The α(1,3)Fucosyltransferase Fuc-TVII Controls Leukocyte Trafficking through an Essential Role in L-, E-, and P-selectin Ligand Biosynthesis

@article{Mal1996TheF,
  title={The $\alpha$(1,3)Fucosyltransferase Fuc-TVII Controls Leukocyte Trafficking through an Essential Role in L-, E-, and P-selectin Ligand Biosynthesis},
  author={Petr Mal{\'y} and Aron D. Thall and Bronislawa Petryniak and Clare E. Rogers and Peter L. R. Smith and Rory M. Marks and Robert James Kelly and Kevin M. Gersten and Guiying Cheng and Thomas L. Saunders and Sally Ann Camper and Raymond T. Camphausen and Francis X. Sullivan and Yuki Isogai and Ole Hindsgaul and Ulrich H. von Andrian and John B. Lowe},
  journal={Cell},
  year={1996},
  volume={86},
  pages={643-653}
}
alpha(1,3)Fucosylated oligosaccharides represent components of leukocyte counterreceptors for E- and P-selectins and of L-selectin ligands expressed by lymph node high endothelial venules (HEV). The identity of the alpha(1,3)fucosyltransferase(s) required for their expression has been uncertain, as has a requirement for alpha(1,3)fucosylation in HEV L-selectin ligand activity. We demonstrate here that mice deficient in alpha(1,3) fucosyltransferase Fuc-TVII exhibit a leukocyte adhesion… Expand
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E-selectin is a cytokine-inducible, calcium-dependent endothelial cell adhesion molecule that plays a critical role in the leucocyte-endothelium interaction during inflammation and is thought toExpand
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References

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TLDR
Observations suggest that Fuc-TVII participates in the generation of α(1,3)fucosylated ligands for L-selectin and provide further evidence for a role for this enzyme in E- and P- selectin ligand expression in leukocytes. Expand
Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.
TLDR
Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc -TVII consists of a unique class of the alpha 1,. Expand
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TLDR
Sialylation precedes both fucosylation and sulfation during biosynthesis of GlyCAM-1, and this ordering will help to identify the critical acceptor structures recognized by lymph node glycosyltransferases and sulfotransferases. Expand
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TLDR
The complete structure of β-eliminated chains of GlyCAM-1 is defined using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. Expand
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TLDR
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TLDR
The structural identification of the fragments relied on the use of a variety of radiolabeled sugar precursors, further chemical and enzymatic hydrolysis, and high-pH anion-exchange chromatography analysis, and evidence is presented that (SO4-6)Gal beta 1-->4GlcNAc forms the core of a sulfated sialyl Lewis x structure that may comprise a recognition determinant on GlyCAM-1. Expand
Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant.
TLDR
The molecular cloning of a cDNA encoding a new human leukocyte alpha-1,3-fucosyltransferase, termed Fuc-TVII, capable of synthesizing the sialyl Lewis x moiety is reported here. Expand
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TLDR
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TLDR
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TLDR
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