, Tanner, MJA: Band 3 Memphis variant II: altered stilbene disulphonate binding and the Diego (Dia) blood group antigen are associated with the human erythrocyte band 3 mutation pro854 leu. J Biol Chem (in press). 10 Anstee, DJ, Tanner, MJA: Biochemical aspects of blood group Rh (Rhesus) antigens in red cell membrane and red cell antigens: in MJA Tanner and DJ Anstee (eds): Bailli res Clinical Haematology, Oxford, 1993, vol 6.2, pp 401–422. 11 Cartron, J-P, Agre, P: Rh blood group antigens: protein and gene structure. Semin Hematol 1993; 30: 193–208. 12 Mouro, I, Colin, Y, Cherif-Zahar, B, Cartron, J-P, Le Van Kim, C: Molecular genetic basis of the human Rhesus blood group system. Nature Genet 1993; 5: 62–65. 13 Avent, ND, Liu, W, Jackson, S, Isaac, A, Anstee, DJ: Molecular cloning of Rh30 cDNA's from individuals expressing different Rh phenotypes: molecular basis of the Rh C/c and E/e polymorphisms. 23rd Congress of Int Soc of Blood Transf, Amsterdam (abstract) 1994. 14 Smith, B L, Preston, G M, Spring, F A, Anstee, DJ, Agre, P: Molecular characterisation of ABH and Colton blood group antigens on human aquaporin-1 (CHIP water channel protein). Clin Res (in press). 15 Agre, P, Preston, GM, Smith, BL, Sup Jung, J, Raina, S, Moon, C, Guggino, WB and Nielson, S: Aquaporin CHIP: the archetypal molecular water channel. Am J Physiol 1993; 265: F463–F476. 16 Anstee, DJ: Minor red cell surface proteins associated with red cell dysfunction: in MJA Tanner and DJ Anstee (eds): Bailli res Clinical Haematology, Oxford, 1993, vol 6.2, pp 445–463. 17 Chaudhuri, A, Polyakova, J, Zbrzezna, V, Williams, K, Gulati, S, Pogo, AO: 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 1993; 90: 10793–10797. 18 Horuk, R, Chitnis, CE, Darbonne, WC, Colby, TJ, Rybicki, A, Hadley, TJ, Miller, LH: A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor. Science 1993; 261: 1182–1184. 19 Parsons, SF, Mawby, WJ, Anstee, DJ: Lutheran blood group glycoprotein is a new member of the immunoglobulin superfamily of proteins. 23rd Congress of ISBT, Amsterdam (abstract) 1994. 20 Staunton, DE, Dustin, ML, Erickson, HP and Springer, TA: The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus. Cell 1990; 61: 243–254. 21 Wang, DN, Khlbrandt, W, Sarabia, VE, Reithmeier, RAF: Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO J 1993; 12: 2233–2239. 22 Walz, T, Smith, BL, Zeidel, ML, Engel, A, Agre, P: Biologically active two-dimensional crystals of Aquaporin CHIP. J Biol Chem 1994; 269: 1583–1586. 23 Berendt, AR, McDowall, A, Craig, AG, Bates, PA, Sternberg, MJE, Marsh, K, Newbold, CI and Hogg, N: The binding site on ICAM-1 for Plasmodium falciporum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site. Cell 1992; 68: 71–81. 