Studies of the role(s) of galectin in quail intestinal mucin organization and secretion

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dc.contributor.advisorCeri, Howard
dc.contributor.authorFang, Rixun
dc.date.accessioned2005-07-29T23:08:38Z
dc.date.available2005-07-29T23:08:38Z
dc.date.issued1994
dc.descriptionBibliography: p. 251-271.en
dc.description.abstractA program of studies was undertaken to explore the role(s) played by galectins at the mucosal surface. The first phase of this project involved purification and characterization of intestinal galectins from rabbit, rat, and quail. A family of galectins were found in mammalian intestinal tissues, however, only a single galectin was identified from the quail. In the second stage of this project, quail intestinal mucin was purified and the biochemical and immunological properties were characterized. Quail mucin was purified by two sequential isopycnic density-gradient centrifugations in CsCl followed by gel filtration chromatography. Purified quail mucin was then characterized by SDS-PAGE, amino acid and carbohydrate composition analyses, immuno-cross reactivity with mammalian mucin antibodies and sensitivity to disulphide-reduction, H2O2 , and trypsin. Quail mucin was revealed to be high molecular weight polymer composed of large heterogeneous glycoprotein monomers and a 110 kD 'link' protein, held together by disulphide bonds. Quail mucin was further identified as a putative ligand for quail galectin in binding studies and through immunohistochemical co-localization in goblet cells. The quail galectin binds quail mucin through the B-galactose residues on the carbohydrate side chains of quail mucin as shown by hapten inhibition studies. A putative membrane receptor of quail galectin on the brush border membrane of the quail small intestine was also detected by radioactive ligand binding assays. The regulation of mucin secretion from the quail small intestine was investigated using in vitro organ culture. Mucin secretion was enhanced by cholera toxin and regulated in a similar fashion to mammalian mucin; being stimulated by cholinergic but not adrenergic stimuli and being sensitive to the activation of protein kinase C and changes in Ca2 + levels. Quail galectin seems to serve as an adhesion molecule for extracellular mucus gel adherence to the epithelial surfaces and maybe also serve as a control for mucin release, which is evidenced by the following discoveries: (1) lactose could release both quail galectin and quail mucin from intestinal tissue; (2) blocking of galectin binding to the mucosal surfaces with antiserum against quail galectin could induce quail mucin release; and (3) binding the mucosal receptors for quail galectin with plant lectins could specifically reduce the rate of baseline secretion of quail mucin. However, lactose-induced mucin release was independent of the muscarinic receptor, protein kinase C and Ca2 +, suggesting that quail galectin may control mucin release through a unique pathway.en
dc.format.extentxxvii, 271 leaves : ill. ; 30 cm.en
dc.identifier.citationFang, R. (1994). Studies of the role(s) of galectin in quail intestinal mucin organization and secretion (Doctoral thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/12953en_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/12953
dc.identifier.isbn0612030997en
dc.identifier.lccQP 552 L42 F363 1994en
dc.identifier.urihttp://hdl.handle.net/1880/30466
dc.language.isoeng
dc.publisher.institutionUniversity of Calgaryen
dc.publisher.placeCalgaryen
dc.rightsUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.
dc.subject.lccQP 552 L42 F363 1994en
dc.subject.lcshLectins - Research
dc.subject.lcshIntestinal mucosa
dc.subject.lcshMucins
dc.titleStudies of the role(s) of galectin in quail intestinal mucin organization and secretion
dc.typedoctoral thesis
thesis.degree.disciplineBiological Sciences
thesis.degree.grantorUniversity of Calgary
thesis.degree.nameDoctor of Philosophy (PhD)
ucalgary.item.requestcopytrue
ucalgary.thesis.accessionTheses Collection 58.002:Box 971 520538281
ucalgary.thesis.notesoffsiteen
ucalgary.thesis.uarcreleaseyen
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