Osteopontin regulates type I collagen fibril formation in bone tissue
File(s)
Published version
Author(s)
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.
Date Issued
2021-01-15
Date Acceptance
2020-04-21
Citation
Acta Biomaterialia, 2021, 120, pp.194-202
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/)
License URL
Sponsor
Wellcome Trust
Identifier
https://www.sciencedirect.com/science/article/pii/S1742706120302373?via%3Dihub
Grant Number
097347/C/11/Z
Subjects
Bone
Collagen
Mineralization
Non-collagenous proteins
Osteopontin
Scanning electron nano beam diffraction
Biomedical Engineering
Publication Status
Published
Date Publish Online
2020-04-25