24 Lewis, M, Anstee, DJ, Bird, GWG, Brodheim, E, Cartron, J-P, Contreras, M, Crookston, M C, Dahr, W, Daniels, GL, Engelfriet, CP, Giles, CM, Issitt, PD, Jrgensen, J, Kornstad, K, Lubenko, A, Marsh, WL, McCreary, J, Moore, BPL, Morel, P, Moulds, JJ, Nevanlinna, H, Nordhagen, R, Okubo, Y, Rosenfield, RE, Rouger, Ph, Rubinstein, P, Salmon, Ch, Seidl, S., Sistonen, P, Tippett, P, Walker, R H, Woodfield, G, Young, S: Blood group terminology 1990. Vox Sang 1990; 58: 152–169. 25 Daniels, GL, Moulds, JJ, Anstee, DJ, Bird, GWG, Brodheim, E, Cartron, J-P, Dahr, W, Engelfriet, CP, Issitt, PD, Jrgensen, J, Kornstad, L, Lewis, M, Levene, C, Lubenko, A, Mallory, D, Morel, P, Nordhagen, R, Okubo, Y, Reid, M, Rouger, Ph, Salmon, Ch, Seidl, S, Sistonen, P, Wendel, S, Woodfield, G, Zelinski, T: ISBT Working Party on terminology of red cell surface antigens. Vox Sang 1993; 65: 77–80. Citing Literature Volume67, Issues3July 1994Pages 1-6 ReferencesRelatedInformation
Publication Year: 1994
Publication Date: 1994-07-01
Language: en
Type: review
Indexed In: ['crossref', 'pubmed']

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'Bruce,': [293, 387], 'LJ,': [294, 388], 'Anstee,': [295, 389, 428, 520, 563, 620, 730, 881, 961], 'Tanner,': [298, 393, 430], 'MJA:': [299, 394, 431], 'red': [301, 441, 445, 623, 629, 1015], 'cell': [302, 442, 446, 624, 630, 1016], 'band': [303, 343, 417, 800], 'variant': [305, 373, 398], 'altered': [307, 400], 'stilbene': [308, 401], 'disulphonate': [309, 402], 'binding': [310, 403, 773, 858], 'is': [311, 736, 868], 'associated': [312, 412, 627], 'Diego': [315, 406], '(Dia)': [316, 407], 'group': [318, 409, 436, 472, 504, 574, 676, 734, 948], 'antigen.': [319], 'Biochem': [320], 'J': [321, 422, 614, 811, 833], '1992;': [322, 875], '288:': [323], '713–716.': [324], '7': [325], 'Yannoukakos,': [326], 'D,': [327, 986], 'Vasseur,': [328], 'Driancourt,': [330], 'Blouquit,': [332], 'Y,': [333, 487, 925, 992], 'Delauney,': [334], 'J,': [335, 596, 653, 905, 913, 976], 'Wajcman,': [336], 'H': [337], 'Bursaux,': [339], 'E:': [340], 'Human': [341], 'erythrocyte': [342, 416, 718, 808], 'polymorphism': [345], '(band': [346], 'Memphis):': [348], 'characterization': [349], 'structural': [352], 'modification': [353], '(Lys': [354], '56': [355], 'Glu)': [356], 'protein': [358, 378, 474, 805], 'chemistry': [359], 'methods.': [360], '1991;': [362], '78:': [363], '117–1120.': [364], '8': [365], 'Hsu,': [366], 'L': [367], 'Morrison,': [369], 'new': [372, 738], 'anion': [376, 803], 'transport': [377, 804], 'erythrocyte.': [381], 'Biochemistry': [382], '1985;': [383], '24:': [384], '3086–3090.': [385], '9': [386], 'DJ,': [390, 429, 564, 882, 962], 'Band': [395], 'Memphis': [397], 'II:': [399], 'antigen': [410], 'are': [411], 'mutation': [419], 'pro854': [420], 'leu.': [421], 'Biol': [423, 834], 'Chem': [424, 835], '(in': [425, 585], 'press).': [426, 586], '10': [427], 'Biochemical': [432], 'aspects': [433], 'Rh': [437, 470, 531, 537], '(Rhesus)': [438], 'antigens': [439, 575], 'membrane': [443, 796], 'antigens:': [447, 473], 'Bailli': [455, 639], '1993,': [460, 644], '6.2,': [462, 646], '401–422.': [464], '11': [465], 'Agre,': [468, 565, 588, 