Non-destructive detection of matrix stabilization correlates with enhanced mechanical properties of self-assembled articular cartilage.
Amino Acid Oxidoreductases
/ pharmacology
Animals
Biomechanical Phenomena
Cartilage, Articular
/ drug effects
Cattle
Collagen
/ metabolism
Compressive Strength
Cross-Linking Reagents
/ chemistry
Extracellular Matrix
/ drug effects
Extracellular Matrix Proteins
/ pharmacology
Humans
Proteoglycans
/ pharmacology
Support Vector Machine
Tensile Strength
Tissue Engineering
Tissue Scaffolds
/ chemistry
autofluorescence
biomechanics
cartilage
imaging
non-destructive monitoring
tissue engineering
Journal
Journal of tissue engineering and regenerative medicine
ISSN: 1932-7005
Titre abrégé: J Tissue Eng Regen Med
Pays: England
ID NLM: 101308490
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
08
03
2018
revised:
05
12
2018
accepted:
13
02
2019
pubmed:
17
2
2019
medline:
17
4
2020
entrez:
17
2
2019
Statut:
ppublish
Résumé
Tissue engineers rely on expensive, time-consuming, and destructive techniques to monitor the composition, microstructure, and function of engineered tissue equivalents. A non-destructive solution to monitor tissue quality and maturation would greatly reduce costs and accelerate the development of tissue-engineered products. The objectives of this study were to (a) determine whether matrix stabilization with exogenous lysyl oxidase-like protein-2 (LOXL2) with recombinant hyaluronan and proteoglycan link protein-1 (LINK) would result in increased compressive and tensile properties in self-assembled articular cartilage constructs, (b) evaluate whether label-free, non-destructive fluorescence lifetime imaging (FLIm) could be used to infer changes in both biochemical composition and biomechanical properties, (c) form quantitative relationships between destructive and non-destructive measurements to determine whether the strength of these correlations is sufficient to replace destructive testing methods, and (d) determine whether support vector machine (SVM) learning can predict LOXL2-induced collagen crosslinking. The combination of exogenous LOXL2 and LINK proteins created a synergistic 4.9-fold increase in collagen crosslinking density and an 8.3-fold increase in tensile strength as compared with control (CTL). Compressive relaxation modulus was increased 5.9-fold with addition of LOXL2 and 3.4-fold with combined treatments over CTL. FLIm parameters had strong and significant correlations with tensile properties (R
Identifiants
pubmed: 30770656
doi: 10.1002/term.2824
pmc: PMC6461514
mid: NIHMS1013059
doi:
Substances chimiques
Cross-Linking Reagents
0
Extracellular Matrix Proteins
0
Proteoglycans
0
link protein
0
Collagen
9007-34-5
Amino Acid Oxidoreductases
EC 1.4.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
637-648Subventions
Organisme : NIAMS NIH HHS
ID : R01 AR067821
Pays : United States
Organisme : NIH HHS
ID : R01AR067821
Pays : United States
Organisme : California Institute for Regenerative Medicine
ID : RT3-07981
Pays : International
Informations de copyright
© 2019 John Wiley & Sons, Ltd.
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