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World class computing and information science research at Strathclyde...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

The Department also includes the iSchool Research Group, which performs leading research into socio-technical phenomena and topics such as information retrieval and information seeking behaviour.

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Modulation of sialyl lewis X dependent binding to e-selectin by glycoforms of alpha-1-acid glycoprotein expressed in rheumatoid arthritis

Jorgensen, H G and Elliott, M A and Priest, R and Smith, K D (1998) Modulation of sialyl lewis X dependent binding to e-selectin by glycoforms of alpha-1-acid glycoprotein expressed in rheumatoid arthritis. Biomedical Chromatography, 12 (6). pp. 343-349. ISSN 0269-3879

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Abstract

Alpha-1-acid glycoprotein (AGP) is an extensively glycosylated acute phase protein of imprecisely defined physiological function. Nonetheless it is known that the oligosaccharide component comprising 42% of the 41 kDa molecular weight is critical to the previously described multifarious immunomodulatory functions of AGP in vitro. Complex oligosaccharides were enzymically released from AGP purified from the blood of rheumatoid arthritis sufferers by our oligosaccharide protective method. Oligosaccharide profiling was by means of high pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD), Monosaccharide composition analysis revealed increased fucosylation of inflammatory AGP oligosaccharide chains, suggesting the potential for expression of the tetrasaccharide antigen and E-Selectin ligand, sialyl Lewis X (sLeX), The hypothesis that AGP may function to inhibit blood cell binding to activated endothelium at E-Selectin was tested in a microtitre cell-protein binding assay. In this system we have shown that the oligosaccharide moiety of AGP, as expressed in inflammatory disease, can inhibit the sLeX/E-Selectin interaction. Thus we have identified a correlation between the abnormal glycosylation of AGP in rheumatoid arthritis and suppression of sLeX dependent cell adhesion through inhibition of E-selectin binding which could be the basis of a novel, site specific, anti-inflammatory agent. (C) 1998 John Wiley & Sons, Ltd.