Show simple item record

dc.contributor.authorBruno, Lucila Santosen_US
dc.date.accessioned2019-12-16T15:46:22Z
dc.date.available2019-12-16T15:46:22Z
dc.date.issued2004
dc.date.submitted2004
dc.identifier.other(OCoLC)57409387
dc.identifier.otherb25360735
dc.identifier.urihttps://hdl.handle.net/2144/38845
dc.descriptionPLEASE NOTE: This work is protected by copyright. Downloading is restricted to the BU community: please click Download and log in with a valid BU account to access. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.en_US
dc.descriptionThesis (D.Sc.)--Boston University, Henry M. Goldman School of Dental Medicine, 2004 (Periodontology and Oral Biology).en_US
dc.descriptionIncludes bibliography (leaves 110-140).en_US
dc.description.abstractSaliva has been long associated with the maintenance of the oral health. The complex mixture of salivary constituents provides an effective set of systems for lubricating and protecting the soft and hard tissues. Among the salivary constituents responsible for these functions are the mucus glycoproteins. It is generally accepted that mucins in saliva occur in two different molecular weight forms: a low molecular weight (MG2) and a high molecular weight (MG1). MG2 is the low molecular weight monomeric mucin secreted by submandibular, sublingual and minor salivary glands. This mucin has been implicated in the non-immune host defense system in the oralcavity since it binds, agglutinates and exerts direct microbicidal effects on a variety of oral bacteria and fungi. MG2 has been also implicated in the formation of heterotypic complexes with other proteins present in salivary secretions such as secretory IgA and lactoferrin. Interactions between proteins occur in many levels within cells and tissues as welI as in glandular secretions and other body fluids under physiological conditions and might result in modified biological activity. To investigate interactions, a submandibular gland prey library was screened with baits encoding the N- and C-terminal regions of MG2 using the yeast two-hybrid system. The N-terminal region interacted with a group of secretory salivary proteins whereas the C-terminal region did not. Interacting proteins included amylase, acidic proline-rich protein 2, basic proline-rich protein 3, lacrimal proline-rich protein 4, statherin and histatin 1.Formation of complexes between these proteins and the N-terminal region of MG2 was confirmed in Far Western blotting experiments and co-immunoprecipitation studies. These results show that protein-protein interactions occur between mucin and non-mucin proteins in the secretory salivary protein "complexome". Interactions could protect complex partners from proteolysis, modulate the biological activity of complexed proteins or serve as a delivery system for distribution of secretory salivary proteins throughout the oral cavity.en_US
dc.language.isoen_US
dc.publisherBoston Universityen_US
dc.rightsThis work is protected by copyright. Downloading is restricted to the BU community. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.en_US
dc.subjectMucinsen_US
dc.subjectSalivaen_US
dc.titleTwo-hybrid analysis of human salivary mucin MG2 (MUC7) interactionsen_US
dc.typeThesis/Dissertationen_US
etd.degree.nameDoctor of Science in Dentistryen_US
etd.degree.leveldoctoralen_US
etd.degree.disciplinePeriodontology and Oral Biologyen_US
etd.degree.grantorBoston Universityen_US


This item appears in the following Collection(s)

Show simple item record