TY - JOUR
T1 - Effects of non-enzymatic glycation on the micro- and nano-mechanics of articular cartilage
AU - Rahnamay Moshtagh, Parisa
AU - Korthagen, N.
AU - van Rijen, M.H.P.
AU - Castelein, R.M.
AU - Zadpoor, Amir
AU - Weinans, Harrie
PY - 2018
Y1 - 2018
N2 - The mechanical properties of articular cartilage depend on the quality of its matrix, which consists of collagens and glycosaminoglycans (GAGs). The accumulation of advanced glycation end products (AGEs) can greatly affect
the mechanics of cartilage. In the current study, we simulated the accumulation of AGEs by using L-threose to cross-link collagen molecules in the cartilage matrix (in vitro). The resulting changes in the mechanical properties (stiffness) of cartilage are then measured both at the micrometer-scale (using micro-indenter) and nanometer-scale (using indentation-type atomic force microscopy). Non-enzymatic cross-linking within the cartilage matrix was confirmed by the browning of L-threose-treated samples. We observed > 3 times increase in the
micro-scale stiffness and up to 12-fold increase in the nano-scale stiffness of the glycated cartilage in the peak pertaining to the collagen fibers, which is caused by cartilage network embrittlement. At the molecular level, we found that besides the collagen component, the glycation process also influenced the GAG macromolecules.
Comparing cartilage samples before and after L-threose treatment revealed that artificially induced-AGEs also
decelerate in vitro degradation (likely via matrix metalloproteinases), observed at both micro- and nano-scales.
The combined observations suggest that non-enzymatic glycation may play multiple roles in mechanochemical
functioning of articular cartilage
AB - The mechanical properties of articular cartilage depend on the quality of its matrix, which consists of collagens and glycosaminoglycans (GAGs). The accumulation of advanced glycation end products (AGEs) can greatly affect
the mechanics of cartilage. In the current study, we simulated the accumulation of AGEs by using L-threose to cross-link collagen molecules in the cartilage matrix (in vitro). The resulting changes in the mechanical properties (stiffness) of cartilage are then measured both at the micrometer-scale (using micro-indenter) and nanometer-scale (using indentation-type atomic force microscopy). Non-enzymatic cross-linking within the cartilage matrix was confirmed by the browning of L-threose-treated samples. We observed > 3 times increase in the
micro-scale stiffness and up to 12-fold increase in the nano-scale stiffness of the glycated cartilage in the peak pertaining to the collagen fibers, which is caused by cartilage network embrittlement. At the molecular level, we found that besides the collagen component, the glycation process also influenced the GAG macromolecules.
Comparing cartilage samples before and after L-threose treatment revealed that artificially induced-AGEs also
decelerate in vitro degradation (likely via matrix metalloproteinases), observed at both micro- and nano-scales.
The combined observations suggest that non-enzymatic glycation may play multiple roles in mechanochemical
functioning of articular cartilage
U2 - 10.1016/j.jmbbm.2017.09.035
DO - 10.1016/j.jmbbm.2017.09.035
M3 - Article
SN - 1751-6161
VL - 77
SP - 551
EP - 556
JO - Journal of the Mechanical Behavior of Biomedical Materials
JF - Journal of the Mechanical Behavior of Biomedical Materials
ER -