Pregled bibliografske jedinice broj: 183535
Application of the newly synthesized Man9 glycoprobe to analyze activity of mannan binding lectin in human sera
Application of the newly synthesized Man9 glycoprobe to analyze activity of mannan binding lectin in human sera // 8th Croatian Biological Congress with International Participation, Proceeding of Abstracts / Besendorfer, Višnja ; Kopjar, Nevenka (ur.).
Zagreb: Hrvatsko biološko društvo, 2003. str. 108-109 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 183535 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Application of the newly synthesized Man9 glycoprobe to analyze activity of mannan binding lectin in human sera
Autori
Šupraha Goreta, Sandra ; Mećava, Nataša ; Flögel, Mirna ; Lauc, Gordan
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
8th Croatian Biological Congress with International Participation, Proceeding of Abstracts
/ Besendorfer, Višnja ; Kopjar, Nevenka - Zagreb : Hrvatsko biološko društvo, 2003, 108-109
Skup
8th Croatian Biological Congress with International Participation
Mjesto i datum
Zagreb, Hrvatska, 27.09.2003. - 02.10.2003
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
Man9 glycoprobe; activity of lectins; mannan binding lectin
Sažetak
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-Acetylganactosamine2 (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 olgosaccharides on IgG contributes to the pathology of rheumatoid arthritis.
Izvorni jezik
Engleski
Znanstvena područja
Biologija