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Analysis of agalacto-IgG in rheumatoid arthritis using surface plasmon resonance
Linköping University, Department of Biomedicine and Surgery, Clinical Chemistry. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Biomedicine and Surgery, Clinical Chemistry. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Biomedicine and Surgery, Clinical Chemistry. Linköping University, Faculty of Health Sciences.
2000 (English)In: Glycoconjugate Journal, ISSN 0282-0080, E-ISSN 1573-4986, Vol. 17, no 5, 323-329 p.Article in journal (Refereed) Published
Abstract [en]

It is well established that IgG from rheumatoid arthritis (RA) patients are less galactosylated than IgG from normal individuals. Determination of agalacto-IgG may therefore aid in diagnosis and treatment of RA. The decrease in galactosylation of IgG leads to an increase in terminal N-acetylglucosamine residues, which can be detected using a specific lectin from Psathyrella velutina. In the present study IgG from RA and control serum was purified using affinity chromatography. The samples were then, after reduction, analyzed on a BIOCORE® 2000 system with immobilized Psathyrella velutina lectin. Using this technique it was possible to discriminate between IgG from RA patients and IgG from control individuals with respect to its content of IgG with terminal N-acetylglucosamine. The affinity biosensor technique makes it possible to detect binding without labeling or using secondary antibodies.

Place, publisher, year, edition, pages
2000. Vol. 17, no 5, 323-329 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-25225DOI: 10.1023/A:1007169621518Local ID: 9664OAI: oai:DiVA.org:liu-25225DiVA: diva2:245552
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13Bibliographically approved
In thesis
1. Shedding light on glycosylation: Analysis of complex carbohydrates using an affinity biosensor
Open this publication in new window or tab >>Shedding light on glycosylation: Analysis of complex carbohydrates using an affinity biosensor
2001 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The main objective during the work described in this thesis has been to develop assays for stodies of complex carbohydrates in a clinical context. Complex carbohydrates, such as free or protein linked oligosaccharides, have been shown to have important biological functions. Furthermore, certain diseases have been associated with changes in oligosaccharide composition. We wanted to explore the potential of affinity biosensors to analyze such changes, since disease-specific carbohydrate stroctores might be useful in the diagnosis and prognosis of diseases.

Throughout this work a surface plasmon based affinity biosensor instrument has been used. The instrmnent detects changes in refractive index close to a sensor surface. By immobilization of, e.g., an antibody at the sensor surface, the change in refractive index caused by antigen binding can be followed over time. The change in refractive index is proportional to the mass of bound antigen. This detection technique was used in the present work to quantitate free oligosaccharides as well as the presence of certain carbohydrate stroctores on glycoproteins.

Two different types of assays for analysis of complex carbohydrates were developed. The first type of assay was a single step assay, where a carbohydrate-binding protein was immobilized at the sensor surface. Changes in response due to binding of free oligosaccharides or glycoproteins in samples were then used to quantitate the content of specific carbohydrate structores. The second type of assay was a sandwich assay, where antibodies directed to the glycoprotein to be stodied were immobilized at the sensor surface. This allowed the glycoprotein to be captored at the sensor surface from crude samples such as diluted blood plasma. The glycosylation of the captored glycoprotein was then analyzed by injection of a lectin over the sensor surface. The relative amount of the carbohydrate stroctore recognized by the lectin was determined by calculating a ratio between sensor responses for bound lectin and captored glycoprotein.

The single step assay was used to quantitate Fragmin ® concentration, a low molecular weight heparin used as an anticoagulant. The single step assay was further used to analyze immunoglobulin G from rheumatoid arthritis patients and control individuals for oligosaccharide chains deficient in galactose, a carbohydrate structure associated with this disease. The sandwich type assay was used to follow changes in fucosylation of an acute-phase protein, α1-acid glycoprotein, in plasma from patients with severe burns. The same assay was also used to stndy the effect of cytokines on secretion and glycosylation of α1-acid glycoprotein from a human hepatoma cell line (HepG2).

Place, publisher, year, edition, pages
Linköping: Linköpings universitet, 2001. 49 p.
Series
Linköping University Medical Dissertations, ISSN 0345-0082 ; 675
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-25678 (URN)10054 (Local ID)91-7219-970-9 (ISBN)10054 (Archive number)10054 (OAI)
Public defence
2001-05-18, Administrationsbyggnadens aula, Universitetssjukhuset, Linköping, 13:30 (Swedish)
Opponent
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2015-09-18Bibliographically approved

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Liljeblad, MathiasLundblad, ArnePåhlsson, Peter

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