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Osteopontin regulates type I collagen fibril formation in bone tissue

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Title: Osteopontin regulates type I collagen fibril formation in bone tissue
Authors: Depalle, B
McGilvery, CM
Nobakhti, S
Aldegaither, N
Shefelbine, SJ
Porter, AE
Item Type: Journal Article
Abstract: Osteopontin (OPN) is a non-collagenous protein involved in biomineralization of bone tissue. Beyond its role in biomineralization, we show that osteopontin is essential to the quality of collagen fibrils in bone. Transmission electron microscopy revealed that, in Opn−/− tissue, the organization of the collagen fibrils was highly heterogeneous, more disorganized than WT bone and comprised of regions of both organized and disorganized matrix with a reduced density. The Opn−/− bone tissue also exhibited regions in which the collagen had lost its characteristic fibrillar structure, and the crystals were disorganized. Using nanobeam electron diffraction, we show that damage to structural integrity of collagen fibrils in Opn−/- bone tissue and their organization causes mineral disorganization, which could ultimately affect its mechanical integrity.
Issue Date: 15-Jan-2021
Date of Acceptance: 21-Apr-2020
URI: http://hdl.handle.net/10044/1/78733
DOI: 10.1016/j.actbio.2020.04.040
ISSN: 1742-7061
Publisher: Elsevier BV
Start Page: 194
End Page: 202
Journal / Book Title: Acta Biomaterialia
Volume: 120
Copyright Statement: © 2020 Acta Materialia Inc. Published by Elsevier Ltd. This is an open access article under the CC BY license. (http://creativecommons.org/licenses/by/4.0/)
Sponsor/Funder: Wellcome Trust
Funder's Grant Number: 097347/C/11/Z
Keywords: Bone
Collagen
Mineralization
Non-collagenous proteins
Osteopontin
Scanning electron nano beam diffraction
Biomedical Engineering
Publication Status: Published
Online Publication Date: 2020-04-25
Appears in Collections:Materials
Faculty of Natural Sciences
Faculty of Engineering



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