• Publications
  • Influence
Recycling of a glycosylphosphatidylinositol-anchored heparan sulphate proteoglycan (glypican) in skin fibroblasts.
It is proposed that a portion of the lipid-anchored proteoglycan glypican is internalized, recycled via the Golgi, where heparan sulphate chains are added, and finally re-deposited at the cell surface.
Self-association of heparan sulfate. Demonstration of binding by affinity chromatography of free chains on heparan sulfate-substituted agarose gels.
It is concluded that association between heparan sulfate chains may be quite specific and that the strength of binding is dependent on co-operative interactions between a number of contact zones.
Heparan sulphate/heparin glycosaminoglycans with strong affinity for the growth-promoter spermine have high antiproliferative activity.
Interactions between polyamines and heparin-related glycosaminoglycans are investigated and it is found that spermine binds to a highly sulphated heparan sulphate/heparin preparation with a dissociation constant of 3.7 x 10(-5)M.
Structure of dermatan sulfate. VII. The copolymeric structure of dermatan sulfate from horse aorta.
Abstract The structure of dermatan sulfate-chondroitin sulfate copolymers, isolated from horse aorta, has been examined. It was found that a large proportion of the galactosaminoglycans of this
A method for the sequence analysis of dermatan sulphate.
A procedure for the analysis of dermatan sulphate from pig skin is described and results with testicular hyaluronidase indicate that the distribution of clustered GlcA-GalNAc repeats is periodic and peaks at positions 1-3, 8-9 and around 25.
Structural studies on heparan sulphates. Characterization of oligosaccharides; obtained by periodate oxidation and alkaline elimination.
Three heparan sulphate fractions were subjected to degradation by periodate oxidation and alkaline elimination and three categories of fragments that were isolated by gel and ion-exchange chromatography were obtained.
Interactions between glycosaminoglycans and blood coagulation factors: 1. Affinity chromatography of glycosaminoglycans on thrombin-substituted agarose
Abstract Various glycosaminoglycans have been subjected to affinity chromatography on immobilized bovine thrombin. Chondroitin sulphate, dermatan sulphate and heparan sulphate variants with a
Heparan/chondroitin/dermatan sulfate primer 2-(6-hydroxynaphthyl)-O-beta-D-xylopyranoside preferentially inhibits growth of transformed cells.
It is shown that 2-(6-hydroxynaphthyl)-O-beta-D-xylopyranoside, which can prime both types of glycan chains, inhibits growth of a set of normal and transformed cells, which concludes that growth inhibition is due to priming of HS and/or CS/DS synthesis.
Prion, Amyloid β-derived Cu(II) Ions, or Free Zn(II) Ions Support S-Nitroso-dependent Autocleavage of Glypican-1 Heparan Sulfate*
It is proposed that one function of the cellular prion protein is to deliver copper(II) for the S-nitrosylation of recycling glypican-1.
Structural requirements for heparan sulphate self-association.
It is concluded that self-interaction between heparan sulphate chains is strongly dependent on the overall molecular conformation and the N-sulphate and carboxylate groups as well as the integrity of the D-glucuronate residue are all essential for maintaining the proper secondary structure.