A new member of the UDP-N-acetylglucosamine:β-galactose β1,3-N-acetylglucosaminyltransferase (β3Gn-T) family having the β3Gn-T motifs was cloned from rat and human cDNA libraries and named β3Gn-T5 based on its position in a phylogenetic tree. We concluded that β3Gn-T5 is the most feasible candidate for lactotriaosylceramide (Lc3Cer) synthase, an important enzyme which plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids. β3Gn-T5 exhibited strong activity to transfer GlcNAc to glycolipid substrates, such as lactosylceramide (LacCer) and neolactotetraosylceramide (nLc4Cer; paragloboside), resulting in the synthesis of Lc3Cer and neolactopentaosylceramide (nLc5Cer), respectively. A marked decrease in LacCer and increase in nLc4Cer was detected in Namalwa cells stably expressing β3Gn-T5. This indicated that β3Gn-T5 exerted activity to synthesize Lc3Cer and decrease LacCer, followed by conversion to nLc4Cer via endogenous galactosylation. The following four findings further supported that β3Gn-T5 is Lc3Cer synthase. 1) The β3Gn-T5 transcript levels in various cells were consistent with the activity levels of Lc3Cer synthase in those cells. 2) The β3Gn-T5 transcript was presented in various tissues and cultured cells. 3) The β3Gn-T5 expression was up-regulated by stimulation with retinoic acid and down-regulated with 12-O-tetradecanoylphorbol-13-acetate in HL-60 cells. 4) The changes in β3Gn-T5 transcript levels during the rat brain development were determined. Points 2, 3, and 4 were consistent with the Lc3Cer synthase activity reported previously. A new member of the UDP-N-acetylglucosamine:β-galactose β1,3-N-acetylglucosaminyltransferase (β3Gn-T) family having the β3Gn-T motifs was cloned from rat and human cDNA libraries and named β3Gn-T5 based on its position in a phylogenetic tree. We concluded that β3Gn-T5 is the most feasible candidate for lactotriaosylceramide (Lc3Cer) synthase, an important enzyme which plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids. β3Gn-T5 exhibited strong activity to transfer GlcNAc to glycolipid substrates, such as lactosylceramide (LacCer) and neolactotetraosylceramide (nLc4Cer; paragloboside), resulting in the synthesis of Lc3Cer and neolactopentaosylceramide (nLc5Cer), respectively. A marked decrease in LacCer and increase in nLc4Cer was detected in Namalwa cells stably expressing β3Gn-T5. This indicated that β3Gn-T5 exerted activity to synthesize Lc3Cer and decrease LacCer, followed by conversion to nLc4Cer via endogenous galactosylation. The following four findings further supported that β3Gn-T5 is Lc3Cer synthase. 1) The β3Gn-T5 transcript levels in various cells were consistent with the activity levels of Lc3Cer synthase in those cells. 2) The β3Gn-T5 transcript was presented in various tissues and cultured cells. 3) The β3Gn-T5 expression was up-regulated by stimulation with retinoic acid and down-regulated with 12-O-tetradecanoylphorbol-13-acetate in HL-60 cells. 4) The changes in β3Gn-T5 transcript levels during the rat brain development were determined. Points 2, 3, and 4 were consistent with the Lc3Cer synthase activity reported previously. UDP-GlcNAc:β-galactose β1,3-N-acetylglucosaminyltransferase UDP-galactose:β-N-acetylglucosamine β1,3-galactosyltransferase uridine diphosphate-N-acetylglucosamine monoclonal antibody base pair(s) polymerase chain reaction open reading frame high performance thin layer chromatography sulfoglucuronylglycolipid glycosphingolipid Lewis a Lewis b Lewis x stage-specific embryonal antigen-1 lactosylceramide (Galβ1–4Glcβ1–1Cer) lactotriaosylceramide (GlcNAcβ1–3Galβ1–4Glcβ1–1Cer) neolactotetraosylceramide (paragloboside: Galβ1–4GlcNAcβ1–3Galβ1–4Glcβ1–1Cer) GlcNAcβ1–3Galβ1–4GlcNAcβ1–3Galβ1–4Glcβ1–1Cer Galβ1–4GlcNAcβ1–3Galβ1–4GlcNAcβ1–3Galβ1–4Glcβ1–1Cer pyridylaminated 2-aminobenzamide lacto-N-neotetraose (Galβ1–4GlcNAcβ1–3Galβ1–4Glc) lacto-N-tetraose (Galβ1–3GlcNAcβ1–3Galβ1–4Glc) lacto-N-fucopentaose-II (Galβ1–3(Fucα1–4)GlcNAcβ1–3Galβ1–4Glc) lacto-N-fucopentaose-III (Galβ1–4(Fucα1–3)GlcNAcβ1–3Galβ1–4Glc) lacto-N-fucopentaose-V (Galβ1–3GlcNAcβ1–3Galβ1–4(Fucα1–3)Glc) lacto-N-difucohexaose-II (Galβ1–3(Fucα1–4)GlcNAcβ1–3Galβ1–4(Fucα1–3)Glc) N-acetyllactosamine (Galβ1–4GlcNAc) Galβ1–4GlcNAcβ1–3Galβ1–4GlcNAc (Galβ1–4GlcNAcβ1–3)2Galβ1–4GlcNAc (Galβ1–4GlcNAcβ1–3)3Galβ1–4GlcNAc (Galβ1–4GlcNAcβ1–3)4Galβ1–4GlcNAc retinoic acid 12-O-tetradecanoylphorbol-13-acetate reverse transcriptase-polymerase chain reaction lactosylceramide:α2,3-sialyltransferase To date, three members of the human β1,3-N-acetylglucosaminyltransferase (β3Gn-T)1 family (β3Gn-T2, -T3, and -T4) (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar, 2Zhou D. Dinter A. Gutierrez Gallego R. Kamerling J.P. Vliegenthart J.F. Berger E.G. Hennet T. Proc. Natl. Acad. Sci. U. S. A. 1999; 96 (; Correction (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 11673–11975): 406-411Crossref PubMed Scopus (87) Google Scholar) and five members of the human β1,3-galactosyltransferase (β3Gal-T) family (β3Gal-T1, -T2, -T3, -T4, and -T5) have been identified (3Sasaki, K., Sasaki, E., Kawashima, K., Hanai, N., Nishi, T., and Hasegawa, M. (1994), Japan patent 0618759 A 940705.Google Scholar, 4Amado K. Almeida R. Carneiro F. Leverly S.B. Holmes E.H. Nomoto M. Hollingsworth M.A. Hassan H. Schwientek T. Nielsen P.A. Bennett E.P. Clausen H. J. Biol. Chem. 1998; 278: 12770-12778Abstract Full Text Full Text PDF Scopus (160) Google Scholar, 5Kolbinger F. Streiff M.B. Katopodis A.G. J. Biol. Chem. 1998; 273: 433-440Abstract Full Text Full Text PDF PubMed Scopus (58) Google Scholar, 6Isshiki S. Togayachi A. Kudo T. Nishihara S. Watanabe M. Kubota T. Kitajima M. Shiraishi N. Sasaki K. Andoh T. Narimatsu H. J. Biol. Chem. 1999; 274: 12499-12507Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar). All of them share amino acid motifs (β3Gn-T motifs or β3Gal-T motifs) in three regions of the catalytic domain. The first, β3Gn-T, was cloned by an expression cloning method an antibody K. K. M. K. Nakagawa S. Sekine S. T. M. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar). enzyme is in that have the β3Gn-T motifs GlcNAc to with an resulting in the synthesis of was named K. K. M. K. Nakagawa S. Sekine S. T. M. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar). was based on with the β3Gal-T family D. Dinter A. Gutierrez Gallego R. Kamerling J.P. Vliegenthart J.F. Berger E.G. Hennet T. Proc. Natl. Acad. Sci. U. S. A. 1999; 96 (; Correction (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 11673–11975): 406-411Crossref PubMed Scopus (87) Google Scholar). We reported three -T3, and -T4, which to the β3Gn-T family (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). the cDNA of was by 2Zhou D. Dinter A. Gutierrez Gallego R. Kamerling J.P. Vliegenthart J.F. Berger E.G. Hennet T. Proc. Natl. Acad. Sci. U. S. A. 1999; 96 (; Correction (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 11673–11975): 406-411Crossref PubMed Scopus (87) Google Scholar). The of was to that of which was and reported by (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). a of four -T3, and -T4, have been to To further the enzyme in and in four were to β3Gn-T activity that the synthesis of β3Gal-T The monoclonal antibody to a carbohydrate which is in in and in named sulfoglucuronylglycolipid and and PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar). have in a of that the as a during the development of the brain to the 1998; PubMed Scopus Google Scholar, N. J. PubMed Scopus Google Scholar, J. PubMed Scopus Google Scholar, S. 1998; PubMed Scopus Google Scholar, J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus Google Scholar). The expression is and in the rat in a with the and the PubMed Scopus Google Scholar). the rat the expression of is N. J. PubMed Scopus Google Scholar, S. J. PubMed Scopus Google Scholar). in cells during the development of the and for J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, S. J. PubMed Scopus Google Scholar, J. PubMed Scopus Google Scholar). rat the expression of and and by chains on by by S. J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. PubMed Scopus Google Scholar) reported changes in the activity of enzyme in with the expression in rat was that Lc3Cer synthase, which the transfer of GlcNAc to the of lactosylceramide with a resulting in the synthesis of Lc3Cer is the key enzyme in the expression of in the rat the activity of synthase was with the in The expression of the Lewis x carbohydrate is and in the brain A. Biol. 1999; PubMed Scopus Google Scholar, J. