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You searched for subject:(Nippostrongylus brasiliensis infection). Showing records 1 – 3 of 3 total matches.

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University of Gothenburg / Göteborgs Universitet

1. Karlsson, Niclas 1966-. Glycosylation of intestinal mucins in health and disease.

Degree: 1997, University of Gothenburg / Göteborgs Universitet

The highly glycosylated proteins found on mucosal surfaces, the mucins, are heterogeneous glycosylated molecules. The mucin oligosaccharides are mainly of the O-linked type, that is linked to the oxygen of serine or threonine, even though also N-linked oligosaccharides (linked to aspargine) may be found. The mucins glycosylation is believed to be important for the protection of mucosal surfaces, and perhaps to modify the physical properties of the mucus. The fundamental knowledge of how mucins are constructed should increase the understanding both of the physiological function and its macroscopic and biochemical properties. This knowledge should give new insights into mucosal related diseases, like chronic bronchitis and cystic fibrosis.In order to characterize intestinal mucins with respect to their glycosylation, oligosaccharides were released and studied mainly by mass spectrometry. A method was developed for further sub-fractionation of released oligosaccharides into neutral, sialylated and sulphated species, based upon their chemical properties. Gas chromatography-mass spectrometry (GC-MS) was adopted for the neutral and sialylated species, while tandem mass spectrometry was used for the sulphated species. Chemical derivatization preceding the mass spectrometric characterization increased the volatility for analysing oligosaccharides with GC-MS, and increased the ionization efficiency for analysing with tandem mass spectrometry. Proton-NMR was used to characterize individual oligosaccharides isolated by high performance-liquid chromatography (HPLC). Monosaccharide composition was analysed by HPLC or GC. Immunological as well as lectin assays were used for the characterization of both mucin oligosaccharides and mucin protein backbone. The expression of mucins and glycosyltransferases were detected using Northern blotting, and the latter was also identified by in vitro enzyme assays.The main impression from the presented data was the complexity of the intestinal mucin glycosylation. Comparison of pig and rat small intestinal mucin oligosaccharides illustrated a species dependent glycosylation. The most obvious difference was among the sialylated oligosaccharides, showing a sialylation pathway in the pig small intestine (sialylation of the 6-position of the polypeptide linked N-acetylgalactosamine), almost absent in the rat small intestine.When analysing the glycosylation of a single intestinal mucin (Muc2) from different rat strains and tissues (small and large intestine), a tissue and individual dependent glycosylation could be found. These differences were due to the presence or absence of blood group related oligosaccharide antigens (blood group A- and Sda/Cad-like antigens). The modification of oligosaccharides by sulphation were found to be similar both between species (rats and pigs) and tissues (small and large intestine).Investigation of how a parasitic infection (Nippostrongylus brasiliensis) influenced the oligosaccharide expression on the rat small intestinal Muc2 mucin showed that the glycosylation was…

Subjects/Keywords: Mucins; glycosylation; oligosaccharides; Muc2; mass spectrometry; Nippostrongylus brasiliensis infection; pig; rat

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Karlsson, N. 1. (1997). Glycosylation of intestinal mucins in health and disease. (Thesis). University of Gothenburg / Göteborgs Universitet. Retrieved from http://hdl.handle.net/2077/12198

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Karlsson, Niclas 1966-. “Glycosylation of intestinal mucins in health and disease.” 1997. Thesis, University of Gothenburg / Göteborgs Universitet. Accessed January 18, 2020. http://hdl.handle.net/2077/12198.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Karlsson, Niclas 1966-. “Glycosylation of intestinal mucins in health and disease.” 1997. Web. 18 Jan 2020.

Vancouver:

Karlsson N1. Glycosylation of intestinal mucins in health and disease. [Internet] [Thesis]. University of Gothenburg / Göteborgs Universitet; 1997. [cited 2020 Jan 18]. Available from: http://hdl.handle.net/2077/12198.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Karlsson N1. Glycosylation of intestinal mucins in health and disease. [Thesis]. University of Gothenburg / Göteborgs Universitet; 1997. Available from: http://hdl.handle.net/2077/12198

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Gothenburg / Göteborgs Universitet

2. Olson, Fredrik 1975-. Alterations of mucin O-glycosylation in response to intestinal infection. Importance of specific glycosyltransferases.