824], 'P:': [469, 566, 825], 'structure.': [477], '193–208.': [482], '12': [483], 'Mouro,': [484], 'I,': [485], 'Cherif-Zahar,': [488], 'B,': [489], 'Van': [493], 'C:': [495], 'genetic': [497], 'basis': [498, 534], 'Rhesus': [502], 'system.': [505], 'Nature': [506], 'Genet': [507], '62–65.': [510], '13': [511], 'Avent,': [512], 'ND,': [513], 'Liu,': [514], 'W,': [515, 787, 895, 970], 'Jackson,': [516], 'S,': [517, 598, 659, 1000, 1004], 'Isaac,': [518], 'A,': [519, 562, 651, 704, 823, 843, 909, 984], 'DJ:': [521, 621, 731], 'cloning': [523], 'Rh30': [525], "cDNA's": [526], 'from': [527], 'individuals': [528], 'expressing': [529], 'different': [530], 'phenotypes:': [532], 'molecular': [533, 610], 'C/c': [538], 'E/e': [540], 'polymorphisms.': [541], '23rd': [542, 746], 'Congress': [543, 747], 'Int': [545], 'Soc': [546], 'Transf,': [549], 'Amsterdam': [550, 750], '(abstract)': [551, 751], '1994.': [552, 752], '14': [553], 'Smith,': [554, 592, 818], 'B': [555], 'L,': [556, 978], 'Preston,': [557, 590], 'G': [558], 'M,': [559, 880, 890, 980, 994], 'F': [561], 'characterisation': [568], 'ABH': [570], 'Colton': [572], 'aquaporin-1': [578], '(CHIP': [579], 'water': [580, 611], 'channel': [581], 'protein).': [582], 'Clin': [583], 'Res': [584], '15': [587], 'P,': [589, 917, 931, 937, 939, 988, 1002], 'GM,': [591], 'BL,': [593, 819], 'Sup': [594], 'Jung,': [595], 'Raina,': [597], 'Moon,': [599], 'Guggino,': [601], 'WB': [602], 'Nielson,': [604], 'S:': [605, 946], 'Aquaporin': [606, 831], 'CHIP:': [607], 'archetypal': [609], 'channel.': [612], 'Am': [613], 'Physiol': [615], '265:': [617], 'F463–F476.': [618], '16': [619], 'Minor': [622], 'surface': [625, 1017], 'proteins': [626], 'dysfunction:': [631], '445–463.': [648], '17': [649], 'Chaudhuri,': [650], 'Polyakova,': [652], 'Zbrzezna,': [654], 'V,': [655], 'Williams,': [656], 'K,': [657, 851, 907], 'Gulati,': [658], 'Pogo,': [660], 'AO:': [661], 'Cloning': [662], 'glycoprotein': [664, 735], 'D': [665], 'cDNA,': [666], 'which': [667], 'encodes': [668], 'major': [670], 'subunit': [671], 'Duffy': [674], 'system': [677], 'receptor': [680, 710], 'Plasmodium': [683, 715, 863], 'vivax': [684], 'malaria': [685], 'parasite.': [686], 'Proc': [687], 'Natl': [688], 'Acad': [689], 'Sci': [690], '90:': [692], '10793–10797.': [693], '18': [694], 'Horuk,': [695], 'R,': [696, 923, 990], 'Chitnis,': [697], 'CE,': [698], 'Darbonne,': [699], 'WC,': [700], 'Colby,': [701], 'TJ,': [702, 706], 'Rybicki,': [703], 'Hadley,': [705], 'Miller,': [707], 'LH:': [708], 'malarial': [713], 'parasite': [714], 'vivax:': [716], 'chemokine': [719], 'receptor.': [720], 'Science': [721], '261:': [723], '1182–1184.': [724], '19': [725], 'Parsons,': [726], 'SF,': [727], 'Mawby,': [728], 'WJ,': [729], 'Lutheran': [732], 'member': [739], 'immunoglobulin': [742], 'superfamily': [743], 'proteins.': [745], 'ISBT,': [749], '20': [753], 'Staunton,': [754], 'DE,': [755], 'Dustin,': [756], 'ML,': [757, 821], 