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The binding characteristics and utilization of Aleuria aurantia, Lens culinaris and few other lectins in the elucidation of fucosyltransferase activities resembling cloned FT VI and apparently unique to colon cancer cells.

Abstract
Human colon carcinoma cell fucosyltransferase (FT) in contrast to the FTs of several human cancer cell lines, utilized GlcNAcbeta1,4GlcNAcbeta-O-Bn as an acceptor, the product being resistant to alpha1,6-L-Fucosidase and its formation being completely inhibited by LacNAc Type 2 acceptors. Further, this enzyme was twofold active towards the asialo agalacto glycopeptide as compared to the parent asialoglycopeptide. Only 60% of the GlcNAc moieties were released from [14C]fucosylated asialo agalacto triantennary glycopeptide by jack bean beta-N-acetylhexosaminidase. These alpha1,3-L-fucosylating activities on multiterminal GlcNAc residues and chitobiose were further examined by characterizing the products arising from fetuin triantennary and bovine IgG diantennary glycopeptides and their exoglycosidase-modified derivatives using lectin affinity chromatography. Utilization of [14C]fucosylated glycopeptides with cloned FTs indicated that Lens culinaris lectin and Aleuria aurantia lectin (AAL) required, respectively, the diantennary backbone and the chitobiose core alpha1,6-fucosyl residue for binding. The outer core alpha1,3- but not the alpha-1,2-fucosyl residues decreased the binding affinity of AAL. The AAL-binding fraction from [14C]fucosylated asialo fetuin, using colon carcinoma cell extract, contained 60% Endo F/PNGaseF resistant chains. Similarly AAL-binding species from [14C]fucosylated TFA-treated bovine IgG using colon carcinoma cell extract showed significant resistance to endo F/PNGaseF. However, no such resistance was found with the corresponding AAL non- and weak-binding species. Thus colon carcinoma cells have the capacity to fucosylate the chitobiose core in glycoproteins, and this alpha1,3-L-fucosylation is apparently responsible for the AAL binding of glycoproteins. A cloned FT VI was found to be very similar to this enzyme in acceptor substrate specificities. The colon cancer cell FT thus exhibits four catalytic roles, i.e., alpha1,3-L-fucosylation of: (a) Galbeta1,4GlcNAcbeta-; (b) multiterminal GlcNAc units in complex type chain; (c) the inner core chitobiose of glycopeptides and glycoproteins; and (d) the nonreducing terminal chiotobiose unit.
AuthorsE V Chandrasekaran, Ram Chawda, John M Rhodes, Robert D Locke, Conrad F Piskorz, Khushi L Matta
JournalCarbohydrate research (Carbohydr Res) Vol. 338 Issue 9 Pg. 887-901 (Apr 22 2003) ISSN: 0008-6215 [Print] Netherlands
PMID12681913 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Disaccharides
  • Glycopeptides
  • Immunoglobulin G
  • Lectins
  • Plant Lectins
  • lectin, Aleuria aurantia
  • lentil lectin
  • Concanavalin A
  • chitobiose
  • Fucosyltransferases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Topics
  • Animals
  • Cattle
  • Chromatography, Affinity
  • Cloning, Molecular
  • Colonic Neoplasms (enzymology)
  • Concanavalin A (metabolism)
  • Disaccharides (metabolism)
  • Fucosyltransferases (chemistry, isolation & purification, metabolism)
  • Glycopeptides (metabolism)
  • Humans
  • Immunoglobulin G (immunology)
  • Lectins (metabolism)
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism)
  • Plant Lectins (metabolism)
  • Substrate Specificity
  • Tumor Cells, Cultured

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