Degree: 2002, University of Gothenburg / Göteborgs Universitet

Mucins are large glycoproteins constituting the major protein component of the mucus layer covering the epithelial surfaces. The mucins are characterised by a dense and heterogeneous O-glycosylation, important for their chemical and physiological properties. The mucus layer forms a selective physical barrier serving to protect the epithelium from physical and chemical stress. With their heterogeneous glycosylation, the mucins probably have a role in the interplay with microbes dwelling at the epithelia, by constituting the targets for microbial adhesins. An increased understanding of mucin O-glycosylation and its biosynthesis would aid in exploring the mechanisms and occurrence of such an interplay.We have studied the O-glycosylation of rat small intestinal mucins, mainly Muc2, during an infection with the parasitic nematode Nippostrongylus brasiliensis. Mucins were collected from the rats at different stages of the infection, and oligosaccharides were released from the protein backbone and separated into neutral, sialylated and sulphated species. The oligosaccharides were structurally analysed, using gas chromatography-mass spectrometry, NMR and high pH anion exchange chromatography. The comparison of the oligosaccharides from normal and infected rats revealed three specific alterations appearing transiently during the infection, indicating a dynamic regulation of mucin O-glycosylation. The alterations were 1) an increased amount of N-acetylneuraminic acid relative to N-glycolylneuraminic acid, 2) the appearance of blood group A terminal epitopes and 3) the appearance of blood group Sda/Cad terminal epitopes. The enzymes responsible for the two first alterations were by northern blotting identified as the CMP-NeuAc hydroxylase and the blood group A GalNAc-transferase, respectively. The rat blood group A glycosyltransferase was cloned and sequenced at the genomic and cDNA levels. The gene was mapped to chromosome 3q11-12 by fluorescence in-situ hybridisation and radiation hybrid mapping. During the cDNA cloning, two similar sequences with 95 percent similarity were identified, both encoding active transferases. By PCR studies on inbred, outbred and interbred rats, the two sequences were shown to be allelic. The unusually large difference between the alleles might indicate an evolutionary pressure in favour of a high mutation frequency for this gene.An aspect of mucin glycosylation that has been difficult to address is the glycosylation of specific O-glycan sites, partly due to the large number of such sites in the mucins. As a step towards such an analysis, a short recombinant reporter protein was constructed, based on sequence from the glycosylated domain of MUC1 and containing only eight O-glycan sites. When this protein was produced in CHO K1 cells, the major oligosaccharides present were mono- and disialylated core 1 glycans, as determined by liquid chromatography-electrospray ionisation-mass spectrometry (LC-ESI-MS) and LC-ESI-MS/MS on released oligosaccharides. N-terminal peptide sequencing showed that all…

Subjects/Keywords: mucins; altered O-glycosylation; Nippostrongylus brasiliensis infection; blood group A glycosyltransferase; Muc2; MUC1; GalNAc-T4; mass spectrometry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Olson, F. 1. (2002). Alterations of mucin O-glycosylation in response to intestinal infection. Importance of specific glycosyltransferases. (Thesis). University of Gothenburg / Göteborgs Universitet. Retrieved from http://hdl.handle.net/2077/15687

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Olson, Fredrik 1975-. “Alterations of mucin O-glycosylation in response to intestinal infection. Importance of specific glycosyltransferases.” 2002. Thesis, University of Gothenburg / Göteborgs Universitet. Accessed January 18, 2020. http://hdl.handle.net/2077/15687.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Olson, Fredrik 1975-. “Alterations of mucin O-glycosylation in response to intestinal infection. Importance of specific glycosyltransferases.” 2002. Web. 18 Jan 2020.

Vancouver:

Olson F1. Alterations of mucin O-glycosylation in response to intestinal infection. Importance of specific glycosyltransferases. [Internet] [Thesis]. University of Gothenburg / Göteborgs Universitet; 2002. [cited 2020 Jan 18]. Available from: http://hdl.handle.net/2077/15687.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Olson F1. Alterations of mucin O-glycosylation in response to intestinal infection. Importance of specific glycosyltransferases. [Thesis]. University of Gothenburg / Göteborgs Universitet; 2002. Available from: http://hdl.handle.net/2077/15687

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Gothenburg / Göteborgs Universitet

