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1 syltransferase 2 is in fact a TSR-specific O-fucosyltransferase.
2 sferase activity with minimal effects on the fucosyltransferase.
3 genes confirm that each encodes an alpha(1,2)fucosyltransferase.
4 compared with those generated with exogenous fucosyltransferase.
5 of a fucose residue in GDP-fucose and a milk fucosyltransferase.
6 y the PgtA galactosyltransferase but not the fucosyltransferase.
7 surface expression of Notch and a protein O-fucosyltransferase.
8 at is defective for sialylation and alpha1,3-fucosyltransferase.
9 ha, a key regulator of expression of various fucosyltransferases.
10 omosome 19q13.3 that encodes three alpha(1,2)fucosyltransferases.
11 organs, indicating that Arabidopsis thaliana fucosyltransferase 1 (AtFUT1) accounts for all of the xy
12 ana, a glycosyl transferase family 37 (GT37) fucosyltransferase 1 (AtFUT1) catalyzes the regiospecifi
14 ed the subcellular localization of protein O-fucosyltransferase 1 (O-FucT-1), which is responsible fo
16 ke repeats that may be modified by protein O-fucosyltransferase 1 (Pofut1), an essential component of
17 ith mutations in keratin 5 (KRT5), protein O-fucosyltransferase 1 (POFUT1), or protein O-glucosyltran
21 we show that mouse embryos lacking protein O-fucosyltransferase 1 die at midgestation with severe def
23 othesis and show the following: 1) protein O-fucosyltransferase 1 is indeed the enzyme that adds O-fu
24 the transfer of fucose to Notch by protein O-fucosyltransferase 1 is necessary for Fringe to function
27 lacking both maternal and zygotic protein O-fucosyltransferase 1, a cell-autonomous and essential co
28 ss these issues, the gene encoding protein O-fucosyltransferase 1, an enzyme required for Notch ligan
33 ted by O-fucosylation (mediated by protein O-fucosyltransferase-1) and Fringe, a beta1,3-N-acetylgluc
34 Another alpha1,3-fucosyltransferase gene, fucosyltransferase 10 (Fut10), is expressed in the ventr
35 n of innate lymphoid cells and expression of fucosyltransferase 2 (Fut2) by IL-22-stimulated IECs.
38 ncentration and the 461G-->A polymorphism of fucosyltransferase 2 (FUT2), a gene associated with susc
39 of intestinal epithelial cells, catalyzed by fucosyltransferase 2 (Fut2), is a major glycosylation me
40 bospondin type 1 repeats (TSRs) by protein O-fucosyltransferase 2 (POFUT2) and is elongated with gluc
41 plasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of
44 rmore, we expressed recombinant Drosophila O-fucosyltransferase 2 and showed that it O-fucosylates TS
48 e show that RNAi-mediated reduction of the O-fucosyltransferase 2 message significantly decreased TSR
53 this study, we verified that mouse protein O-fucosyltransferase-2 (POFUT2) specifically adds O-fucose
54 DM4, IDDM5, IDDM6, IDDM8, and IDDM10 and the fucosyltransferase-2 locus for linkage in sib pairs with
55 of glycosyltransferase expression identified fucosyltransferase 3 (Fut3) as the key enzyme driving sL
56 trate that hematopoietic progenitors lacking fucosyltransferase 4 and 7 do not express functional PSG
59 nds contribute to metastasis using alpha(1,3)fucosyltransferase 7 (Fuc-TVII(-/-))-deficient mice.
