Naslov
Analysis of mannose binding lectin activity in human sera

Autori
Šupraha Goreta, Sandra ; Flögel, Mirna ; Lauc, Gordan

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Abstracts 4th Croatian Congress of Medical biochemists, Biochemia Medica, Vol.13, supplement No 1-2 / Topić, Elizabeta ; Vrkić, Nada ; Štefanović, Mario - Zagreb, 2003

Skup
4th Croatian Congress of Medical Biochemists

Mjesto i datum
Zadar, Hrvatska, 24.09.2003. - 28.09.2003

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
MBL; lectin activity; glycoprobes

Sažetak
Analysis of mannose binding lectin activity in human sera S. Šupraha Goreta, M. Flögel and G. Lauc Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, A. Kovačića 1, 10 000 Zagreb, Croatia (sandras@pharma.hr) Aiming to improve tools for the analysis of lectins, we have recently developed a new class of complex neoglycoconjugates named Glycoprobes (Glycobiology 10:357, 2000). Glycoprobes consists of a oligosaccharide ligand, photoreactive crosslinker and a digoxin tag, and enable direct analysis of lectin activity in complex biological samples. Mannan-binding lectin (MBL) is a C-type lectin with a typical soluble collectin structure. It functions as a pattern recognition molecule that binds repeating sugar arrays on many microbial surfaces. Its ability to activate complement response makes it an important player in the first line of defense, as well as in some pathological processes. To be able to analyze MBL activity in human serum we synthesized a specific glycoprobe containing Mannose9-N-Acetylgalactosamine2 (Man9) glycan as a ligand. Using Man9-glycoprobe we assayed MBL activity in 30 sera of patients with rheumatoid arthritis and 25 sera of matching healthy controls. It is important to note that this was the first example where activity, and not the simple presence of MBL protein was assayed. Very large biological variability of MBL activity was found to exist in both studied groups, while there appeared to be no significant difference between the groups. This result does not support the hypothesis that binding of MBL to degalactosylated oligosaccharides on IgG contributes to the pathology of rheumatoid arthritis.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

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