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Two glycosylation alterations of mouse intestinal mucins due to infection caused by the parasite Nippostrongylus brasiliensis.

Artikel i vetenskaplig tidskrift
Författare Jessica Holmén
Fredrik J. Olson
Hasse Karlsson
Gunnar C. Hansson
Publicerad i Glycoconjugate journal
Volym 19
Nummer/häfte 1
Sidor 67-75
ISSN 0282-0080
Publiceringsår 2002
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 67-75
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Animals, Carbohydrate Sequence, Fucosyltransferases, genetics, metabolism, Gas Chromatography-Mass Spectrometry, Glycosylation, Intestines, metabolism, parasitology, Mice, Molecular Sequence Data, Mucins, chemistry, metabolism, N-Acetylneuraminic Acid, metabolism, Nippostrongylus, physiology, Oligosaccharides, chemistry, metabolism, RNA, Messenger, genetics, metabolism, Strongylida Infections, metabolism, parasitology, Sulfates, metabolism
Ämneskategorier Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

The glycosylation alterations of mouse small intestinal mucins during a 12-day infectious cycle caused by the parasite Nippostrongylus brasiliensis have been studied. The guanidinium chloride insoluble mucins were isolated at day 0 to 12 from the small intestine of infected and non-infected C57BL/6 mice. The O-linked oligosaccharides were released by reductive beta-elimination from the mucins and separated into neutral, sialylated and sulfated fractions. All fractions were analyzed by monosaccharide composition analysis and the neutral oligosaccharides were structurally characterized by gas chromatography/mass spectrometry. Two oligosaccharides containing blood group H-type epitopes (Fucalpha1-2Gal-) were transiently expressed with a maximum at day 6. Additional oligosaccharides with the common structure HexNAc-Gal-3GalNAcol were transiently induced with a maximum at day 10. Northern blot analysis on total RNA showed a transient expression at day 4-6 of the Fut2 gene encoding a Fucalpha1-2 fucosyltransferase, probably responsible for the detected blood group H-type epitopes. Comparisons with the corresponding infection in rat studied previously, revealed structurally different alterations, although occurring as transient events in both species. Both showed an induced blood group-type transferase halfway through the infection (a blood group A transferase in rat) and an induced transferase adding a terminal GalNAc (to a sialic acid- containing epitope in rat) towards the end of the infection. These differences between closely related species suggest rapid evolutionary alterations in glycosyltransferase expression.

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