{"id":{"repo_id":"wvu","oai_identifier":"oai:researchrepository.wvu.edu:etd-2271"},"canonical_url":"https://search.dev.ndltd.org/etd/wvu/oai:researchrepository.wvu.edu:etd-2271","repository":{"repo_id":"wvu","name":"West Virginia University","base_url":"https://researchrepository.wvu.edu/do/oai/"},"display":{"title":"Effects of type-I collagen fractional composition and pyridinium crosslink content on cortical bone strength in the human femur","abstract":"Type-I collagen's role in the formation of bone and its inherent strength have been well documented by studies in genetic diseases such as Osteogenesis Imperfecta. Type-I collagen's role in healthy bone, and the changes that occur to collagen during aging, which may eventually lead to osteoporosis, is less understood. Changes that may occur include differences in collagen production and in its processing such as differences in glycosylation and the hydroxylation of specific amino acid residues. Changes in the reducible and non-reducible crosslink content, or changes in the ratio of crosslinks to total collagen may also occur. The present study investigated (1) type-I collagen content in cortical bone from the human femur, (2) the mature, non-reducible pyridinium crosslink content of this bone, and (3) assessed the potential relationships of these findings to fracture resistance and to the age and sex of the bone donor. It was hypothesized that higher amounts of type-I collagen and pyridinium crosslinks per dry weight of bone would correspond to increased force required for fracture. (Abstract shortened by UMI.).","abstract_html":"Type-I collagen's role in the formation of bone and its inherent strength have been well documented by studies in genetic diseases such as Osteogenesis Imperfecta. Type-I collagen's role in healthy bone, and the changes that occur to collagen during aging, which may eventually lead to osteoporosis, is less understood. Changes that may occur include differences in collagen production and in its processing such as differences in glycosylation and the hydroxylation of specific amino acid residues. Changes in the reducible and non-reducible crosslink content, or changes in the ratio of crosslinks to total collagen may also occur. The present study investigated (1) type-I collagen content in cortical bone from the human femur, (2) the mature, non-reducible pyridinium crosslink content of this bone, and (3) assessed the potential relationships of these findings to fracture resistance and to the age and sex of the bone donor. It was hypothesized that higher amounts of type-I collagen and pyridinium crosslinks per dry weight of bone would correspond to increased force required for fracture. (Abstract shortened by UMI.).","abstract_has_math":false,"creators":["Rice, Michael Blair"],"institution":null,"degree_name":"MS","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Phil Keeting."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2001,"date_issued":"2001-05-01T07:00:00Z","date_published":"2001-05-01T07:00:00Z","updated_at":"2026-07-24T06:15:31Z","subjects":["Molecular biology","Cellular biology","Developmental biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://researchrepository.wvu.edu/etd/1268"],"render_values":[{"text":"https://researchrepository.wvu.edu/etd/1268","href":"https://researchrepository.wvu.edu/etd/1268","code":true}]}]},"links":{"outbound_url":"https://doi.org/10.33915/etd.1268","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Phil Keeting."]},{"key":"dc:creator","label":"Author","values":["Rice, Michael Blair"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2019-01-17T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["MS"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Molecular biology","Cellular biology","Developmental biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://doi.org/10.33915/etd.1268","https://researchrepository.wvu.edu/etd/1268"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Type-I collagen's role in the formation of bone and its inherent strength have been well documented by studies in genetic diseases such as Osteogenesis Imperfecta. Type-I collagen's role in healthy bone, and the changes that occur to collagen during aging, which may eventually lead to osteoporosis, is less understood. Changes that may occur include differences in collagen production and in its processing such as differences in glycosylation and the hydroxylation of specific amino acid residues. Changes in the reducible and non-reducible crosslink content, or changes in the ratio of crosslinks to total collagen may also occur. The present study investigated (1) type-I collagen content in cortical bone from the human femur, (2) the mature, non-reducible pyridinium crosslink content of this bone, and (3) assessed the potential relationships of these findings to fracture resistance and to the age and sex of the bone donor. It was hypothesized that higher amounts of type-I collagen and pyridinium crosslinks per dry weight of bone would correspond to increased force required for fracture. (Abstract shortened by UMI.)."]},{"key":"dc:title","label":"Title","values":["Effects of type-I collagen fractional composition and pyridinium crosslink content on cortical bone strength in the human femur"]}]}],"canonical_facts":{"dc:contributor":["Phil Keeting."],"dc:creator":["Rice, Michael Blair"],"dc:date.available":["2019-01-17T08:00:00Z"],"dc:description.abstract":["Type-I collagen's role in the formation of bone and its inherent strength have been well documented by studies in genetic diseases such as Osteogenesis Imperfecta. Type-I collagen's role in healthy bone, and the changes that occur to collagen during aging, which may eventually lead to osteoporosis, is less understood. Changes that may occur include differences in collagen production and in its processing such as differences in glycosylation and the hydroxylation of specific amino acid residues. Changes in the reducible and non-reducible crosslink content, or changes in the ratio of crosslinks to total collagen may also occur. The present study investigated (1) type-I collagen content in cortical bone from the human femur, (2) the mature, non-reducible pyridinium crosslink content of this bone, and (3) assessed the potential relationships of these findings to fracture resistance and to the age and sex of the bone donor. It was hypothesized that higher amounts of type-I collagen and pyridinium crosslinks per dry weight of bone would correspond to increased force required for fracture. (Abstract shortened by UMI.)."],"dc:identifier":["https://doi.org/10.33915/etd.1268","https://researchrepository.wvu.edu/etd/1268"],"dc:subject":["Molecular biology","Cellular biology","Developmental biology"],"dc:title":["Effects of type-I collagen fractional composition and pyridinium crosslink content on cortical bone strength in the human femur"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["MS"]},"updated_at":"2026-07-24T06:15:31Z"}