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J. Biol. Chem., Vol. 265, Issue 26, 15424-15431, Sep, 1990
MC Bourin, E Lundgren-Akerlund and U Lindahl
Previous studies on rabbit thrombomodulin (TM) revealed that certain
anticoagulant activities expressed by TM depend on the presence of an
acidic domain tentatively identified as a sulfated galactosaminoglycan
(Bourin, M.-C., Ohlin, A.-K., Lane, D., Stenflo, J., and Lindahl, U. (1988)
J. Biol. Chem. 263, 8044-8052). The glycan was released by alkaline
beta-elimination, isolated by ion-exchange chromatography, and radiolabeled
by partial N-deacetylation (hydrazinolysis) followed by re-
N-[3H]acetylation. The labeled product behaved like standard chondroitin
sulfate on ion-exchange chromatography, exhibited a Mr of 10-12 x 10(3) on
gel chromatography, and was susceptible to degradation by chondroitinase
and testicular hyaluronidase. The major labeled degradation products
following digestion of the glycosaminoglycan with chondroitinase were
identified, depending on the incubation conditions, either as
4/6-mono-O-sulfated, 4,5-unsaturated disaccharides (delta HexA-GalNAc(S]
and N-acetylgalactosamine 4,6-di-O-sulfate (GalcNAc (diS], the latter
component accounting for approximately 25% of the total label, or as a
major fraction of labeled trisaccharide, with the predominant structure
GalNAc(diS)-GlcA-GalNAc(diS). The terminal GalNAc(diS) unit (not
substituted at C3) was shown to be more susceptible to N-deacetylation
during hydrazinolysis than were the internal GalNAc units (substituted at
C3), and thus was more extensively labeled, resulting in
over-representation of this unit. It is concluded that rabbit TM is a
chondroitin sulfate proteoglycan, which carries a single glycan side chain
characterized by an unusual accumulation of sulfate groups at the
nonreducing terminus. Metabolically 35S-labeled TM was isolated from
cultured rabbit heart endothelial cells and characterized as a chondroitin
sulfate proteoglycan which accounted for 1-2% of the total 35S-labeled
cell- associated macromolecules. The isolated chondroitin sulfate showed
weaker antithrombin-dependent anticoagulant activity, on a molar basis,
than the intact TM proteoglycan. The anticoagulant action of TM thus
depends on a unique form of functional collaboration between the different
constituents of a glycoconjugate.
Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan
Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, Uppsala.
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