60 e examined the transcriptional regulation of fucosyltransferase 7 (FUT7), an enzyme crucial for gener
61 f N-glycans on glycoproteins is catalyzed by fucosyltransferase 8 (FUT8) in mammalian cells and is in
64 n this study, we examined mice deficient for fucosyltransferase 9 (Fut9), which is thought to synthes
73 yzed by FT85, a 768-amino acid protein whose fucosyltransferase activity maps to the C-terminal half
75 alylated structures by high-level alpha(1,2)-fucosyltransferase activity reduces monocyte adherence a
77 that Fut10 is involved in a unique alpha1,3-fucosyltransferase activity with stringent substrate spe
78 ialyl Lewis x, sialyl Lewis a, alpha(1,3/1,4)fucosyltransferase activity, and FUT3 transcript, but an
83 genic mice by expressing a human alpha 1,3/4-fucosyltransferase (alpha 1,3/4-FT; EC 2.4.1.65) along t
84 g GDP-fucose:N-acetylglucosaminyl alpha(1,3) fucosyltransferase (alpha(1,3)-Fuc-T) activity was recen
85 in-of-function mutant expresses an alpha(1,3)fucosyltransferase (alpha(1,3)Fuc-T) activity that gener
86 sferase [alpha(2,3)ST], or Galbeta 2-alpha-L-fucosyltransferase [alpha(1,2)FT; EC 2.4.1.691, etc.
88 n H-type GDPFuc:beta-D-galactoside alpha1, 2-fucosyltransferase (alpha1,2FT) was stably transfected i
89 antial redundancy in the mammalian alpha-1,3-fucosyltransferase and alpha-1,2-fucosyltransferase gene
90 ts, enzymatic transfers with a milk alpha1,3-fucosyltransferase and an alpha2,3-sialyltransferase (ST
91 eting expression of the endogenous alpha-1,3-fucosyltransferase and beta-1,2-xylosyltransferase genes
93 ibitory activities correlated inversely with fucosyltransferase and sialyltransferase activity based
94 scale) of an endoplasmic reticulum-resident fucosyltransferase and two potential anticancer protein
95 hat the common motif shared by both alpha1,2-fucosyltransferases and alpha1,6-fucosyltransferases hav
96 ences in the relative activities of alpha1,3-fucosyltransferases and alpha2,3-sialyltransferases in t
98 involved in glycan modifications, including fucosyltransferases and sialyltransferases, during infla
99 C79a/Ig-alpha, C79b/Ig-beta, and Fut3/alpha-fucosyltransferase); and (ii). variants of bacteriophage
100 yltransferase1 (GALT1), Arabidopsis alpha1,4-fucosyltransferase, and Rattus norvegicus alpha2,6-sialy
101 lysis predicts that these family members are fucosyltransferases, and we first hypothesized that some
102 ate that this cDNA and its cognate alpha(1,3)fucosyltransferase are expressed in endothelial cells li
103 Fucalpha(1-->2)Galbeta moieties and cognate fucosyltransferases are also expressed by epithelial cel
105 e various studies, the specificities of many fucosyltransferases are still unknown, so new approaches
106 human FucT using a structure of a bacterial fucosyltransferase as a template demonstrated that the a
109 requirement for E-selectin ligands, alpha1,3 fucosyltransferases, beta1 and alphaVbeta3 integrins, an
111 whether high-level expression of alpha(1,2)-fucosyltransferase by porcine endothelium would reduce h
112 ficant differences in expression of alpha1,3-fucosyltransferases, C2GnT (Core2 transferase), or P-sel
114 -1 cDNA is coexpressed with an alpha 1,3/1,4 fucosyltransferase cDNA in COS cells, a functional prote
116 gain-of-function experiments where all three fucosyltransferases conferred E-selectin-mediated rollin
121 -fucose:beta(1-->4)-D-galactosyl-R 2-alpha-L-fucosyltransferase enzymes (EC 2.4.1.69) responsible for
122 leles of the Pofut1 gene, which encodes an O-fucosyltransferase essential for Notch-ligand binding.
