ライフサイエンスコーパス: N-acetyllactosamine

1 s with increased branching and extended poly-N-acetyllactosamine.

2 not require DD-heptose to form the terminal N-acetyllactosamine.

3 opically labeled CMP-N-acetylneuraminate and N-acetyllactosamine.

4 ic pathway leading to the addition of sialyl-N-acetyllactosamine.

5 ty to bacterial glycans that lack lactose or N-acetyllactosamine.

6 conformational behavior and lipophilicity of N-acetyllactosamine.

7 ipooligosaccharide (LOS) which terminates in N-acetyllactosamine.

8 sulfate (KS) is a sulfated linear polymer of N-acetyllactosamine.

9 recognizes poly-N-acetylglucosamine and poly-N-acetyllactosamine.

10 ding a galactose to linear and branched poly-N-acetyllactosamines.

11 ently add N-acetyllactosamine to linear poly-N-acetyllactosamines.

12 -3GalNAc termini, and some increases in poly-N-acetyllactosamines.

13 ther beta-Xyl or chains of, on average, five N-acetyllactosamine (-3Galbeta1-4GlcNAcbeta1-) (LacNAc)

14 ntain primarily complex-type structures with N-acetyllactosamine, a preferred galectin ligand.

15 s for lactose, lactulose, lacto-N-biose, and N-acetyllactosamine, all of which exhibit binding enthal

16 methyl beta-galactopyranoside, lactose, and N-acetyllactosamine and a greater -delta H value for the

17 three other H. ducreyi strains also contain N-acetyllactosamine and are highly sialylated (approxima

18 o-MM factor, NGFR, implicating i-linear poly-N-acetyllactosamine and Gal-8 as biomarkers and therapeu

19 ng the MM glycome by enforcing i-linear poly-N-acetyllactosamine and Gal-8 expression.

20 its desulfated form, as well as di-, tetra- (N-acetyllactosamine and lacto-N-tetraose) and octasaccha

21 h sequence and linkage data are obtained for N-acetyllactosamine and sialyl-N-acetyllactosamine oligo

22 0 have been previously found to terminate in N-acetyllactosamine and sialyl-N-acetyllactosamine, Neu5

23 ated that itraconazole globally reduced poly-N-acetyllactosamine and tetra-antennary complex N-glycan

24 eyi contain terminal sialic acid attached to N-acetyllactosamine and that this modification is likely

25 rabinose, 2'-O-methyllactose, lacto-N-biose, N-acetyllactosamine, and thiodigalactopyranoside.

26 cans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines, and on alpha(2)-HS-glycoprotein.

27 Complex glycan structural features, such as N-acetyllactosamine antenane, neuraminic acids, and nonr

28 Poly-N-acetyllactosamines are attached to N-glycans, O-glycan

29 ases, which play important roles in how poly-N-acetyllactosamines are synthesized in different accept

30 beled UMP-NeuAc's as the donor substrate and N-acetyllactosamine as the acceptor.

31 at 297.8 K to 6.54 +/- 0.97 x 10(4) M-1 for N-acetyllactosamine at 281.3 K.

32 blood group H on a 6-linked branch of a poly-N-acetyllactosamine backbone.

33 e of galectin-3 (GaL3), a multicompartmented N-acetyllactosamine-binding chimeric lectin, on atheroge

34 that 4-F-GlcNAc (putative inhibitor of poly-N-acetyllactosamine biosynthesis) was more potent than B

35 amine (4-F-GlcNAc), a metabolic inhibitor of N-acetyllactosamine biosynthesis, and analyzed tumor gro

36 osamine is a unique carbohydrate composed of N-acetyllactosamine branches attached to linear poly-N-a

37 N-Acetyllactosamine, but not sucrose, treatment of cells

38 I-branched poly-N-acetyllactosamine can carry bivalent functional oligos

39 lts also showed that monosialyl and disialyl N-acetyllactosamines can serve equally as an acceptor, s

40 s with IGHV4-34*01 heavy chains bind to poly-N-acetyllactosamine carbohydrates (I/i antigen) on eryth

41 syl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manalpha1-3 arm

42 -3 arm may carry predominantly branched poly-N-acetyllactosamine chains.

