scholarly journals A damage model for collagen fibres with an application to collagenous soft tissues

2020 ◽  
Vol 476 (2236) ◽  
pp. 20190821
Author(s):  
Gerhard A. Holzapfel ◽  
Ray W. Ogden
Keyword(s):  
Soft Tissues ◽  
Damage Model ◽  
Three Dimensional ◽  
Collagen Fibres ◽  
Physiological Loading ◽  
Cross Links ◽  
Complex Boundary ◽  
Tail Tendon ◽  
Similar Basis ◽  
Rat Tail

We propose a mechanical model to account for progressive damage in collagen fibres within fibrous soft tissues. The model has a similar basis to the pseudoelastic model that describes the Mullins effect in rubber but it also accounts for the effect of cross-links between collagen fibres. We show that the model is able to capture experimental data obtained from rat tail tendon fibres, and the combined effect of damage and collagen cross-links is illustrated for a simple shear test. The proposed three-dimensional framework allows a straightforward implementation in finite-element codes, which are needed to analyse more complex boundary-value problems for soft tissues under supra-physiological loading or tissues weakened by disease.

Mechanical properties of collagen fibres: a comparison of reconstituted and rat tail tendon fibres

Biomaterials ◽  
1989 ◽  
Vol 10 (1) ◽  
pp. 38-42 ◽  
Author(s):  
Y.Pedro Kato ◽  
David L. Christiansen ◽  
Rita A. Hahn ◽  
Sheu-Jane Shieh ◽  
Jack D. Goldstein ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibres ◽  
Tail Tendon ◽  
Rat Tail

Physical and Physical-Chemical Heterogeneity of Collagen Fibres from Rat Tail Tendon

Gerontology ◽  
1962 ◽  
Vol 6 (2-3) ◽  
pp. 102-117 ◽  
Author(s):  
M. Chvapil ◽  
Z. Hruza ◽  
Z. Roth
Keyword(s):  
Chemical Heterogeneity ◽  
Collagen Fibres ◽  
Physical Chemical ◽  
Tail Tendon ◽  
Rat Tail

scholarly journals The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo

1971 ◽  
Vol 121 (2) ◽  
pp. 257-259 ◽  
Author(s):  
A. J. Bailey ◽  
Catherine M. Peach
Keyword(s):  
Soft Tissues ◽  
Cross Link ◽  
Collagen Fibres ◽  
Cross Links

Two aldimine bonds have been shown to be present as stabilizing cross-links in intact collagen fibres from soft tissues: dehydrohydroxylysinonorleucine as a major component and dehydrolysinonorleucine being present in trace quantities. In the highly insoluble collagens less dehydrohydroxylysinonorleucine is present but the proportion of dehydrolysinonorleucine increases. In elastin the latter aldimine is reduced in vivo to give a more stable cross-link but no comparable reduction could be detected with either of the aldimines present in collagen.

scholarly journals Validation of an Empirical Damage Model for Aging and in Vivo Injury of the Murine Patellar Tendon

2013 ◽  
Vol 135 (4) ◽  
Author(s):  
Mark R. Buckley ◽  
Andrew A. Dunkman ◽  
Katherine E. Reuther ◽  
Akash Kumar ◽  
Lydia Pathmanathan ◽  
...  
Keyword(s):  
Soft Tissues ◽  
Damage Model ◽  
Damage Parameter ◽  
Post Injury ◽  
Equilibrium Stress ◽  
Physiological Loading ◽  
Age Related ◽  
Injury Group ◽  
Old Mice

While useful models have been proposed to predict the mechanical impact of damage in tendon and other soft tissues, the applicability of these models for describing in vivo injury and age-related degeneration has not been investigated. Therefore, the objective of this study was to develop and validate a simple damage model to predict mechanical alterations in mouse patellar tendons after aging, injury, or healing. To characterize baseline properties, uninjured controls at age 150 days were cyclically loaded across three strain levels and five frequencies. For comparison, damage was induced in mature (120 day-old) mice through either injury or aging. Injured mice were sacrificed at three or six weeks after surgery, while aged mice were sacrificed at either 300 or 570 days old. Changes in mechanical properties (relative to baseline) in the three week post-injury group were assessed and used to develop an empirical damage model based on a simple damage parameter related to the equilibrium stress at a prescribed strain (6%). From the derived model, the viscoelastic properties of the 300 day-old, 570 day-old, and six week post-injury groups were accurately predicted. Across testing conditions, nearly all correlations between predicted and measured parameters were statistically significant and coefficients of determination ranged from R2 = 0.25 to 0.97. Results suggest that the proposed damage model could exploit simple in vivo mechanical measurements to predict how an injured or aged tendon will respond to complex physiological loading regimens.

The Influence of Biological Aging on the Friction of Collagen Fibres from Rat Tail Tendon

Gerontology ◽  
1966 ◽  
Vol 12 (1) ◽  
pp. 1-5 ◽  
Author(s):  
D.P. Goverdham Rao ◽  
N. Ramanathan
Keyword(s):  
Biological Aging ◽  
Collagen Fibres ◽  
Tail Tendon ◽  
Rat Tail

The Effects of Irradiation with High Energy Electrons on the Structure and Reactivity of Native and Cross-Linked Collagen Fibres

1970 ◽  
Vol 7 (2) ◽  
pp. 387-405
Author(s):  
R. A. GRANT ◽  
R. W. COX ◽  
C. M. KENT
Keyword(s):  
Maximum Dose ◽  
High Energy ◽  
Hot Water ◽  
Collagen Fibres ◽  
High Energy Electrons ◽  
Staining Techniques ◽  
Tail Tendon ◽  
Polypeptide Chains ◽  
Rat Tail ◽  
Tendon Collagen

Native and cross-linked rat tail tendon collagen was irradiated with high energy electrons up to a maximum dose of 100x104 J kg-1 (100Mrd). Fibres irradiated dry showed greater damage when examined in the electron microscope using negative staining techniques than those irradiated wet. Cross-linking with glutaraldehyde prior to irradiation resulted in the band structure being preserved even at the highest dose but an unequal shrinkage of the bands was noted. Irradiation altered the reactivity of both native and cross-linked collagen with collagenase and elastase. Wet- but not dry-irradiated native collagen became resistant to collagenase. Both wet- and dry-irradiated specimens were digested with elastase. Cross-linked collagen, normally resistant to both elastase and collagenase, became sensitive after varying doses of radiation; different results were obtained after irradiation in the wet and dry states. Irradiated collagen reacted abnormally with various histological stains and tended to resemble elastin in tinctorial properties. No marked changes were noted in the amino acid composition of the collagen after irradiation. Solubility in dilute alkali, acetic acid and hot water was decreased after irradiation of collagen in the wet state and increased after irradiation in the dry state. The results were consistent with the hypothesis that electron irradiation of collagen in the dry state results in scission of the polypeptide chains and that, in the presence of water, this is accompanied by the formation of intermolecular bonds. It also appears that changes in the configuration of the polypeptide chains accompany both these processes.

Dietary, Caging and Temperature Factors in the Ageing of Collagen Fibres in Rat Tail Tendon

Gerontology ◽  
1981 ◽  
Vol 27 (1-2) ◽  
pp. 37-41 ◽  
Author(s):  
Arthur V. Everitt ◽  
Barbara D. Porter ◽  
Matthew Steele
Keyword(s):  
Collagen Fibres ◽  
Tail Tendon ◽  
Temperature Factors ◽  
Rat Tail
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