123 egrins and targeted deletion of an alpha(1,3)fucosyltransferase essential for selectin ligand synthes
124 re 1 beta 3-galactosyltransferase and alpha2-fucosyltransferase exhibit unique peptide/glycopeptide s
125 helial cell line transfected with alpha(1,2)-fucosyltransferase, expressing reduced surface expressio
126 y factors resulted in the down-regulation of fucosyltransferase expression, reflected by altered glyc
127 yltransferase (ST) activity and low alpha1,2-fucosyltransferase (FT) activities were detected from du
129 ned blood group H gene-specified alpha 1,2-L-fucosyltransferase (FT) toward a variety of sulfated, si
131 redominant HUVEC sialyltransferases (ST) and fucosyltransferases (FT), key enzymes in sLe(x) and Le(x
133 ique specificities of the cloned alpha 1,3-L-fucosyltransferases (FTs), FT III (Lewis type), FT IV (m
134 or murine neutrophils by exogenous alpha1-3-fucosyltransferase FTVI and GDP-fucose created many new
135 trate here that mice deficient in alpha(1,3) fucosyltransferase Fuc-TVII exhibit a leukocyte adhesion
137 en in wild-type mice; mice lacking alpha 1,3-fucosyltransferases Fuc-TIV and Fuc-TVII; or mice lackin
138 e sialyltransferase ST3Gal-III compared with fucosyltransferases Fuc-TIV/VII in the synthesis of the
140 co-expressed with both C2GnT and an alpha1 3 fucosyltransferase (Fuc-TIII, Fuc-TIV, or Fuc-TVII).
141 s deficient in the expression of alpha-(1, 3)fucosyltransferase (Fuc-TVII), an enzyme known to be req
142 or both PSGL-1 and its modifying alpha-(1,3) fucosyltransferase, Fuc-TVII, allowed binding and infect
143 the catalytic domain of two human alpha1,3/4-fucosyltransferases (fucosyltransferases (FucTs) III and
146 r laboratories indicated that the alpha(1,3)-fucosyltransferase FucT-VII regulates the synthesis of E
147 ed prominently but incompletely by alpha(1,3)fucosyltransferase FucT-VII-dependent fucosylation.
148 E-selectins and that the leukocyte alpha(1,3)fucosyltransferases FucT IV and FucT VII do not provide
149 tin ligand biosynthesis include the alpha1,3-fucosyltransferases FucT-VII and FucT-IV, one or more si
152 his deficiency results from reduced alpha1,3-fucosyltransferase (FucT) expression and activity in the
155 in ligands must be fucosylated by alpha(1,3)-fucosyltransferase (FucT)-IV or FucT-VII as rolling is a
161 ion of the two principal leukocyte alpha 1,3 fucosyltransferases, FucT-IV and FucT-VII, in a panel of
163 acid sequence alignment of human alpha1, 3/4-fucosyltransferases (FucTs) demonstrates that three high
164 y of domain swap mutants of human alpha1,3/4-fucosyltransferases (FucTs) III and V has been carried o
165 of two human alpha1,3/4-fucosyltransferases (fucosyltransferases (FucTs) III and V), and to identify
166 transfer of two of these (the core alpha1,3-fucosyltransferase FUT-1 and the core alpha1,6-fucosyltr
167 cosyltransferase FUT-1 and the core alpha1,6-fucosyltransferase FUT-8) were previously characterized.
168 e surface glycans by inhibition of alpha(1,3)fucosyltransferase (FUT) gene expression is an attractiv
169 a GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase (FUT) in an antisense orientation in
172 ha1,6-fucosylation levels by up-regulating N-fucosyltransferases FUT1, FUT4 and FUT8 expression, resp
175 contributions of all three myeloid alpha1,3-fucosyltransferases (FUT4, FUT7, and FUT9) to selectin-l
177 r the inability of the biosynthetic alpha1,6-fucosyltransferase (FUT8) to directly fucosylate full-si
181 n was homozygous recessive for the alpha(1,2)fucosyltransferase gene (FUT2) in the ABH histo-blood gr
182 infection, and expression of the alpha(1,2) fucosyltransferase gene (FUT2) responsible for the secre
183 from transgenic pigs expressing the alpha1,2 fucosyltransferase gene (H-transferase or HT) gene into
184 located between the secretor type alpha(1,2)-fucosyltransferase gene cluster (FUT1-FUT2-FUT2P) and th
187 cloned and expressed the chicken alpha(1,3)-fucosyltransferase gene involved in LewisX biosynthesis,