43 NAc preferentially to galactosyl residues of N-acetyllactosamine close to nonreducing terminals.

44 y crystallographic structure of the galectin-N-acetyllactosamine complex determined by Liao et al.

45 Both glycoproteins display poly-N-acetyllactosamines, consistent with virion assembly in

46 of sialylated glycoforms but a reduction in N-acetyllactosamine containing glycoforms.

47 lyltransferases, SiaA, and LsgB, that affect N-acetyllactosamine containing glycoforms.

48 se-linked glycan structures, including sulfo-N-acetyllactosamine containing modifications.

49 Characterization of the large poly-N-acetyllactosamine containing N-glycans of the TbGnTII

50 TbGT8 influences the processing of the poly N-acetyllactosamine-containing asparagine-linked glycans

51 cterized to demonstrate that they produced a N-acetyllactosamine-containing LOS by silver-stained sod

52 tants that were unable to add sialic acid to N-acetyllactosamine-containing LOS.

53 lly recognize a triantennary sialylated poly-N-acetyllactosamine-containing N-glycan exposed on the h

54 ans, including some exceptionally large poly-N-acetyllactosamine-containing structures.

55 side GD1a and oligosaccharides containing an N-acetyllactosamine core.

56 ing from a single chemically synthesized tri-N-acetyllactosamine derivative.

57 A range of N-acetyllactosamine derivatives (compounds 4-7) that hav

58 nt classes of complex glycans including poly-N-acetyllactosamine derivatives, human milk oligosacchar

59 of CD45, and more specifically, an N-linked N-acetyllactosamine determinant preferentially expressed

60 ate carbohydrate chains consist of repeating N-acetyllactosamine disaccharides with sulfation on the

61 cells, indicating direct inhibition on poly-N-acetyllactosamine elongation and selectin-binding dete

62 complete loss of sialylation of the terminal N-acetyllactosamine epitope and expression of the higher

63 ll glomeruli-specific N-glycans contained an N-acetyllactosamine epitope.

64 had no effect on sialylation of the terminal N-acetyllactosamine epitope.

65 ncement of both beta(1,6) branching and poly-N-acetyllactosamine expression on N-cadherin.

66 N-acetyllactosamine synthesis, allowing poly-N-acetyllactosamine extension mostly along the linear po

67 Poly-N-acetyllactosamine extension of core 4 branches is, how

68 In O-glycan biosynthesis, N-acetyllactosamine extension of core 4 branches was fou

69 jor product was the oligosaccharide with one N-acetyllactosamine extension on the linear Galbeta1-->4

70 ct contained galactosylated I-branch without N-acetyllactosamine extension.

71 opy compensation, and, with the exception of N-acetyllactosamine, follow a van't Hoff dependence of t

72 ed by the addition of beta1,3-linked GlcA to N-acetyllactosamine followed by sulfation of the C-3 pos

73 branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranc

74 group consists of Neu5Acalpha2-3(lactose or N-acetyllactosamine) forms that lack the branched mannos

75 -sialyltransferases for the common substrate N-acetyllactosamine (Gal(beta)1-4GlcNAc-R) on N-linked c

76 lated derivatives of the glycan structure B4-N-acetyllactosamine (GalB1,4GlcNAc or type-2 LacNAc, her

77 fated glycans, in particular sulfated type 2 N-acetyllactosamine (GalB1-4GalNAcB), which is found on

78 timal configuration of sulfate esters on the N-acetyllactosamine (Galbeta1-->4GlcNAc) core of sulfosi

79 hyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported.

