Naslov
Newly synthesized Man9-glycoprobe enables direct analysis of mannan binding lectin activity in human serum

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

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

Izvornik
2nd Scientific Symposium with International Participation '45 years of molecular biology in Croatia - 50 years of double helix', Book of Abstracts / Ambriović Ristov, Andreja ; Brozović, Anamarija - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 2003, 38-39

Skup
2nd Scientific Symposium with International Participation '45 years of molecular biology in Croatia - 50 years of double helix'

Mjesto i datum
Zagreb, Hrvatska, 20.11.2003. - 21.11.2003

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
Man9 glycoprobe; activity of lectins; mannan binding lectin

Sažetak
Numerous biological processes are based on highly specific interactions between oligosaccharide structures of glycoconjugates and their receptors, lectins. However, precise biological roles of many lectins are still mostly unknown, partly because of the lack of adequate methods that could enable analysis of lectin activity. 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 an oligosaccharide ligand, photoreactive crosslinker and a digoxin tag, and enable direct analysis of lectin activity in complex biological samples. The mannan binding lectin (MBL) plays a major role in innate immunity through its ability to activate complement upon binding to carbohydrate arrays on the surface of various microorganisms. It is a C-type lectin with a typical soluble collectin structure. 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 is an important element in the pathology of rheumatoid arthritis.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA