{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,2,20]],"date-time":"2024-02-20T17:04:44Z","timestamp":1708448684616},"reference-count":43,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2013,11,13]],"date-time":"2013-11-13T00:00:00Z","timestamp":1384300800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Xenotransplantation"],"published-print":{"date-parts":[[2014,1]]},"abstract":"Abstract<\/jats:title>Background<\/jats:title>The human H\u2010transferase (\u03b12FucT) was introduced in Gal\u2010negative pigs to produce pig organs not only free from Gal\u2010antigens, but also in which the uncapped N\u2010acetyllactosamine precursor had been transformed into non\u2010xenogenic blood group H type 2 compounds. This work is the first descriptive analysis of glycolipids from the GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> pig. The aim was to investigate the cell membrane antigens in GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> tissues to explore its efficacy as an organ donor. Also, detailed knowledge on the correlation between the cellular glycosyltransferase configuration and the resulting carbohydrate phenotype expression is valuable from a basic glycobiological perspective.<\/jats:p><\/jats:sec>Methods<\/jats:title>Neutral and acidic glycolipids from GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> small intestine were compared with glycolipids from two wildtype and two GalT\u2010KO<\/jats:styled-content> pig intestines. Glycolipid reactivity was tested on thin layer chromatography plates using chemical reagents, antibodies, lectins, and human serum. Structural characterization of neutral glycolipids was performed by LC<\/jats:styled-content>\u2010ESI<\/jats:styled-content>\/MS<\/jats:styled-content> and proton NMR<\/jats:styled-content> spectroscopy.<\/jats:p><\/jats:sec>Results<\/jats:title>Characterization of the glycolipid expression in GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> intestine showed absence of Gal antigens and decreased\/unchanged levels of the N\u2010acetyllactosamine precursor and the blood group H type 2 expression, when compared with the wildtype. The reactivity of human serum antibodies to GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> derived glycolipids was similar or slightly elevated when compared with GalT\u2010KO<\/jats:styled-content> glycolipids. Results from LC<\/jats:styled-content>\u2010ESI<\/jats:styled-content>\/MS<\/jats:styled-content> and proton NMR<\/jats:styled-content> spectroscopy revealed no established neutral xenogenic antigens in the GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> pig, and could thus not explain the immunologic reactivity to human serum antibodies. The antibody binding to acidic glycolipids is most likely to be explained by the abundance of N\u2010glycolylneuraminic acid epitopes in pig tissues. Six neutral complex biantennary glycolipids with blood group H type 1, 2, Lewisx<\/jats:sup> and Lewisy<\/jats:sup> determinants were found, of which three were identified in this work for the first time. One of these was a nonaglycosylceramide with blood group H type 2 and lactosyl determinants linked to a lactotetraosyl core, and the other two were decaglycosylceramides with blood group H type 1 and H type 2 determinants linked to a neolactotetraosyl core, and Lewisx<\/jats:sup> and blood group H type 1 determinants on a lactotetraosyl core, respectively.<\/jats:p><\/jats:sec>Conclusions<\/jats:title>Lipid\u2010linked carbohydrate antigens in the GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> pig intestine showed no or minor qualitative difference when compared with GalT\u2010KO<\/jats:styled-content> pigs. The GalT\u2010KO<\/jats:styled-content>\/FucT\u2010TG<\/jats:styled-content> pig did not appear to have an advantage over the GalT\u2010KO<\/jats:styled-content> pig with respect to reactivity with human antibodies from a xenotransplantation perspective.<\/jats:p><\/jats:sec>","DOI":"10.1111\/xen.12071","type":"journal-article","created":{"date-parts":[[2013,11,13]],"date-time":"2013-11-13T11:06:43Z","timestamp":1384340803000},"page":"57-71","source":"Crossref","is-referenced-by-count":4,"title":["The alpha1,3GalT knockout\/alpha1,2FucT transgenic pig does not appear to have an advantage over the alpha1,3GalT knockout pig with respect to glycolipid reactivity with human serum antibodies"],"prefix":"10.1111","volume":"21","author":[{"given":"Mette","family":"Diswall","sequence":"first","affiliation":[{"name":"Department of Surgery Institute of Clinical Sciences Sahlgrenska Academy\/Gothenburg University Gothenburg Sweden"},{"name":"Department of Clinical Chemistry and Transfusion Medicine Institute of Biomedicine Sahlgrenska Academy at University of Gothenburg Gothenburg Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John","family":"Benktander","sequence":"additional","affiliation":[{"name":"Department of Medical Biochemistry and Cell Biology Institute of Biomedicine University of Gothenburg Gothenburg Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonas","family":"\u00c5ngstr\u00f6m","sequence":"additional","affiliation":[{"name":"Department of Medical Biochemistry and Cell Biology