Research article summary (published 2 Feb 1998):

The alpha 1-->3 fucosylation at the penultimate GlcNAc catalyzed by fucosyltransferase VII is blocked by internally fucosylated residue in sialosyl long-chain poly-LacNAc: enzymatic basis for expression of physiological E-selectin epitope.

Full Abstract

Sialosyl-fucosyl poly-LacNAc without sialosyl-Lex epitope in myeloid cell line HL60 was shown to be the ligand for E-selectin-dependent adhesion, particularly under dynamic flow conditions, in our previous study (Handa K, Stroud MR, Hakomori S, Biochemistry 36, 12412-12420, 1997). HL60 cells express only fucosyl-transferase (FT) IV and VII. X3NeuAcVII3FucnLc10, a representative component showing E-selectin-dependent binding under dynamic flow conditions, is not alpha 1-->3 fucosylated at the penultimate GlcNAc catalyzed by FT-VII, but is alpha 1-->3 fucosylated at the internal GlcNAc catalyzed by FT-IV. VI3NeuAcnLc6 is converted to VI3NeuAcIII3FucnLc6 by FT-IV, but is also converted to VI3NeuAcV3FucnLc6 by FT-VII. Thus, penultimate fucosylation catalyzed by FT-VII is not restricted for nLc6 backbone, but is highly restricted for nLc10 backbone. The cooperative effect of FT-IV and FT-VII for synthesis of poly-LacNAc having sialosyl-Lex with internal fucosylation may be blocked or highly restricted in poly-LacNAc having more than two LacNAc units, because preferential alpha 1-->3 fucosylation by FT-IV takes place at internal GlcNAc, inhibiting penultimate fucosylation by FT-VII.

Author information

Author/s: Handa, K (K); Withers, D A (DA); Hakomori, S (S);

Affiliation: Division of Biomembrane Research, Pacific Northwest Research Foundation, Seattle, Washington, USA.

Grants: CA42505 (Agency:NCI NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.

Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun), published in UNITED STATES. (Language: eng)

Reference: 1998-Feb; vol 243 (issue 1) : pp 199-204

Dates: Created 1998/03/16; Completed 1998/03/16; Revised 2007/11/14;

PMID: 9473504, status: MEDLINE (last retrieved date: 2/18/2009)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MeSH Headings (categories) shown below.

Acetylglucosamine - metabolism Base Sequence Carbohydrate Sequence DNA Primers - genetics E-Selectin - chemistry; immunology; metabolism Epitopes - chemistry Fucose - metabolism Fucosyltransferases - drug effects; metabolism

HL-60 Cells Humans Ligands Molecular Sequence Data N-Acetylneuraminic Acid - chemistry Neutrophils - metabolism Oligosaccharides - chemistry; metabolism Polysaccharides - chemistry; metabolism

Note: Bold headings indicate primary MeSH headings or qualifiers.

Associated Chemicals: 5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosamine (0) ; DNA Primers (0) ; E-Selectin (0) ; Epitopes (0) ; Ligands (0) ; Oligosaccharides (0) ; Polysaccharides (0) ; N-Acetylneuraminic Acid (131-48-6) ; Fucose (3713-31-3) ; Acetylglucosamine (7512-17-6) ; poly-N-acetyllactosamine (82441-98-3) ; Fucosyltransferases (EC 2.4.1.-) ; galactoside 3-fucosyltransferase (EC 2.4.1.152)

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