'Erickson,': [758], 'HP': [759], 'Springer,': [761], 'TA:': [762], 'arrangement': [764], 'immunoglobulin-like': [767], 'domains': [768], 'ICAM-1': [770, 861], 'sites': [774], 'LFA-1': [776], 'rhinovirus.': [778], 'Cell': [779, 874], '1990;': [780, 953], '61:': [781], '243–254.': [782], '21': [783], 'Wang,': [784], 'DN,': [785], 'Khlbrandt,': [786], 'Sarabia,': [788], 'VE,': [789], 'Reithmeier,': [790], 'RAF:': [791], 'Two-dimensional': [792], 'structure': [793], 'domain': [797], '3,': [801], 'membrane.': [809], 'EMBO': [810], '12:': [813], '2233–2239.': [814], '22': [815], 'Walz,': [816], 'T,': [817], 'Zeidel,': [820], 'Engel,': [822], 'Biologically': [826], 'active': [827], 'two-dimensional': [828], 'crystals': [829], 'CHIP.': [832], '1994;': [836], '269:': [837], '1583–1586.': [838], '23': [839], 'Berendt,': [840], 'AR,': [841], 'McDowall,': [842], 'Craig,': [844], 'AG,': [845], 'Bates,': [846], 'PA,': [847], 'Sternberg,': [848], 'MJE,': [849], 'Marsh,': [850, 910], 'Newbold,': [852], 'CI': [853], 'Hogg,': [855], 'N:': [856], 'site': [859], 'falciporum-infected': [864], 'erythrocytes': [865], 'overlaps,': [866], 'but': [867], 'distinct': [869], 'from,': [870], 'LFA-1-binding': [872], 'site.': [873], '68:': [876], '71–81.': [877], '24': [878], 'Lewis,': [879, 979], 'Bird,': [883, 963], 'GWG,': [884, 964], 'Brodheim,': [885, 965], 'E,': [886, 966], 'Contreras,': [889], 'Crookston,': [891], 'M': [892], 'Dahr,': [894, 969], 'Daniels,': [896, 957], 'GL,': [897, 958], 'Engelfriet,': [898, 971], 'CP,': [899, 972], 'CM,': [901], 'Issitt,': [902, 973], 'PD,': [903, 974], 'Jrgensen,': [904, 975], 'Kornstad,': [906, 977], 'Lubenko,': [908, 983], 'WL,': [911], 'McCreary,': [912], 'Moore,': [914], 'BPL,': [915], 'Morel,': [916, 987], 'Moulds,': [918, 959], 'JJ,': [919, 960], 'Nevanlinna,': [920], 'H,': [921, 942], 'Nordhagen,': [922, 989], 'Okubo,': [924, 991], 'Rosenfield,': [926], 'RE,': [927], 'Rouger,': [928, 995], 'Ph,': [929, 996], 'Rubinstein,': [930], 'Salmon,': [932, 997], 'Ch,': [933, 998], 'Seidl,': [934, 999], 'S.,': [935], 'Sistonen,': [936, 1001], 'Tippett,': [938], 'Walker,': [940], 'R': [941], 'Woodfield,': [943, 1005], 'G,': [944, 1006], 'Young,': [945], 'terminology': [949, 1013], '1990.': [950], 'Sang': [952, 1020], '58:': [954], '152–169.': [955], '25': [956], 'Levene,': [981], 'Mallory,': [985], 'Reid,': [993], 'Wendel,': [1003], 'Zelinski,': [1007], 'T:': [1008], 'ISBT': [1009], 'Working': [1010], 'Party': [1011], 'antigens.': [1018], '65:': [1022], '77–80.': [1023], 'Citing': [1024], 'Literature': [1025], 'Volume67,': [1026], 'Issues3July': [1027], '1994Pages': [1028], 'ReferencesRelatedInformation': [1030]}, 'cited_by_api_url': 'https://api.openalex.org/works?filter=cites:W2076746819', 'counts_by_year': [{'year': 2019, 'cited_by_count': 1}, {'year': 2013, 'cited_by_count': 3}], 'updated_date': '2024-09-25T23:56:26.396999', 'created_date': '2016-06-24'}

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