Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)

Dissertation (MSD) --Boston University, Goldman School of Dental Medicine, 2012 (Department of Oral Biology). === Includes bibliographic references: leaves 71-77. === Lysyl oxidases constitute a family of enzymes responsible for the formation of crosslinks in collagen and elastin. These enzymes have...

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Main Author: Alsofi, Loai Abdulfattah M.
Language:en_US
Published: Boston University 2018
Subjects:
Online Access:https://hdl.handle.net/2144/31296
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spelling ndltd-bu.edu-oai-open.bu.edu-2144-312962019-05-10T15:11:28Z Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II) Alsofi, Loai Abdulfattah M. Bone and bones Enzyme precursors Protein-lysine 6-oxidase Dissertation (MSD) --Boston University, Goldman School of Dental Medicine, 2012 (Department of Oral Biology). Includes bibliographic references: leaves 71-77. Lysyl oxidases constitute a family of enzymes responsible for the formation of crosslinks in collagen and elastin. These enzymes have also been linked to pathological fibrosis. The importance of collagen in the structural and mechanical properties of bone led us to investigate the hypothesis that the absence of one or more of these enzymes could lead to a significant bone phenotype. This phenotype could resemble osteoporosis or diabetic bone disease. In addition, we tried to overexpress lysyl oxidase proenzyme in vitro. The ability to produce enough amounts of lysyl oxidase proenzyme and the ability to process it and activate it could facilitate the development of drugs that control its activity in pathological fibrosis. [TRUNCATED] 2018-09-18T15:34:03Z 2018-09-18T15:34:03Z 2012 2012 Thesis/Dissertation https://hdl.handle.net/2144/31296 en_US This work is being made available in OpenBU by permission of its author, and is available for research purposes only. All rights are reserved to the author. Boston University
collection NDLTD
language en_US
sources NDLTD
topic Bone and bones
Enzyme precursors
Protein-lysine 6-oxidase
spellingShingle Bone and bones
Enzyme precursors
Protein-lysine 6-oxidase
Alsofi, Loai Abdulfattah M.
Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)
description Dissertation (MSD) --Boston University, Goldman School of Dental Medicine, 2012 (Department of Oral Biology). === Includes bibliographic references: leaves 71-77. === Lysyl oxidases constitute a family of enzymes responsible for the formation of crosslinks in collagen and elastin. These enzymes have also been linked to pathological fibrosis. The importance of collagen in the structural and mechanical properties of bone led us to investigate the hypothesis that the absence of one or more of these enzymes could lead to a significant bone phenotype. This phenotype could resemble osteoporosis or diabetic bone disease. In addition, we tried to overexpress lysyl oxidase proenzyme in vitro. The ability to produce enough amounts of lysyl oxidase proenzyme and the ability to process it and activate it could facilitate the development of drugs that control its activity in pathological fibrosis. [TRUNCATED]
author Alsofi, Loai Abdulfattah M.
author_facet Alsofi, Loai Abdulfattah M.
author_sort Alsofi, Loai Abdulfattah M.
title Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)
title_short Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)
title_full Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)
title_fullStr Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)
title_full_unstemmed Bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (II)
title_sort bone phenotype of lysyl oxidase isoform knockout mice & in vitro expression of lysyl oxidase proenzyme (ii)
publisher Boston University
publishDate 2018
url https://hdl.handle.net/2144/31296
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