80 possess essentially the same affinities for N-acetyllactosamine; however, the animal lectin shows a

81 ialylated, triantennary oligosaccharide with N-acetyllactosamine (i.e. Galbeta1,4GlcNAc-) or lacto-N-

82 ansferases and fucosyltransferases recognize N-acetyllactosamine in a different conformation.

83 a for 4-6 showed that each enzyme recognizes N-acetyllactosamine in a low minimum energy conformation

84 T-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans.

85 ransferase, was capable of synthesizing poly-N-acetyllactosamine in core 2 branched oligosaccharides.

86 demonstrate the importance of Gal-1-binding N-acetyllactosamines in controlling the fate and functio

87 consistent with previous findings that poly-N-acetyllactosamines in human erythrocytes, PA-1 embryon

88 Poly-N-acetyllactosamines in mucin-type O-glycans can be form

89 the present study, we first found that poly-N-acetyllactosamines in N-glycans are most efficiently s

90 e presence of core 1 O-glycans, but not poly-N-acetyllactosamine, in apically targeted MUC1 and chime

91 N-Acetyllactosamine is a common saccharide motif found i

92 I-branched poly-N-acetyllactosamine is a unique carbohydrate composed of

93 Poly-N-acetyllactosamine is a unique carbohydrate composed of

94 Poly-N-acetyllactosamine is a unique carbohydrate that can ca

95 It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they

96 N-acetyllactosamine is the most prevalent disaccharide m

97 gh mannose glycans, complex glycans with 2-4 N-Acetyllactosamine (LacNAc) antennae, and Poly-LacNAc g

98 an galectin-3 with its native natural ligand N-acetyllactosamine (LacNAc) at atomic precision.

99 It is based on the enzymatic assembly of N-acetyllactosamine (LacNAc) backbones as thioglycosides

100 tive manner, sulfates and fucosides on oligo-N-acetyllactosamine (LacNAc) chains to provide any struc

101 enous lectin that recognizes glycans bearing N-acetyllactosamine (LacNAc) epitopes, induces branching

102 ces (Galbeta1-4GlcNAc)(n) when compared with N-acetyllactosamine (LacNAc) glycans (Galbeta1-4GlcNAc).

103 The N-acetyllactosamine (LacNAc) repeat modules were synthes

104 TfR binds tomato lectin (TL), specific for N-acetyllactosamine (LacNAc) repeats, and previous studi

105 Galectins bind N-acetyllactosamine (LacNAc) units within N-glycans init

106 lycan that has N-acetylglucosamine (GlcNAc), N-acetyllactosamine (LacNAc), and unnatural Galalpha(1,4

107 anti-skin inflammatory activity by ablating N-acetyllactosamine (LacNAc), sialyl Lewis X (sLe(X)), a

108 re that sialylated glycosphingolipids with 5 N-acetyllactosamine (LacNAc, Galbeta1-4GlcNAcbeta1-3) re

109 ere used to map the binding site of sulfated N-acetyllactosamine (LacNAc; previously shown to bind AA

110 bilized extended glycans containing terminal N-acetyllactosamine (LN; Galbeta1-4GlcNAc) sequences on

111 est that metabolic lowering of Gal-1-binding N-acetyllactosamines may attenuate tumor growth by boost

112 zyme is responsible for the synthesis of the N-acetyllactosamine moiety.

113 h transfers a galactose molecule to terminal N-acetyllactosamine (N-lac) present on various glycoprot

114 terminate in N-acetyllactosamine and sialyl-N-acetyllactosamine, Neu5Ac alpha 2-->3Gal beta 1-->4Glc

115 Poly-N-acetyllactosamine oligomer is a type-2 glycan core fro

116 Development of an effective synthesis of N-acetyllactosamine oligomers will therefore provide a n

117 he programmable one-pot synthesis of various N-acetyllactosamine oligomers.