188 othelium by transfection with the alpha(1,2)-fucosyltransferase gene reduced susceptibility to human
189 transferase genes and demonstrate a role for fucosyltransferase gene regulation in the developmental
192 nce of the repeats, including the alpha(1-2) fucosyltransferase gene, necessary for the synthesis of
193 etween nonmammalian and mammalian alpha(1,3)-fucosyltransferase genes and demonstrate a role for fuco
194 es from the open reading frames of the mouse fucosyltransferase genes corresponding to human FUT1, FU
195 hese and other results suggest that multiple fucosyltransferase genes in C. elegans may encode enzyme
198 ndothelial cell transfection with alpha(1,2)-fucosyltransferase has been shown to reduce terminal sia
201 dentification of the gene encoding protein O-fucosyltransferase I now makes possible mutational strat
202 on of amino acids found in human alpha1, 3/4-fucosyltransferase III (FucT III) conferred a significan
203 ted from CHO cells cotransfected with either fucosyltransferase III (sPSGL-1/Fuc-TIII) or fucosyltran
204 cells were stably transfected with alpha1, 3-fucosyltransferase III to express sialyl Lewis X structu
205 t that the AtFUT family is likely to include fucosyltransferases important for the synthesis of wall
207 s, we have investigated the role of alpha1,3-fucosyltransferases in generating E-selectin ligands, an
208 quences and confirm the primacy of alpha(1,3)fucosyltransferases in the synthesis of selectin ligands
209 ting E-selectin ligand-synthesizing alpha1,3 fucosyltransferases in transgenic adenoma of mouse prost
211 binding or for localization of the alpha1,2-fucosyltransferase involved in O-antigen biosynthesis.
212 loitation of the specificity of the enzymes (fucosyltransferases) involved in fucosylation is a recur
213 otein ligand-1 (PSGL-1) modified by alpha1,3-fucosyltransferase is the principal selectin ligand on s
214 t evidence that FUT8, the mammalian alpha1,6-fucosyltransferase, is the sole enzyme responsible for t
215 cosylated sLe(x) receptors, and two enzymes, fucosyltransferase IV (FucT-IV) and VII (FucT-VII), are
217 d alpha-2,3-sialyltransferases and alpha-1,3-fucosyltransferases IV and VI were determined, and the r
220 2 beta1,6-N-acetylglucosaminyltransferase or fucosyltransferases IV/VII were impaired for engraftment
223 We also stably expressed human alpha1,3-fucosyltransferase IX in the L8-GalNAcT cells to establi
224 g and characterization of a murine alpha(1,3)fucosyltransferase locus whose expression pattern correl
225 fferently to conformational changes, and the fucosyltransferases lost less activity than the sialyltr
226 fucosylated glycoconjugates and an alpha1, 2-fucosyltransferase messenger RNA in the small-intestinal
227 veal that FUT-6, another C. elegans alpha1,3-fucosyltransferase, modifies nematode glycan cores, spec
228 ferase 2 was assumed to be another protein O-fucosyltransferase, no biochemical characterization exis
230 th factor-like repeats, GDP-fucose protein O-fucosyltransferase (O-FucT-1), was purified previously f
231 nalysis reveals that, unlike all other known fucosyltransferases, O-FucT-1 is a soluble protein that
232 er of the large GT-B fold family, like other fucosyltransferases of known structures, it contains a v
233 and its ligands are modified by a protein O-fucosyltransferase (OFUT1) that attaches fucose to a Ser
234 is presumed to require one or more alpha(1,3)fucosyltransferases, operating upon common 3'-sialylated
237 cosylated FVII EGF-1 was achieved by using O-fucosyltransferase purified from Chinese hamster ovary c
239 ly and indicates that sialyltransferases and fucosyltransferases recognize N-acetyllactosamine in a d
240 ndothelial cell transfection with alpha(1,2)-fucosyltransferase reduced terminal sialic acid expressi
241 l mediator of Notch receptors, and Pofut1, a fucosyltransferase required for the activity of Notch re
242 scherichia coli O128:B12 encodes an alpha1,2-fucosyltransferase responsible for adding a fucose onto
