Imperial College London
Alternate

ProfessorAlexandraPorter

Faculty of Engineering, Department of Materials

Professor of Bio-imaging and Analysis
 
 
 
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Contact

 

+44 (0)20 7594 9691a.porter

 
 
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Location

 

B341 Royal School of MinesRoyal School of MinesSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Depalle:2021:10.1016/j.actbio.2020.04.040,
author = {Depalle, B and McGilvery, CM and Nobakhti, S and Aldegaither, N and Shefelbine, SJ and Porter, AE},
doi = {10.1016/j.actbio.2020.04.040},
journal = {Acta Biomaterialia},
pages = {194--202},
title = {Osteopontin regulates type I collagen fibril formation in bone tissue},
url = {http://dx.doi.org/10.1016/j.actbio.2020.04.040},
volume = {120},
year = {2021}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Depalle,B
AU  - McGilvery,CM
AU  - Nobakhti,S
AU  - Aldegaither,N
AU  - Shefelbine,SJ
AU  - Porter,AE
DO  - 10.1016/j.actbio.2020.04.040
EP  - 202
PY  - 2021///
SN  - 1742-7061
SP  - 194
TI  - Osteopontin regulates type I collagen fibril formation in bone tissue
T2  - Acta Biomaterialia
UR  - http://dx.doi.org/10.1016/j.actbio.2020.04.040
UR  - https://www.sciencedirect.com/science/article/pii/S1742706120302373?via%3Dihub
UR  - http://hdl.handle.net/10044/1/78733
VL  - 120
ER  -
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