118 obtained for N-acetyllactosamine and sialyl-N-acetyllactosamine oligosaccharide antennae from biante

119 MECA-79 antibody, which reacts with 6-sulfo N-acetyllactosamine on extended core 1 O-glycans.

120 Gal-8 bound preferentially to i-linear poly-N-acetyllactosamines on N-glycans of the TIC marker and

121 arge complex-type N-glycans with linear poly-N-acetyllactosamine (PL) [-3Galbeta1-4GlcNAcbeta1-](n) e

122 core fucosylation, and the abundance of poly-N-acetyllactosamine (PL) [-3Galbeta1-4GlcNAcbeta1-](n) s

123 ine (LN; Galbeta1-4GlcNAc) sequences on poly-N-acetyllactosamine (PL; (-3Galbeta1-4GlcNAcbeta1-)(n))

124 n olfactory sensory neurons (OSNs) with poly-N-acetyllactosamine (PLN) oligosaccharides determined by

125 hibited higher binding for glycans with poly-N-acetyllactosamine (poly(LacNAc)) sequences (Galbeta1-4

126 Poly-N-acetyllactosamine (poly-LacNAc) is ubiquitously expres

127 hat can participate in the synthesis of poly-N-acetyllactosamine (polyLacNAc) chains.

128 hat can participate in the synthesis of poly-N-acetyllactosamine (polyLacNAc) chains.

129 Enzymatic reduction in surface poly-N-acetyllactosamine (polyLacNAc) glycans in HL60 cells r

130 However, one motif found in N-glycans, poly-N-acetyllactosamine (polyLacNAc), still poses a substant

131 ibody (MAb) 3F11, a MAb which recognizes the N-acetyllactosamine portion of strain 35000HP LOS.

132 A77 lacks the galactose residue found in the N-acetyllactosamine portion of the strain 35000HP LOS as

133 ant lacks the galactose residue found in the N-acetyllactosamine portion of the strain 35000HP LOS.

134 e, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branc

135 eisseria gonorrhoeae sialylates the terminal N-acetyllactosamine present on its lipooligosaccharide (

136 g moderate amounts of sialyl Lewis X in poly-N-acetyllactosamines produced large numbers of lung tumo

137 abundance of the Lewis(x) sequence based on N-acetyllactosamine recognized by anti-L5, and a paucity

138 ucity of the Lewis(x) sequence based on poly-N-acetyllactosamine recognized by anti-SSEA-1; (ii) insi

139 N-acetylglucosamine residues within the poly(N-acetyllactosamine) repeat sequence and signals represe

140 OS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region

141 osamine is a unique carbohydrate composed of N-acetyllactosamine repeats and provides the backbone st

142 branched oligosaccharides with multiple poly-N-acetyllactosamine repeats is nearly abolished by AZT c

143 -TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNA

144 Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to

145 First, N-acetyllactosamine repeats were more readily added to t

146 x N- and O-glycans with remarkably elongated N-acetyllactosamine repeats with Lewis epitopes.

147 dramatically as the acceptors contained more N-acetyllactosamine repeats, consistent with the fact th

148 n acceptors containing increasing numbers of N-acetyllactosamine repeats, in contrast to beta4Gal-TI,

149 re consists of (-6GalB1-4GlcNAcB1-)( 4) poly-N-acetyllactosamine repeats.

150 uestion of how the gonococcus infects men if N-acetyllactosamine residues are substituted by Neu5Ac d

151 N-acetyllactosamine residues on LOS must be free of N-ac

152 The structure of BT1043 complexed with N-acetyllactosamine reveals that recognition is mediated

153 n this work, we have investigated the type-2 N-acetyllactosamine scaffold using the complete series o

154 , the transfected cells showed a decrease in N-acetyllactosamine sialylation.

155 amine extension mostly along the linear poly-N-acetyllactosamine side chain.

156 them, cores 2 and 4 are important for having N-acetyllactosamine side chains, which can be further mo

157 3Gal-3, -4, and -6, which act on the type II N-Acetyllactosamine structure (Galbeta1,4GlcNAc) to crea

158 expressed enzyme that synthesizes the beta4-N-acetyllactosamine structure in glycoconjugates.

