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dc.contributor.advisorPhillips, Charlotte L.eng
dc.contributor.authorBrodeur, Amanda C., 1978-eng
dc.date.issued2006eng
dc.date.submitted2006 Springeng
dc.descriptionTitle from title screen of research.pdf file (viewed on December 22, 2006).eng
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.eng
dc.description"May 2006"eng
dc.descriptionVita.eng
dc.descriptionIncludes bibliographical references.eng
dc.descriptionThesis (Ph. D.) University of Missouri-Columbia 2006.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Biochemistry (Medicine).eng
dc.description.abstractType I collagen is the most abundant structural protein in the body. Type I collagen generally exists as a heterotrimeric protein; however, a homotrimeric isotype of type I collagen has been identified. Our lab currently studies the COL1A2 deficient mouse model which is homozygous for a mutation that causes the mice to synthesize homotrimeric type I collagen exclusively. We recently identified deposition of type I collagen in the kidneys of the COL1A2 deficient mouse model and under normal physiologic conditions such accumulation is pathologic. The primary goal of this research is to investigate the molecular mechanisms involved in the regulation of type I collagen within the kidney by evaluating synthetic and degradative pathways. As presented here, the accumulation of homotrimeric type I collagen in the kidneys of the COL1A2 deficient mice occurs postnatally and appears to be due to an increase in the synthetic pathway, as well as an alteration in the degradative pathway. Gaining a further understanding of the mechanisms behind the deposition of collagen within the kidney will hopefully lead to a greater understanding of secondary renal injury seen in the progression to end-stage renal disease, a complication of a variety diseases, including diabetic and IgA nephropathy. Further, characterization of the role of homotrimeric type I collagen will also lead to a greater understanding of its role in developmental and pathological events.eng
dc.identifier.merlin.b57475180eng
dc.identifier.oclc77524171eng
dc.identifier.otherBrodeurA-041706-D5065eng
dc.identifier.urihttp://hdl.handle.net/10355/4479eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcollectionUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations.eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2006 Dissertationseng
dc.source.originalSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subject.lcshKidney glomerulus -- Diseaseseng
dc.subject.lcshCytoskeletal proteinseng
dc.subject.meshCollagen Type I -- metabolismeng
dc.subject.meshKidney Glomerulus -- pathologyeng
dc.subject.meshMice, Mutant Strainseng
dc.subject.meshOsteogenesis Imperfecta -- geneticseng
dc.subject.meshOsteogenesis Imperfecta -- pathologyeng
dc.titleGlomerular deposition of homotrimeric type I collagen in the COL1A2 deficient mouseeng
dc.typeThesiseng
thesis.degree.disciplineBiochemistry (Medicine) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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