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1 beta-galactoside alpha2,6-sialyltransferase (ST6Gal-I).
2 beta-galactoside:alpha2-6-sialyltransferase (ST6Gal-I).
3 -galactosamide alpha-2,6-sialyltranferase I (ST6Gal-I).
4 tial for proper conformation and activity of ST6Gal I.
5 role of the S-sialylmotif of the same enzyme ST6Gal I.
6 lects for clonal variants with more abundant ST6Gal-I.
7 lylation of these integrins with recombinant ST6Gal-I.
8 olon epithelial cell line lacking endogenous ST6Gal-I.
9 and GnT-II or trans-Golgi enzymes GalT-I and ST6Gal-I.
10 and not on alpha2,6-sialic acids produced by ST6Gal-I.
11 ding is attenuated upon forced expression of ST6Gal-I.
12 ynthesized 13C-CMP-NeuAc to the desialylated ST6Gal-I.
14 at the coordinate up-regulation of gal-3 and ST6Gal-I, a feature that is characteristic of colon carc
17 heroid growth, and clonal variants with high ST6Gal-I activity preferentially survived in CSC culture
18 ated DNA damage, indicating that suppressing ST6Gal-I activity sensitizes inherently resistant cells
19 view summarizes the evidence suggesting that ST6Gal-I activity serves as an "off switch" for galectin
20 g TNFR1 at the cell surface via sialylation, ST6Gal-I acts as a functional switch to divert signaling
28 precursor protein and the sialyltransferase ST6Gal I and is important in the pathogenesis of Alzheim
29 an nodes provided novel evidence for altered ST6Gal-I and GnT-IV glycotransferase activities in lung
30 cans and by other sialyltransferases such as ST6Gal-I and ST6GalNAc-I, forming alpha2,6-sialylated co
31 y 50% of colon adenocarcinomas) up-regulates ST6Gal-I and, in turn, increases sialylation of beta1 in
32 e in the expression of the sialyltransferase ST6Gal I, and an increase in the expression of the galac
33 lation, we forced constitutive expression of ST6Gal-I, and found that this strongly inhibited PMA-ind
39 yposialylation), through BACE1 inhibition or ST6Gal-I constitutive overexpression, eliminates VCAM-1
40 ialic acid residues were also observed, with ST6Gal-I deficiency causing loss on endothelium and ST3G
42 date the mechanisms involved, we report that ST6Gal-I deficiency induces immunoglobulin M (IgM) antig
43 ed the subcellular location and mechanism of ST6Gal I dimer formation, as well as the role of Cys res
44 ed increased dimer formation suggesting that ST6Gal I dimers may be critical in the oligomerization p
46 Pulse-chase analysis demonstrated that the ST6Gal I disulfide-bonded dimer forms in the endoplasmic
49 EK, but not phosphoinositide 3-kinase, block ST6Gal-I down-regulation, integrin hyposialylation, and
50 estingly, macrophage differentiation induces ST6Gal-I down-regulation, leading to reduced alpha2-6 si
51 inhibits galectin-1 death, we expressed the ST6Gal I enzyme in a galectin-1-sensitive murine T cell
53 e for the first time the in vivo role of the ST6Gal-I enzyme in the growth and differentiation of spo
54 spondingly, at these later time points, high ST6Gal-I expressers displayed sustained activation of th
55 atient-derived xenograft tumors enriched for ST6Gal-I-expressing cells relative to pair-matched untre
58 cells following viral infection, suggesting ST6Gal I expression remains high on activated B cells in
61 tive enrichment in clonal variants with high ST6Gal-I expression is observed upon prolonged serum dep
62 these results, serum-starved cells with high ST6Gal-I expression maintain a greater number of S phase
65 PDAC cells, we found that knockdown (KD) of ST6Gal-I expression, as well as removal of surface alpha
66 tive enrichment of clonal variants with high ST6Gal-I expression, further substantiating a role for S
70 Finally, we show that beta1 integrins from ST6Gal-I expressors have increased association with tali
72 er number of S phase cells compared with low ST6Gal-I expressors, reflecting enhanced proliferation.