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, Y. J. PubMed Scopus Google Scholar, R. J. 1999; PubMed Scopus Google Scholar, S. S. 1999; PubMed Scopus Google Scholar, A. J. T. J. PubMed Scopus Google Scholar, 1998; PubMed Scopus Google Scholar, A. J. Google Scholar). The as a in the of the 1998; PubMed Scopus Google Scholar, M. A. S. A. J. Full Text Full Text PDF PubMed Scopus Google Scholar, J. K. 1999; PubMed Scopus Google Scholar). The expression on in brain is by the Lc3Cer synthase which a of the the S. J. PubMed Scopus Google Scholar). and the of in of Lc3Cer synthase is an important enzyme with to M. A. K. J. A. N. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar). HL-60 a human of a or M. A. K. J. A. N. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar). The Lc3Cer synthase and synthase which share the lactosylceramide key in the of in the the of HL-60 cells by 12-O-tetradecanoylphorbol-13-acetate was by of synthase and of Lc3Cer synthase. during the of HL-60 cells by acid neolacto-series were by of Lc3Cer synthase. and PubMed Scopus Google Scholar) concluded that cells exhibited β3Gn-T activity substrates, to the expression of of in the cells exhibited activity for The of Lc3Cer activity in cells the of Lc3Cer synthase is the enzyme the expression of neolacto-series and plays important in cells. the cloned and a member of the β3Gn-T family and identified β3Gn-T5 as the most candidate for Lc3Cer synthase. The were cultured in with The were or from Japan or which to nLc4Cer and PubMed Scopus Google Scholar, J. S. J. Biol. Chem. Full Text PDF PubMed Google were for and respectively. The cells were cultured in with The of was for The of cells was by We a rat cDNA for a the a rat cDNA a of β3Gn-T5. This the the β3Gal-T (β3Gn-T) motifs which by the and The cDNA of cells in a S. Togayachi A. Kudo T. Nishihara S. Watanabe M. Kubota T. Kitajima M. Shiraishi N. Sasaki K. Andoh T. Narimatsu H. J. Biol. Chem. 1999; 274: 12499-12507Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar) was with the rat β3Gn-T5 cDNA as a to the human β3Gn-T5 cDNA which a We a rat β3Gn-T5 in The the method for of was in in S. Togayachi A. Kudo T. Nishihara S. Watanabe M. Kubota T. Kitajima M. Shiraishi N. Sasaki K. Andoh T. Narimatsu H. J. Biol. Chem. 1999; 274: 12499-12507Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar, T. Y. Togayachi A. K. Watanabe M. M. Nishihara S. Narimatsu H. 1998; Google Scholar). of various human tissues were of various were and in to the of the for three cloned β3Gn-T -T3, and -T4, the and the were reported (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). the β3Gn-T5 a was by a cDNA a A a base the of the β3Gn-T5 cDNA was as The was with and was with This was followed by of the to the of the β3Gn-T5 by the following and reverse of in was in in a of S. Togayachi A. Kudo T. Nishihara S. Watanabe M. Kubota T. Kitajima M. Shiraishi N. Sasaki K. Andoh T. Narimatsu H. J. Biol. Chem. 1999; 274: 12499-12507Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar, K. K. M. K. Nakagawa S. Sekine S. T. M. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar, K. Watanabe K. Sekine S. T. M. N. T. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar, K. K. N. N. S. N. S. T. J. Biol. Chem. Full Text PDF PubMed Google Scholar, K. K. K. M. Watanabe S. N. T. J. Biol. Chem. Full Text PDF PubMed Google Scholar, T. Y. Togayachi A. M. T. Sasaki K. Narimatsu H. J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus Google Scholar). The of with of three cloned β3Gn-T -T3, and -T4, was reported (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). the β3Gn-T5 was from the β3Gn-T5 in and with The was with and of of the a was by Namalwa cells. cells were in the of a of cells were to The levels of the in the Namalwa cells were by of glycolipid of the Namalwa cells with were with and were from the cells. were from the with and with with the were in to in for and with the been with the were with the and to The glycolipid were with the and to glycolipid to cells was to of were by with of and was with the antibody as PubMed Scopus Google Scholar). The catalytic of of -T3, been as a with in cells as in a (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). the a a of β3Gn-T5 to was by The was with to the The and were and to the were as and reverse The was the and of the the was by and and was the and of to is an expression from and a the of human and We as (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). cells were with a of of and for to β3Gn-T with were by antibody and with 4 The in were named and by were to an The was with monoclonal and with the The of on was by A. Kudo T. Y. H. Nishihara S. Andoh T. M. K. S. Narimatsu H. J. 1999; PubMed Scopus Google Scholar) to the of of β3Gn-T, the enzyme in the and the in the of Namalwa cells and cultured were to the of β3Gn-T various was to the as and for the The various cultured cells were in a and of in the was for the enzyme were with 2-aminobenzamide or pyridylaminated (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar, S. H. M. A. M. Narimatsu H. 1999; PubMed Scopus Google Scholar) and for The β3Gn-T activity was in a reaction or and the enzyme for the reaction was by for and the was with of for the was an A of was to high performance chromatography on a The reaction were with a of and with a (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar, S. H. M. A. M. Narimatsu H. 1999; PubMed Scopus Google Scholar). We an of the of glycolipid The β3Gn-T activity for was in a reaction of of glycolipid and the enzyme for the reaction was by for and of was The reaction was for glycolipid were from the a a was with of and with of The of the reaction was on the of the was of were with and the were in an of The were on a with a of The of the were with a HL-60 cells were an of and with or M. A. K. J. A. N. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar). various the of the the cells were and the in the cells was for of were and and the from was to was from a of rat of and was for cDNA The cDNA the of rat β3Gn-T5 was as a from which a was by of a A a and a reverse was for the The was on A cDNA β3Gn-T motifs was during the of a rat cDNA We cloned a human cDNA to the rat cDNA and named β3Gn-T5. The amino acid in the human and rat was This indicated that the The human β3Gn-T5 cDNA a a of amino as in β3Gn-T5 is to a of a of a of and a and catalytic of β3Gn-T5 the three motifs of members of the β3Gal-T and β3Gn-T four were to in the four which that of for of the of the β3Gn-T a of acid which a as in a of Y. J. 1999; PubMed Scopus Google was were in the of β3Gn-T5. of them was in was to to a and the cDNA the is of a a phylogenetic the four members of the β3Gn-T family a which is from β3Gal-T β3Gn-T5 is in the β3Gn-T family is in an from the of the -T3, and -T4, a in the phylogenetic and and a The of β3Gn-T5 that of β3Gn-T in and was in tissues and with the expression was on the and The tissues a high were and and a and and and the β3Gn-T5 a high All cells for and the β3Gn-T5 transcript a high the cells from for an and HL-60 cells a cells The expression levels in the cultured cells those in the tissues of β3Gn-T in various human by of β3Gn-T transcript in a new The of four -T3, -T4, and as with a in the were named and respectively. The of enzyme were for the β3Gn-T We activity of the four and The β3Gn-T activity of was of the enzyme and the the activity of is presented as and as exhibited activity the following pyridylaminated and and exhibited activity or exhibited activity and and exhibited activity or exhibited activity and exhibited activity or exhibited activity pyridylaminated substrates, and exhibited activity or The β3Gn-T activity of was the activity of The three and exhibited activity for and and exhibited activity for and as for activity