Structural study of the sugar chains of porcine factor VIII--tissue- and species-specific glycosylation of factor VIII.

3Gal group, and 23% of the biantennary complex-type sugar chains contained the bisecting N-acetylglucosamine residue. These structures were not detected in the sugar chains of human plasma factor VIII. An in vitro competition study of von Willebrand factor and anti-Gal antibody for binding to factor VIII revealed that von Willebrand factor prevented antibody binding to Gal alpha 1-->3Gal groups in porcine factor VIII sugar chains. This suggests that anti-Gal antibody present in human plasma may not interact with the sugar chains of therapeutic porcine factor VIII. Reverse-transcription polymerase chain reaction was used to identify porcine tissues producing FVIII mRNA. These studies revealed that the kidney is one of the major tissues expressing factor VIII which may contain the sugar chains with the bisecting N-acetylglucosamine residue. -->
Substance Nomenclature: 0 (Lectins)
0 (Oligosaccharides)
0 (RNA, Messenger)
0 (Recombinant Proteins)
0 (von Willebrand Factor)
9001-27-8 (Factor VIII)
EC 3.2.1.- (Glycoside Hydrolases)
EC 3.2.1.18 (Neuraminidase)
Entry Date(s): Date Created: 19931201 Date Completed: 19940128 Latest Revision: 20061115
Update Code: 20231215
DOI: 10.1006/abbi.1993.1595
PMID: 8274017
Autor: Hironaka T; Department of Biochemistry, University of Tokyo, Japan., Furukawa K, Esmon PC, Yokota T, Brown JE, Sawada S, Fournel MA, Kato M, Minaga T, Kobata A
Jazyk: angličtina
Zdroj: Archives of biochemistry and biophysics [Arch Biochem Biophys] 1993 Dec; Vol. 307 (2), pp. 316-30.
DOI: 10.1006/abbi.1993.1595
Abstrakt: The asparagine-linked sugar chains of blood coagulation factor VIII purified from porcine plasma were released as oligosaccharides by hydrazinolysis. These sugar chains were converted to radioactive oligosaccharides by reduction with sodium borotritide and separated into neutral and acidic fractions by paper electrophoresis. Most of the acidic oligosaccharides were converted to neutral ones by sialidase digestion, indicating that they are sialyl derivatives. The neutral and the sialidase-treated acidic oligosaccharides were fractionated by serial chromatography on immobilized lectin columns. Structural study of each oligosaccharide by sequential exoglycosidase digestion and by methylation analysis revealed that porcine factor VIII contains high mannose-type and bi-, tri-, and tetraantennary complex-type sugar chains. Sixty-seven percent of the complex-type sugar chains contained the Gal alpha 1-->3Gal group, and 23% of the biantennary complex-type sugar chains contained the bisecting N-acetylglucosamine residue. These structures were not detected in the sugar chains of human plasma factor VIII. An in vitro competition study of von Willebrand factor and anti-Gal antibody for binding to factor VIII revealed that von Willebrand factor prevented antibody binding to Gal alpha 1-->3Gal groups in porcine factor VIII sugar chains. This suggests that anti-Gal antibody present in human plasma may not interact with the sugar chains of therapeutic porcine factor VIII. Reverse-transcription polymerase chain reaction was used to identify porcine tissues producing FVIII mRNA. These studies revealed that the kidney is one of the major tissues expressing factor VIII which may contain the sugar chains with the bisecting N-acetylglucosamine residue.
Databáze: MEDLINE
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