% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Montanari:619954,
author = {Montanari, Juliette and Schwob, Lucas and Marie-Brasset,
Aurélie and Vinatier, Claire and Lepleux, Charlotte and
Antoine, Rodolphe and Guicheux, Jérôme and Poully,
Jean-Christophe and Chevalier, François},
title = {{P}ilot screening of potential matrikines resulting from
collagen breakages through ionizing radiation},
journal = {Radiation and environmental biophysics},
volume = {63},
number = {3},
issn = {0301-634X},
address = {New York, NY},
publisher = {Springer},
reportid = {PUBDB-2024-08045},
pages = {337-350},
year = {2024},
abstract = {Little is known regarding radiation-induced matrikines and
the possible degradation of extracellular matrix following
therapeutic irradiation. The goal of this study was to
determine if irradiation can cut collagen proteins at
specific sites, inducing potentially biologically active
peptides against cartilage cells. Chondrocytes cultured as
3D models were evaluated for extracellular matrix
production. Bystander molecules were analyzed in vitro in
the conditioned medium of X-irradiated chondrocytes.
Preferential breakage sites were analyzed in collagen
polypeptide by mass spectrometry and resulting peptides were
tested against chondrocytes. 3D models of chondrocytes
displayed a light extracellular matrix able to maintain the
structure. Irradiated and bystander chondrocytes showed a
surprising radiation sensitivity at low doses,
characteristic of the presence of bystander factors,
particularly following 0.1 Gy. The glycine-proline peptidic
bond was observed as a preferential cleavage site and a
possible weakness of the collagen polypeptide after
irradiation. From the 46 collagen peptides analyzed against
chondrocytes culture, 20 peptides induced a reduction of
viability and 5 peptides induced an increase of viability at
the highest concentration between 0.1 and 1 µg/ml. We
conclude that irradiation promoted a site-specific
degradation of collagen. The potentially resulting peptides
induce negative or positive regulations of chondrocyte
growth. Taken together, these results suggest that ionizing
radiation causes a degradation of cartilage proteins,
leading to a functional unbalance of cartilage homeostasis
after exposure, contributing to cartilage dysfunction.},
cin = {FS-BIG},
ddc = {530},
cid = {I:(DE-H253)FS-BIG-20220318},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633)},
pid = {G:(DE-HGF)POF4-633},
experiment = {EXP:(DE-MLZ)External-20140101},
typ = {PUB:(DE-HGF)16},
pubmed = {39115696},
UT = {WOS:001286364200001},
doi = {10.1007/s00411-024-01086-z},
url = {https://bib-pubdb1.desy.de/record/619954},
}