3. Holmén Larsson, Jessica M. 1971-. O-glycosylation of intestinal and respiratory mucins in health and disease.

Degree: 2006, University of Gothenburg / Göteborgs Universitet

Mucins are large glycoproteins with a diverse O-glycosylation constituting up to 80% of the total mucin mass. The mucus layer covering the epithelial cells of the gastrointestinal and respiratory tract is largely made up of gel-forming mucins. MUC2 is the main gel-forming mucin in the intestinal tract and its O-glycosylation has been studied in health and disease in this thesis. Glycosylation alterations in relation to infection/inflammation in diseases affecting the mucosa as Cystic Fibrosis and Ulcerative colitis, have been identified. The glycosylation of mouse small intestinal mucins was studied during an infection cycle induced by the parasite Nippostrongylus brasiliensis. The O-linked oligosaccharides were released from the guanidinium chloride insoluble mucins and structurally characterized by gas chromatography/mass spectrometry. Two oligosaccharides containing blood group H-type epitopes (Fuc Ñ1-2Gal-) were transiently expressed with a peak at day 6. Northern blot analysis on total RNA showed a transient expression at day 4-6 of the Fut2 gene encoding the Fuc Ñ1-2 fucosyltransferase synthesizing the H-epitope. Additional oligosaccharides with the common structure HexNAc-Gal-3GalNAcol were transiently expressed with a peak at day 10. Secretor-negative women have an increased risk for recurrent vaginitis caused by C. albicans. A model of this disease is the Fut2-LacZ-null mice lacking the Fut2 enzyme. The aim of the study was to determine if the lack of Fut2 affected the glycosylation of mucins in the gastrointestinal tract. Mass spectrometry showed a complete loss of terminal fucosylation on the O-linked oligosaccharides of the colonic insoluble mucins in the mutant mice. Inoculation by gastric lavage with C. albicans showed no differences in colonization between mouse genotypes. The results suggest that the increased risk of recurrent vaginitis in secretor negative women, is not due to less intestinal colonization.There has been a long time controversy in Cystic Fibrosis (CF) research regarding the observed changes in mucin glycosylation. Are they due to an absent CFTR channel or secondary effects due to infection/ inflammation? We addressed this question by studying mucins secreted by non-infected second passage primary human bronchial epithelial (HBE) cell cultures. The O-linked oligosaccharides, released from purified non-CF and CF mucins, showed large inividual variations, but no significant differences between the two groups. To conclude, no differences in the mucin O-glycan repertoire was found, suggesting that observed CF glycosylation alterations are due to infection/inflammation. Novel proteomic and glycoproteomic methods were used to study sigmoid colon biopsies from active and inactive ulcerative colitis patients and compared to controls. In a total of 50 patients, the monomeric form of MUC2 was semiquantified and 5-10-fold individual differences in MUC2 amounts were observed. The O-glycosylation of colonic MUC2 was studied with a high sensitivity nanoLC/MS setup, developed in-house. More than 50…

Subjects/Keywords: Mucins; oligosaccharide; O-linked glycosylation; mass spectrometry; MUC2; Fut2 enzyme; Nippostrongylus brasiliensis infection; Cystic Fibrosis; Ulcerative colitis

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Holmén Larsson, J. M. 1. (2006). O-glycosylation of intestinal and respiratory mucins in health and disease. (Thesis). University of Gothenburg / Göteborgs Universitet. Retrieved from http://hdl.handle.net/2077/16931

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Holmén Larsson, Jessica M 1971-. “O-glycosylation of intestinal and respiratory mucins in health and disease.” 2006. Thesis, University of Gothenburg / Göteborgs Universitet. Accessed January 18, 2020. http://hdl.handle.net/2077/16931.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Holmén Larsson, Jessica M 1971-. “O-glycosylation of intestinal and respiratory mucins in health and disease.” 2006. Web. 18 Jan 2020.

Vancouver:

Holmén Larsson JM1. O-glycosylation of intestinal and respiratory mucins in health and disease. [Internet] [Thesis]. University of Gothenburg / Göteborgs Universitet; 2006. [cited 2020 Jan 18]. Available from: http://hdl.handle.net/2077/16931.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Holmén Larsson JM1. O-glycosylation of intestinal and respiratory mucins in health and disease. [Thesis]. University of Gothenburg / Göteborgs Universitet; 2006. Available from: http://hdl.handle.net/2077/16931

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.