In vivo and in vitro aging of collagen examined using an isometric melting technique

Mitchell, Thomas W.; Rigby, B.J.

doi:10.1016/0005-2795(75)90080-x

Cited by 30 publications

(11 citation statements)

References 3 publications

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“…Thermal denaturation of collagenous structures occurs when heating induces "melting" of the helically confined collagen molecule (15). With the apparatus described above, the contraction that occurs when the molecules randomize registers as an S. C .…”

Section: Discussionmentioning

confidence: 99%

Collagen Cross‐Linking and Resorption: Effect of Glutaraldehyde Concentration

1990

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Cross-linked collagen bioprostheses usually are designed to be inert and nonresorbable, resulting in fatigue and wear failure in high-stress environments. Eventual replacement of the implant, although minimizing strength loss during resorption, would result in a graft with reparative ability. Kangaroo tail tendon (KTT) partially cross-linked with glutaraldehyde (GA) was evaluated in vitro for resistance to bacterial collagenase digestion and in vivo for biocompatibility and resorbability in an intramuscular implant assay. Cross-linking was quantified by thermal denaturation studies. Incomplete cross-linking was achieved with concentrations of GA less than 0.1% (w/v). KTT cross-linked in greater than or equal to 0.05% GA were collagenase resistant being incompletely digested after 240 h. Cross-linking of KTT with low concentrations of GA resulted in partial collagenase resistance and slowed resorption.

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Section: Discussionmentioning

confidence: 99%

Collagen Cross‐Linking and Resorption: Effect of Glutaraldehyde Concentration

1990

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“…14 This thermally induced structural transition shows itself as the so-called collagen shrinkage phenomenon in which, if collagen is heated slowly, it contracts 15,16 at a certain temperature or, if it is held at a constant length, it develops a contractile force. 17,18 The shrinkage behavior is indicative of the overall condition of the crosslinks in the collagen network and the stability they induce. 19 The technique has proved valuable in assessing the efficiency and density of artificially induced intermolecular crosslinks, produced by various chemical tanning agents, on a number of tissues.…”

Section: Collagen's Thermal Stabilitymentioning

confidence: 99%

The role of collagen in the declining mechanical properties of aging human cortical bone

Zioupos

Currey

Hamer

1999

J. Biomed. Mater. Res.

318

153

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The importance of the mechanical role of collagen in bone is becoming increasingly more clear as evidence mounts on the detrimental effects of altered collagen on the mechanical properties of bone. We previously examined a set of mechanical properties (material stiffness, strength, and toughness) of human femoral bone (ages 35-92) and found that a gradual deterioration in these properties occurs with age. The present study examines the collagen of the same specimens and relates the collagen properties to the mechanical ones. In the collagen we measured the concentration of stable mature crosslinks, the shrinkage temperature, and the rate of contraction during isometric heating. The changes in the concentration of mature (pyridinium and deoxypyridinium) crosslinks showed no clear relationship to age nor did they correlate with the mechanical properties. The shrinkage temperature declined with age and correlated with a bone's toughness. The maximum rate of contraction was strongly correlated with three different measures of tissue toughness, but much less to stiffness and strength. Our results reinforce speculation regarding the toughening role of collagen in bone mechanics and suggest that the fragility of aging bone may be related to collagen changes.

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“…This may explain the dramatic decrease of biomechanical values after cooking for both types of birds. In cooked tendons, higher biomechanical values observed in LR birds indicate that they are better able to resist heat denaturation probably because of a higher level of collagen inter-molecular cross-linking normally associated with older age and higher level of physical activity (Sinex, 1964;Davison and Patel, 1975;Mitchell and Rigby, 1975).…”

Section: Discussionmentioning

confidence: 99%

Biochemical and biomechanical properties of tendons in two commercial types of chickens

Moussa

Babile

Fernández

et al. 2007

Animal

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The quality of the attachment of meat to bone is often reported to be insufficient by more and more poultry's consumers. This is particularly true for thigh meat in broilers. The aim of this study was to compare muscle to bone attachment (namely, tendons) from a biomechanical and a biochemical point of view in 50 standard (S) and 50 Label Rouge (LR) chickens. Carcasses weighted around 1.7 kg in the two groups. Two tendons were harvested and proceeded for passive stretch tests, prior to cooking or not, to determine main mechanical characteristics (maximum load, stiffness and longitudinal strain). Biochemical parameters such as dry matter percentage, total collagen content, collagen solubility and sulphated glycosaminoglycans (sGAGs) content were also determined. Results showed that biomechanical values differ largely between the two studied tendons. For a given tendon, the values were also different between the two groups of chickens mainly after cooking. The results clearly showed that, mainly after cooking, the mechanical resistance of tendon to stretch was better in LR than in S chickens. LR chickens were reported to have tendons with higher collagen and sGAGs contents associated with a lower collagen solubility. These differences may explain biomechanical differences observed for the two types of tendons and could be due to increased age and/or higher physical activity of LR chickens.

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In vivo and in vitro aging of collagen examined using an isometric melting technique

Cited by 30 publications

References 3 publications

Collagen Cross‐Linking and Resorption: Effect of Glutaraldehyde Concentration

Collagen Cross‐Linking and Resorption: Effect of Glutaraldehyde Concentration

The role of collagen in the declining mechanical properties of aging human cortical bone

Biochemical and biomechanical properties of tendons in two commercial types of chickens

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