Co-purification of the Lewis blood group N-acetylglucosaminide alpha 1 goes to 4 fucosyltransferase and an N-acetylglucosaminide alpha 1 goes to 3 fucosyltransferase from human milk.

Prieels, Jean‐Paul; Monnom, Dominique; Dolmans, Marcel; Beyer, Thomas A.; Hill, Robert R.L.

doi:10.1016/s0021-9258(19)68643-6

Cited by 172 publications

(5 citation statements)

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“…The cDNA for FTase was generated by PCR from human genomic DNA (Clontech) based on the sequence reported by Weston et al (1992), and the construct was ligated into mammalian expression system pMON3359 (Hippenmeyer & Highkin, 1993). The enzyme was partially purified from conditioned medium by ammonium sulfate precipitation and SP-Sephadex chromatography (Prieels et al, 1981). Trypanosoma cruzi /3-galactoside-a2,3-irans-sialidase was isolated by immunoaffinity chromatography and immobilized on Concanavalin A-Sepharaose as previously described (Scudder et al, 1993).…”

Section: Methodsmentioning

confidence: 99%

Binding of Sialyl Lewis X to E-Selectin As Measured by Fluorescence Polarization

Jacob¹,

Kirmaier²,

Abbas³

et al. 1995

Biochemistry

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Section: Methodsmentioning

confidence: 99%

Binding of Sialyl Lewis X to E-Selectin As Measured by Fluorescence Polarization

Jacob¹,

Kirmaier²,

Abbas³

et al. 1995

Biochemistry

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“…25,26 Chun-Hung Lin a-1,3/4-Fucosyltransferases Fut3-7 and fut9 genes encode six a-1,3-FucTs (FucT-III, -IV, -V, -VI, -VII and FucT-IX) which are responsible for the last step in the synthesis of Lewis antigens including Le x , Le y , Le a , Le b , sLe x and sLe a . [27][28][29][30] Among them, FucT-III and FucT-V have additional a-1,4-activity, and are capable of adding L-fucose to both type I and type II acceptors. FucT-III, -V and -VI can utilize both sialylated and non-sialylated acceptors.…”

Section: A-12-fucoyltransferasesmentioning

confidence: 99%

Development of fucosyltransferase and fucosidase inhibitors

Lin

2013

Chem. Soc. Rev.

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L-Fucose-containing glycoconjugates are essential for a myriad of physiological and pathological activities, such as inflammation, bacterial and viral infections, tumor metastasis, and genetic disorders. Fucosyltransferases and fucosidases, the main enzymes involved in the incorporation and cleavage of L-fucose residues, respectively, represent captivating targets for therapeutic treatment and diagnosis. We herein review the important breakthroughs in the development of fucosyltransferase and fucosidase inhibitors. To demonstrate how the synthesized small molecules interact with the target enzymes, i.e. delineation of the structure-activity relationship, we cover the reaction mechanisms and resolved X-ray crystal structures, discuss how this information guides the design of enzyme inhibitors, and explain how the molecules were optimized to achieve satisfying potency and selectivity.

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“…An area of recent interest is the design of potential substrates and inhibitors of fucosyl and sialyl transferases involved in the assembly of the Sialyl Lewis-x structure (a tumor-associated structure and ligand of E-selectin-mediated inflammatory processes) . These enzymes are involved in the last steps of the biosynthesis of Lewis oligosaccharide antigens by transferring α-fucopyranosyl residues . In this context, Ogawa et al have carried out studies aimed at finding inhibitors of the biosynthesis of Lewis oligosaccharide antigens. , They reported the synthesis of carbasugar analogues of the disaccharide fragment highlighted in Figure .…”

Section: 2 Biological Activity Of Carbapyranosesmentioning

confidence: 99%