243 obiose unit of these N-glycans, but only the fucosyltransferases responsible for transfer of two of t
244 on, sulfation, and fucosylation by alpha 1,3-fucosyltransferase(s) (FucT), are required for functiona
247 ster ovary (CHO) cells expressing PSGL-1 and fucosyltransferase show a dramatic increase in binding t
248 tivity of the sialyltransferases whereas the fucosyltransferases showed some activity, albeit very lo
249 were stably transfected with alpha(1,3/1,4) fucosyltransferase-specific cDNA (B16F10ft), allowing th
250 studies and structure comparison with other fucosyltransferases suggest that FUT1 uses a SN2-like re
251 rt provides the first evidence that a single fucosyltransferase, termed FucT-VII, controls the synthe
252 function beta3-galactosyltransferase/alpha2-fucosyltransferase that contributes the 2nd and 3rd suga
255 dy binds fucosyltransferase1, an alpha-(1,2)-fucosyltransferase that synthesizes H-type structures on
256 glycoprotein ligand-1 (PSGL-1) and alpha1-3-fucosyltransferases that construct the glycan determinan
257 xpression of Fut genes that encode alpha-1,3-fucosyltransferases, the enzymes that generate the Le(x)
258 ochemically identified to encode an alpha1,2-fucosyltransferase through radioactivity assays, as well
259 d cells of GDP-fucose, the substrate used by fucosyltransferases to incorporate fucose into protein a
262 cceptor substrate specificity into alpha1, 3-fucosyltransferase V (FucT V), which, under the same ass
263 as the donor substrate for recombinant human fucosyltransferase V, and GDP-d-[3H]arabinosep serves as
265 hosphate (GDP) fucose and exogenous alpha1-3 fucosyltransferase VI increased cell-surface sLe(x) dete
266 eated ex vivo for 30 minutes with the enzyme fucosyltransferase-VI and guanosine diphosphate fucose t
267 The selectin pathway recruiter, alpha-1,3-fucosyltransferase-VI enzyme, significantly increased Tr
270 trophils also expressed transcripts encoding fucosyltransferase VII (FucT-VII) and Core2GlcNAcT-I, wh
271 pressed equivalently high levels of alpha1,3-fucosyltransferase VII (FucT-VII) as wild-type Th1 cells
272 hese ligands is the expression of alpha(1,3)-fucosyltransferase VII (FucT-VII), a FucT essential for
273 have determined the role of tissue-specific fucosyltransferase VII (FucT-VII), an enzyme necessary f
277 tment (resulting from targeted disruption of fucosyltransferase VII [FTVII]), and the absence of matu
280 we transduced Jurkat (JK) T cells expressing fucosyltransferase VII with a chimeric chemokine recepto
281 ese hamster ovary cells, along with CD34 and fucosyltransferase VII, results in ligand activity, as d
282 e cell-surface receptor, PSGL-1, mediated by fucosyltransferase VII, serves as a mechanism for regula
283 arting JK lines, the resulting cell line (JK fucosyltransferase VII-CCR6) migrated 6-fold better to C
284 cotransfected with cDNAs encoding alpha (1,3)fucosyltransferase-VII (FucT-VII) and PSGL-1 rolled on L
285 ontrast to cells cotransfected with alpha1-3 fucosyltransferase-VII (FucT-VII) plus PSGL-1, K562 cell
287 -selectin, correlated with elevated alpha1,3-fucosyltransferase-VII messenger RNA levels, but selecti
288 ferases alpha2,3-sialyltransferase, alpha1,3-fucosyltransferase-VII, and core 2 beta1,6 N-acetylgluco
289 ific glycosyltransferases including alpha1,3-fucosyltransferase-VII, core 2 beta1-6-N-glucosaminyltra
290 ated, and negligibly inhibitory, whereas the fucosyltransferase was active toward small substrates.
292 atode N-glycan core in vitro using all three fucosyltransferases was performed, and the nature of the
293 with another recently characterized alpha1,2-fucosyltransferase (WbsJ) of E. coli O128:B12 indicates
295 es of FKP and a Helicobacter pylori alpha1,3 fucosyltransferase, we prepared a library of Le(x) trisa
296 sferase activity and a decrease in alpha(1,3)fucosyltransferases when these cells differentiate towar
298 in CHO LEC11 cells with an active alpha(1,3)-fucosyltransferase, which makes possible the biosynthesi
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