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dc.contributor.authorNagao, Kiyokoen_US
dc.date.accessioned2020-03-04T16:43:29Z
dc.date.available2020-03-04T16:43:29Z
dc.date.issued2006
dc.date.submitted2006
dc.identifier.other(OCoLC)71226043
dc.identifier.otherb26863716
dc.identifier.urihttps://hdl.handle.net/2144/39689
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 (MSD) -- Boston University Goldman School of Dental Medicine (Orthodontics and Oral Biology)en_US
dc.descriptionIncludes bibliographical references : leaves 54-68.en_US
dc.description.abstractType 1 diabetes is associated with several pathological complications. Diabetic bone disease is one of them which consists of weak bones, low bone turnover osteopenia, and low bone density. Advanced glycation end products (AGEs) are believed to contribute to these complications which are caused by elevated serum glucose levels. However, it is not clear how AGEs cause osteopenia, which factors induce osteopenia,and what biological processes might be regulated by AGEs. The hypothesis of this research is that AGEs inhibit osteoblast function and contribute to inhibited bone healing and formation in type 1 diabetes. To examine this hypothesis, we used N[epsilon]-(carboxymethyl) lysine modified collagen (CML-collagen) as a known AGE. We show that CML-collagen inhibits in vitro bone formation as determined by measurements of calcium deposition by primary osteoblast cultures grown on pre-coated CML-collagen or control collagen plates. The results indicated that cells grown on CML-collagen deposit less calcium compared to control-collagen. Then we carried out DNA microarray analysis in order to know which genes were regulated by growth on CML-collagen. We found that Ras oncogene family member Rab7, integrin-binding sialoprotein (bone sialoprotein 1), and dimethylarginine dimethylaminohydrolase 1 were up regulated by CML-collagen. 3-hydroxy-3-methylglutaryl-Coenzyme A reductase (HMG-CoA), cartilage oligomeric matrix protein (Comp), and protocadherin beta 4 precursor were down regulated by CML-collagen.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.subjectBone diseases, metabolicen_US
dc.subjectDiabetes mellitus, type 1en_US
dc.subjectGlycosylation end products, advanceden_US
dc.subjectIntramolecular lyasesen_US
dc.titleEffects of advanced glycation end products on osteoblastic cellsen_US
dc.typeThesis/Dissertationen_US
etd.degree.nameMaster of Science in Dentistryen_US
etd.degree.levelmastersen_US
etd.degree.disciplineOrthodontics and Oral Biologyen_US
etd.degree.grantorBoston Universityen_US


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