http://www.cnr.it/ontology/cnr/individuo/prodotto/ID48203
Solid phase immunoadsorption for therapeutic and analytical studies on neuropathy-associated anti-GM1 antibodies (Articolo in rivista)
- Type
- Label
- Solid phase immunoadsorption for therapeutic and analytical studies on neuropathy-associated anti-GM1 antibodies (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1093/glycob/cwl074 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- K. Townson; J. Boffey; D. Nicholl; J. Veitch; D. Bundle; P. Zhang; E. Samain; T. Antoine; A. Bernardi; D. Arosio; S. Sonnino; N. Isaacs; H.J. Willison (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://glycob.oxfordjournals.org/content/17/3/294 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1-4,13 : Division of Clinical Neurosciences, Glasgow Biomedical Research Centre, University of Glasgow, Glasgow G12 8TA, United Kingdom /
1,12 : Department of Chemistry, Glasgow Biomedical Research Centre, University of Glasgow, Glasgow G12 8TA, United Kingdom /
5,6 : Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada /
7,8 : CERMAV-CNRS, BP53, F-38041 Grenoble Cedex 9, France /
9,10 : Dipartimento di Chimica Organica e Industriale, Universita' degli Studi di Milano, Via Venezian 21, I-20133 Milano, Italy /
11 : Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, 20090 Segrate MI, Italy /
11 : Center of Excellence on Neurodegenerative Diseases, University of Milan, 20090 Segrate MI, Italy (literal)
- Titolo
- Solid phase immunoadsorption for therapeutic and analytical studies on neuropathy-associated anti-GM1 antibodies (literal)
- Abstract
- Autoimmune neuropathies including Guillain-Barre syndrome are frequently associated with anti-GM1 ganglioside antibodies. These are believed to play a pathogenic role and their clearance from the circulation would be predicted to produce therapeutic benefit. This study examines the conditions required for effective immunoadsorption of anti-GM1 antibodies using glycan-conjugated Sepharose as a matrix. In solution inhibition studies using a range of GM1-like saccharides in conjunction with mouse and human anti-GM1 antibodies, the whole GM1 pentasaccharide beta-Gal-(1-3)-beta-GalNAc-(1-4)-[alpha-Neu5Ac-(2-3)]-beta-Gal-(1-4)-beta-Glc was the favored ligand for maximal inhibiton of antibody-GM1 interactions in comparison with monosaccharides, Gal-(1-3)-beta-GalNAc-beta OMe, and synthetic GM1 mimetics. Immunoadsorption studies comparing binding of mouse monoclonal anti-GM1 antibodies to GM1-Sepharose and beta-Gal-(1-3)-beta-GalNAc-Sepharose confirmed the preference seen in solution inhibition studies. GM1-Sepharose columns were then used to adsorb anti-GM1 immunoglobulin G and immunoglobulin M antibodies from human neuropathy sera. Anti-GM1 antibodies subsequently eluted from the columns often showed a striking monoclonal or oligoclonal pattern, indicating that the immune response to GM1 is restricted to a limited number of B-cell clones, even in the absence of a detectable serum paraprotein. These data support the view that immunoadsorption plasmapheresis could potentially be developed for the acute depletion of serum anti-GM1 antibodies in patients with neuropathic disease, and also provide purified human anti-GM1 antibodies for analytical studies. (literal)
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