was for a activity for a that and exhibited levels of β3Gn-T activity and an of enzyme for the reaction (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). The having the of of were with and as S. H. M. A. M. Narimatsu H. 1999; PubMed Scopus Google Scholar). The was as a and in that or respectively. The β3Gn-T activity of was the of enzyme and its activity is as and the of the to in a GlcNAc with the of activity to of the of exhibited activity for of The activity of was detected with the of in the the and The of for the and were of those for the activity of in the activity in a new To the glycolipid were the of Namalwa cells stably expressing were as a of to of β3Gn-T activity in Namalwa the transcript of in Namalwa The Namalwa cells of the -T4, and The of transcript in cells with the or β3Gn-T5 were and respectively. The of transcript in cells with the was as as that in Namalwa cells. We HL-60 cells as a for HL-60 of β3Gn-T and transcript of and in the of cells exhibited strong activity for the synthesis of Lc3Cer and The of HL-60 cells LacCer and were by of the in The activity of LacCer is presented as and as exhibited strong activity LacCer resulting in the synthesis of Lc3Cer the three activity The Namalwa cells and the Namalwa cells and for the synthesis of The cells an increase in the transcript for the was in the cells. were and respectively. exhibited strong activity The activity of for synthesis was the as that for Lc3Cer the of the four three of -T3, and -T4, were the in the (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar) glycolipid was in in the activity of LacCer is presented as exhibited strong LacCer and nLc4Cer in with the nLc4Cer LacCer as an and GlcNAc to nLc4Cer to as an exhibited activity activity activity the glycolipid activity of in the glycolipid activity in a new from the of of the of LacCer of as with that of the the were detected in the and cells. the nLc4Cer of cells a strong as with that of the The detected that of nLc4Cer of cells to is that with and J. S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). The as The β3Gn-T5 in the cells the LacCer, and the Lc3Cer was by endogenous to Namalwa cells to an of of the nLc4Cer in the cells was further to by the β3Gn-T5 and to by endogenous The Lc3Cer activity was in cells various cultured cells in the activity of was as and the for Lc3Cer activity of the cells were to The of Lc3Cer activity was with the of β3Gn-T5 transcript is with the levels of the β3Gn-T of cells the most followed by and cells in for activity and the of cells an which exhibited the high expression of β3Gn-T5 We the Lc3Cer activity of cells with the of β3Gn-T5 and the β3Gn-T5 and exhibited activity of Lc3Cer of Lc3Cer synthase activity with the transcript of β3Gn-T5 in various activity for Lc3Cer of β3Gn-T transcript in a new the activity transcript cells. cells of exhibited activity of Lc3Cer synthase. was a or in The indicated that the Lc3Cer activity is by β3Gn-T5 in in the expression of transcript during the by in to that of the HL-60 the during the by in in the rat the expression of transcript and by The β3Gn-T5 changes in the transcript The of β3Gn-T5 transcript from to and the the the expression was Lc3Cer synthase plays a key role in the of carbohydrate synthesis in during and in the -T3, and the Lc3Cer synthase. We of the of the transcript levels of in various were with the Lc3Cer and in the as a candidate for the Lc3Cer synthase. We concluded that β3Gn-T5 is the most feasible candidate for the following 1) and the of cells exhibited strong activity to synthesize Lc3Cer in 2) LacCer was to to neolacto-series in the cells. 3) The transcript levels of β3Gn-T5 in various tissues and were consistent with the Lc3Cer activity as reported previously. 4) The expression of the β3Gn-T5 transcript in various cultured cells was with the Lc3Cer The changes in transcript during HL-60 and during rat brain development were consistent with those of the Lc3Cer activity as reported by PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, M. A. K. J. A. N. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The enzyme in the cells nLc4Cer which a carbohydrate chain LacCer, the exhibited the activity The in activity the to or the of in the reaction the to the by the domain. We that the which is to the of with a carbohydrate which with carbohydrate The in Namalwa cells activity the the reaction for β3Gn-T the as a the is that the enzyme the with glycolipid Lc3Cer synthase been detected in the rat brain J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google cells M. A. K. J. A. N. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar, PubMed Scopus Google Scholar, S. M. T. J. PubMed Scopus Google Scholar, M. S. J. Biol. Chem. Full Text PDF PubMed Google Scholar, F. J.P. J. Biol. Chem. Full Text PDF PubMed Google and tissues E.H. PubMed Scopus Google Scholar, E.H. S. J. Biol. Chem. Full Text PDF PubMed Google Scholar, M. PubMed Scopus Google Scholar). tissues the Lc3Cer synthase was identified to a key enzyme in the of the carbohydrate chain on neolacto-series The of cells exhibited strong activity for substrates, LacCer and as as and the and This indicated that β3Gn-T5 a of The marked in the β3Gn-T5 activity for the chain that with a such as for β3Gn-T5. PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google the activity of β3Gn-T LacCer and nLc4Cer was of rat brain during of during the the This consistent with the that the by a β3Gn-T5. The and Namalwa cells β3Gn-T activity for activity for We which enzyme activity in the Namalwa cells. The activity by endogenous or in the Namalwa cells. The Lc3Cer synthase is a key enzyme in the expression of a of nLc4Cer and its the expression of and the is by the Lc3Cer synthase PubMed Scopus Google Scholar, S. J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. PubMed Scopus Google Scholar, J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The in the of β3Gn-T5 transcript in rat brain that in Lc3Cer activity reported PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar, J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). This indicated that β3Gn-T5 is the Lc3Cer synthase. To or β3Gn-T5 is with on and on neolacto-series in a Lc3Cer synthase is an important enzyme in The changes in the transcript during HL-60 in consistent with the of M. A. K. J. A. N. M. J. Biol. Chem. Full Text PDF PubMed Google Scholar). PubMed Scopus Google Scholar) reported that Lc3Cer in or levels of β3Gn-T5 HL-60 cells and cells of β3Gn-T5. This supported that β3Gn-T5 is for the synthesis of Lc3Cer in cells. Holmes E.H. PubMed Scopus Google Scholar) reported the β3Gn-T for the synthesis of in the cells of a human The the of β3Gn-T activity LacCer and This to that were by a as in the of rat the that β3Gn-T5 the of Lc3Cer and the is M. PubMed Scopus Google Scholar) a Lc3Cer and in on the M. PubMed Scopus Google to in which the synthesis of Lc3Cer or with the to the by Holmes E.H. S. J. Biol. Chem. Full Text PDF PubMed Google Scholar) in which high activity of Lc3Cer synthase was detected in tissues of and in the activity was in cells. the of β3Gn-T5 This is consistent with the of Holmes E.H. S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). of the We or the β3Gn-T up-regulated in the tissues of the in was most and the chain on the chain is the most candidate for the enzyme which to the β3Gn-T5 is in the synthesis of chains or of and exhibited β3Gn-T activity in a (1Shiraishi N. Natsume A. Togayachi A. Endo T. Akashima T. Yamada Y. Imai N. Nakagawa S. Koizumi S. Sekine S. Narimatsu H. Sasaki K. J. Biol. Chem. 2001; 276: 3498-3507Abstract Full Text Full Text PDF PubMed Scopus (118) Google of enzyme were for the The for and from the and for and The β3Gn-T (β3Gal-T) family is with and having been cloned and to The that as Lc3Cer synthase The of the indicated that β3Gn-T5 is the most feasible candidate for Lc3Cer synthase. the the of synthase, the key enzyme the expression of on We of for with We Nakagawa and for and respectively.
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Togayachi et al. (2001) studied this question.
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