75 sferase of protein Asn-linked glycosylation (ST6Gal I) forms disulfide-bonded dimers that exhibit dec
76 HO-K1 cells indicated that expression of the ST6Gal I gene causes selective 9-O-acetylation of alpha2
78 D22 and ST6Gal-I knockout mice revealed that ST6Gal-I-generated B cell CD22L plays a role in splenic
79 c and BM-derived DCs, which does not contain ST6Gal-I-generated sialic acids and which, unlike the B
82 Although the recombinant soluble form of ST6Gal I has six cysteines, quantitative analysis indica
83 enon is reproducible by stable expression of ST6Gal I in parental CHO cells, but not upon transfectio
84 beta1-integrin function, we stably expressed ST6Gal-I in a colon epithelial cell line lacking endogen
86 hairpin RNA (shRNA)-mediated attenuation of ST6Gal-I in colon carcinoma cells with elevated endogeno
87 hese results implicate a functional role for ST6Gal-I in fostering tumor cell survival within the ser
88 This first in vivo evidence for a role of ST6Gal-I in tumor progression was confirmed using a nove
89 ubset development, whereas the DC-associated ST6Gal-I-independent CD22L may be required for the maint
90 sfection of CHO-GD3-OAc(-) mutant cells with ST6Gal-I induced 9-O-acetylation specifically on sialyla
94 c cells and primary human CD14(+) monocytes, ST6Gal-I is down-regulated, leading to beta1 hyposialyla
104 ing pancreatic and ovarian cancer cells with ST6Gal-I knockdown or overexpression, we determined that
105 ubcutaneous tumor formation was inhibited by ST6Gal-I knockdown, whereas in a chemically induced tumo
106 of splenic and BM B cell subsets in CD22 and ST6Gal-I knockout mice revealed that ST6Gal-I-generated
107 isoforms of the alpha2,6-sialyltransferase (ST6Gal I) leads to differences in their trafficking, pro
108 , we find that serum-starved cells with high ST6Gal-I levels exhibit increased activation of prosurvi
109 nded TNF treatment (6-24 h), cells with high ST6Gal-I levels exhibited resistance to TNF-induced apop
110 ine-resistant MiaPaCa-2 cells display higher ST6Gal-I levels than treatment-naive cells along with a
112 metastasis and poor survival, and therefore ST6Gal-I-mediated hypersialylation likely plays a role i
113 transfer purified B cells from wild-type or ST6Gal I(-/-) mice into B cell-deficient (microMT(-/-))
117 versed collagen binding back to the level of ST6Gal-I nonexpressors, confirming that alpha2-6 sialyla
121 g that O-acetylation is not induced when the ST6Gal I or ST8Sia I cDNAs are overexpressed in SV40 T a
122 umor initiation model, mice with conditional ST6Gal-I overexpression exhibited enhanced tumorigenesis
123 arian and pancreatic cancer cell models with ST6Gal-I overexpression or knockdown, we find that serum
134 th suppressed BCR signaling, B cells lacking ST6Gal I showed a net redistribution of the BCR to clath
135 her neuraminidase treatment or expression of ST6Gal-I shRNA markedly enhanced TNFalpha-mediated apopt
136 ged by exogenously administering recombinant ST6Gal I sialyltransferase and azide-modified CMP-Neu5Ac
141 onocyte/macrophage lineage down-regulate the ST6Gal-I sialyltransferase via a protein kinase C/Ras/ER
146 a-galactoside alpha-2,6-sialyltransferase 1 (ST6Gal-I) sialyltransferase, which is up-regulated in nu
149 entify the death receptor, Fas (CD95), as an ST6Gal-I substrate, and show that alpha2-6 sialylation o
151 as-dependent alteration in the expression of ST6Gal I, the enzyme that adds alpha2-6-linked sialic ac
152 pha2-6 sialylation and increased activity of ST6Gal-I, the Golgi glycosyltransferase that creates alp
153 that that uses alpha-2,6-sialyltransferase (ST6Gal-I) to enzymatically add 13C-N-acetylneuraminic ac
155 Galbeta1,4GlcNAc alpha2,6-sialyltransferase (ST6Gal I) transfectants were made to replace the endogen
156 d vector-transfected control cells in vitro, ST6Gal I transfection abolished invasion in vitro and in
157 mice in comparison with animals deficient in ST6Gal-I (transfers alpha2-6-linked sialic acid to Galbe
160 r previous study the larger L-sialylmotif of ST6Gal I was analyzed by site-directed mutagenesis, whic
163 sion due to the various 13C-NeuAc adducts on ST6Gal-I was observed in a 3D experiment correlating 1H-
164 uced by the human alpha2-6 sialyltransferase ST6Gal-I, were identified as potent anti-inflammatory me
166 ialyltransferases ST3Gal-III, ST3Gal-IV, and ST6Gal-I, which together are responsible for addition of
168 ed removal of the native NeuAc residues from ST6Gal-I with neuraminidase, separation of the neuramind
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