Institute of Biomedicine University of Gothenburg Gothenburg Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Susann","family":"Teneberg","sequence":"additional","affiliation":[{"name":"Department of Medical Biochemistry and Cell Biology Institute of Biomedicine University of Gothenburg Gothenburg Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael E.","family":"Breimer","sequence":"additional","affiliation":[{"name":"Department of Surgery Institute of Clinical Sciences Sahlgrenska Academy\/Gothenburg University Gothenburg Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2013,11,13]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0307819101"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1078942"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/nbt0302-251"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1068228"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-3089.2006.00368.x"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/nm1172"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1038\/nm1171"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1097\/01.TP.0000130487.68051.EB"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-3089.2009.00564.x"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1097\/01.tp.0000287599.46165.15"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.transproceed.2008.01.032"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.13.13.1762"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1034\/j.1399-3089.2002.0o142.x"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1096\/fj.02-0630fje"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.transproceed.2007.12.025"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1095\/biolreprod.102.014647"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a123530"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(87)38018-8"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1471-4159.1963.tb08933.x"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-3089.1998.tb00017.x"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/2.6.529"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-3089.2004.00192.x"},{"key":"e_1_2_7_24_1","doi-asserted-by":"crossref","first-page":"8554","DOI":"10.1016\/S0021-9258(17)37231-9","article-title":"Characterization of binding of Gal beta 4GlcNAc\u2010specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk","volume":"269","author":"Teneberg S","year":"1994","journal-title":"J Biol Chem"},{"key":"e_1_2_7_25_1","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1016\/S0021-9258(19)40169-5","article-title":"Isolation to homogeneity and partial characterization of a histo\u2010blood group A defined Fuc alpha 1\u20132Gal alpha 1\u20133\u2010N\u2010acetylgalactosaminyltransferase from human lung tissue","volume":"265","author":"Clausen H","year":"1990","journal-title":"J Biol Chem"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)68541-8"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1292\/jvms.56.375"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-1345(98)01847-8"},{"key":"e_1_2_7_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)60561-7"},{"key":"e_1_2_7_30_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwq070"},{"key":"e_1_2_7_31_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwh003"},{"key":"e_1_2_7_32_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/7.7.943"},{"key":"e_1_2_7_33_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/8.6.533"},{"key":"e_1_2_7_34_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10719-008-9125-9"},{"key":"e_1_2_7_35_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00335a028"},{"key":"e_1_2_7_36_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M112.387654"},{"key":"e_1_2_7_37_1","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-137-7-1591"},{"key":"e_1_2_7_38_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(90)80693-D"},{"key":"e_1_2_7_39_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwn125"},{"key":"e_1_2_7_40_1","doi-asserted-by":"publisher","DOI":"10.1002\/ajpa.10018"},{"key":"e_1_2_7_41_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20090835"},{"key":"e_1_2_7_42_1","doi-asserted-by":"publisher","DOI":"10.1111\/xen.12019"},{"key":"e_1_2_7_43_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-2277.2008.00736.x"},{"key":"e_1_2_7_44_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.transproceed.2011.09.024"}],"container-title":["Xenotransplantation"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1111%2Fxen.12071","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/xen.12071","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T11:27:20Z","timestamp":1696159640000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/xen.12071"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,11,13]]},"references-count":43,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2014,1]]}},"alternative-id":["10.1111\/xen.12071"],"URL":"https:\/\/doi.org\/10.1111\/xen.12071","archive":["Portico"],"relation":{},"ISSN":["0908-665X","1399-3089"],"issn-type":[{"value":"0908-665X","type":"print"},{"value":"1399-3089","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,11,13]]}}}