{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T13:12:59Z","timestamp":1790860379726,"version":"4.1.0"},"reference-count":45,"publisher":"National Academy of Sciences","issue":"26","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1997,12,23]]},"abstract":"<jats:p>\n                    The structure and biosynthesis of poly-\n                    <jats:italic>N<\/jats:italic>\n                    -acetyllactosamine display a dramatic change during development and oncogenesis. Poly-\n                    <jats:italic>N<\/jats:italic>\n                    -acetyllactosamines are also modified by various carbohydrate residues, forming functional oligosaccharides such as sialyl Le\n                    <jats:sup>x<\/jats:sup>\n                    . Herein we describe the isolation and functional expression of a cDNA encoding \u03b2-1,3-\n                    <jats:italic>N<\/jats:italic>\n                    -acetylglucosaminyltransferase (iGnT), an enzyme that is essential for the formation of poly-\n                    <jats:italic>N<\/jats:italic>\n                    -acetyllactosamine. For this expression cloning, Burkitt lymphoma Namalwa KJM-1 cells were transfected with cDNA libraries derived from human melanoma and colon carcinoma cells. Transfected Namalwa cells overexpressing the i antigen were continuously selected by fluorescence-activated cell sorting because introduced plasmids containing Epstein\u2013Barr virus replication origin can be continuously amplified as episomes. Sibling selection of plasmids recovered after the third consecutive sorting resulted in a cDNA clone that directs the increased expression of i antigen on the cell surface. The deduced amino acid sequence indicates that this protein has a type II membrane protein topology found in almost all mammalian glycosyltransferases cloned to date. iGnT, however, differs in having the longest transmembrane domain among glycosyltransferases cloned so far. The iGnT transcript is highly expressed in fetal brain and kidney and adult brain but expressed ubiquitously in various adult tissues. The expression of the presumed catalytic domain as a fusion protein with the IgG binding domain of protein A enabled us to demonstrate that the cDNA encodes iGnT, the enzyme responsible for the formation of GlcNAc\u03b21\u2009\u2192\u20093Gal\u03b21\u2009\u2192\u20094GlcNAc\u2009\u2192\u2009R structure and poly-\n                    <jats:italic>N<\/jats:italic>\n                    -acetyllactosamine extension.\n                  <\/jats:p>","DOI":"10.1073\/pnas.94.26.14294","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:31:39Z","timestamp":1027679499000},"page":"14294-14299","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":134,"title":["Expression cloning of cDNA encoding a human \u03b2-1,3-\n                    <i>N<\/i>\n                    -acetylglucosaminyltransferase that is essential for\u2009poly-\n                    <i>N<\/i>\n                    -acetyllactosamine\u2009synthesis"],"prefix":"10.1073","volume":"94","author":[{"given":"Katsutoshi","family":"Sasaki","sequence":"first","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazumi","family":"Kurata-Miura","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minoru","family":"Ujita","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiyohiko","family":"Angata","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Satoshi","family":"Nakagawa","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susumu","family":"Sekine","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatsunari","family":"Nishi","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minoru","family":"Fukuda","sequence":"additional","affiliation":[{"name":"Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan; and Glycobiology Program, The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1997,12,23]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4684-7464-0_4"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/314053a0"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-230X(08)60215-8"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)50640-2"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)50747-X"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.7326\/0003-4819-44-2-221"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.149.4.975"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)50685-8"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)90706-4"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)44173-1"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1987.tb13502.x"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.7.3.468"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)37777-9"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)74225-2"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)90602-2"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(90)90444-J"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1701274"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1701275"},{"key":"e_1_3_3_19_2","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1093\/oso\/9780199633876.003.0004","volume-title":"Molecular Glycobiology","author":"Lowe B J","year":"1994","unstructured":"B J Lowe Molecular Glycobiology, eds M Fukuda, O Hindsgaul (Oxford Univ. 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