Intestinal mucins from cystic fibrosis mice show increased fucosylation due to an induced Fucalpha1-2 glycosyltransferase.

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Thomsson, Kristina A,1969Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry (author)

Intestinal mucins from cystic fibrosis mice show increased fucosylation due to an induced Fucalpha1-2 glycosyltransferase.

Article/chapterEnglish2002

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2002

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LIBRIS-ID:oai:gup.ub.gu.se/106583
https://gup.ub.gu.se/publication/106583URI
https://doi.org/10.1042/BJ20020371DOI

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Language:English

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Subject category:ref swepub-contenttype
Subject category:art swepub-publicationtype

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In gene-targeted mouse models for cystic fibrosis (CF), the disease is mainly manifested by mucus obstruction in the intestine. To explore the mucus composition, mucins insoluble and soluble in 6 M guanidinium chloride were purified by three rounds of isopycnic ultracentrifugation from the small and large intestines of CF mice (Cftr(m1UNC)/Cftr(m1UNC)) and compared with wild-type mice. The amino acid composition was typical of that for mucins and showed increased amounts of the insoluble (2.5-fold increase) and soluble (7-fold increase) mucins in the small intestine of the CF mice compared with wild-type mice. Mucins from the large intestine of both wild-type and CF mice showed a high but constant level of fucosylation. In contrast, the insoluble and soluble mucins of the small intestine in CF mice revealed a large increase in fucose, whereas those of wild-type mice contained only small amounts of fucose. This increased fucosylation was analysed by releasing the O-linked oligosaccharides followed by GC-MS. NMR spectroscopy revealed that the increased fucosylation was due to an increased expression of blood group H epitopes (Fucalpha1-2Gal-). Northern-blot analysis, using a probe for the murine Fucalpha1-2 fucosyltransferase (Fut2), showed an up-regulation of this mRNA in the small intestine of the CF mice, suggesting that this enzyme is responsible for the observed increase in blood group H-type glycosylation. The reason for this up-regulation could be a direct or indirect effect of a non-functional CF transmembrane conductance regulator (CFTR) caused by the absence of CFTR channel.

Subject headings and genre

MEDICIN OCH HÄLSOVETENSKAP Medicinsk bioteknologi Medicinsk bioteknologi hsv//swe
MEDICAL AND HEALTH SCIENCES Medical Biotechnology Medical Biotechnology hsv//eng
Animals
Blotting
Northern
Chromatography
Gas
Cystic Fibrosis
metabolism
Fucose
metabolism
Glycosyltransferases
metabolism
Intestines
metabolism
Mice
Mucins
chemistry
isolation & purification
metabolism
Nuclear Magnetic Resonance
Biomolecular

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Hinojosa-Kurtzberg, Marina (author)
Axelsson, Karin AGothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry (author)
Domino, Steven E (author)
Lowe, John B (author)
Gendler, Sandra J (author)
Hansson, Gunnar C.,1951Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry(Swepub:gu)xhagun (author)
Göteborgs universitetInstitutionen för medicinsk och fysiologisk kemi (creator_code:org_t)

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In:The Biochemical journal367:Pt 3, s. 609-160264-6021

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