159 Galectin-3 binds poly-N-acetyllactosamine structures on glycoproteins, but its

160 they produced extended GlcNAc-sulfated poly-N-acetyllactosamine structures with more than four repea

161 onger carbohydrate substrates that have poly-N-acetyllactosamine structures, suggesting the involveme

162 B3GNT2 encodes a poly-N-acetyllactosamine synthase that targets >10 ligands an

163 te that beta4Gal-TIV is responsible for poly-N-acetyllactosamine synthesis in core 2 branched O-glyca

164 results, taken together, indicate that poly-N-acetyllactosamine synthesis in N-glycans and core 2- a

165 l-TI was found to be most efficient for poly-N-acetyllactosamine synthesis in N-glycans.

166 and/or proteins involved in sialylation and N-acetyllactosamine synthesis were also downregulated in

167 h is a rate-limiting step in I-branched poly-N-acetyllactosamine synthesis, allowing poly-N-acetyllac

168 1, an enzyme proposed to be involved in poly-N-acetyllactosamine synthesis, were causal for congenita

169 termine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor

170 multiple internal GlcNAc of unbranched poly-N-acetyllactosamine, termed "myeloglycan," the physiolog

171 hed O-glycans contain fewer and shorter poly-N-acetyllactosamines than N-glycans in many cells.

172 ing activity of the B. arenarum galectin for N-acetyllactosamine, the human blood group A tetrasaccha

173 finities and -delta H values for lactose and N-acetyllactosamine, the soybean agglutinin possesses si

174 possess essentially the same affinities for N-acetyllactosamine, the two mutants possess much lower

175 ess a unique glycome featuring i-linear poly-N-acetyllactosamines through the loss of I-branching enz

176 ltransferase and beta4Gal-TI efficiently add N-acetyllactosamine to linear poly-N-acetyllactosamines.

177 accharide (LOS) containing a terminal sialyl N-acetyllactosamine trisaccharide.

178 ng upon common 3'-sialylated and/or sulfated N-acetyllactosamine-type precursors.

179 ore than four repeats of the GlcNAc-sulfated N-acetyllactosamine unit in the presence of corneal N-ac

180 , the Lc3 synthase could extend the terminal N-acetyllactosamine unit of nLc4 and also had a broad sp

181 core with > 10 monosaccharide units (or > 4 N-acetyllactosamine units) showed E-selectin binding und

182 e having at least 10 monosaccharide units (4 N-acetyllactosamine units) with internal multiple fucosy

183 class Ib molecules studied to date, carries N-acetyllactosamine units.

184 Ic, and the large difference in the price of N-acetyllactosamine vs. lactose, it is suggested that la

185 The efficacy of the galectin-3 inhibitor N-acetyllactosamine was evaluated in TGR(mREN2)27 (REN2)

186 ucosaminyltransferase, the formation of poly-N-acetyllactosamine was found to be extremely inefficien

187 When a beta1,6-GlcNAc branched poly-N-acetyllactosamine was incubated with a mixture of beta

188 Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbe

189 ng when galectin-3, with preference for poly-N-acetyllactosamine, was depleted from polarized MDCK ce

190 tivity and both activities were inhibited by N-acetyllactosamine, whereas a C-terminal deletion mutan

191 lactosamine branches attached to linear poly-N-acetyllactosamine, which is synthesized by I-branching

192 ly to beta1,6-GlcNAc attached to linear poly-N-acetyllactosamines, while beta1, 3-N-acetylglucosaminy

193 librium dialysis, N-Gal-1 and V5D-Gal-1 bind N-acetyllactosamine with a Kd approximately 90 microM, w

194 Thus, these data imply that capping N-acetyllactosamine with alphaGal or alphaFuc and the co

195 of the terminal alpha-Gal or whether capping N-acetyllactosamine with another oligosaccharide would a