Stress-induced molecular rearrangement in tendon collagen

Mosler, E.; Folkhard, W.; Knörzer, E.; Nemetschek-Gansler, H.; Nemetschek, Th.; Koch, Michel H. J.

doi:10.1016/0022-2836(85)90244-x

Cited by 194 publications

(123 citation statements)

References 12 publications

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“…The mechanical behaviour of cross-link-deficient collagen is in this respect somewhat similar to immature collagen, where lower fracture stress and enhanced creep behaviour were also observed (Kastelic & Bear 1980). Combining the wealth of structural and mechanical information available for the collagen fibril, (Hodge & Petruska 1963;Mosler et al 1985;Folkhard et al 1986;Hulmes et al 1995;Fratzl et al 1993Fratzl et al , 1997Sasaki & Odajima 1996;Misof et al 1997;Sasaki et al 1999), the proteoglycan-rich matrix (Scott 1991;Cribb & Scott 1995), as well as the covalent cross-links (Light & Bailey 1982;Eyre et al 1984;Davison 1989;Lees et al 1990;Bailey et al 1998), we propose a simple model for the strain-rate-dependent effects reported in this paper. This model is illustrated in figure 5.…”

Section: Discussionmentioning

confidence: 99%

“…The most probable processes are thought to be the stretching of the collagen triple helices and the cross-links between the helices, implying a side-by-side gliding of neighbouring molecules, leading to structural changes at the level of the collagen fibrils. This has previously been investigated by the use of synchrotron radiation diffraction experiments (Mosler et al 1985;Folkhard et al 1986;Sasaki & Odajima 1996;Fratzl et al 1997;Sasaki et al 1999). By monitoring the structure factors of the second and third order maximum, it was shown that during stretching the length of the gap region was increased with respect to the overlap region, implying a considerable gliding of neighbouring molecules (Folkhard et al 1986;Fratzl et al 1997).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Viscoelastic properties of collagen: synchrotron radiation investigations and structural model

Puxkandl

Zizak

Paris

et al. 2002

Phil. Trans. R. Soc. Lond. B

465

390

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Collagen type I is the most abundant structural protein in tendon, skin and bone, and largely determines the mechanical behaviour of these connective tissues. To obtain a better understanding of the relationship between structure and mechanical properties, tensile tests and synchrotron X-ray scattering have been carried out simultaneously, correlating the mechanical behaviour with changes in the microstructure. Because intermolecular cross-links are thought to have a great influence on the mechanical behaviour of collagen, we also carried out experiments using cross-link-deficient tail-tendon collagen from rats fed with β-APN, in addition to normal controls.The load-elongation curve of tendon collagen has a characteristic shape with, initially, an increasing slope, corresponding to an increasing stiffness, followed by yielding and then fracture. Cross-link-deficient collagen produces a quite different curve with a marked plateau appearing in some cases, where the length of the tendon increases at constant stress. With the use of in situ X-ray diffraction, it was possible to measure simultaneously the elongation of the collagen fibrils inside the tendon and of the tendon as a whole. The overall strain of the tendon was always larger than the strain in the individual fibrils, which demonstrates that some deformation is taking place in the matrix between fibrils. Moreover, the ratio of fibril strain to tendon strain was dependent on the applied strain rate. When the speed of deformation was increased, this ratio increased in normal collagen but generally decreased in cross-link-deficient collagen, correlating to the appearance of a plateau in the force-elongation curve indicating creep.We proposed a simple structural model, which describes the tendon at a hierarchical level, where fibrils and interfibrillar matrix act as coupled viscoelastic systems. All qualitative features of the strain-rate dependence of both normal and cross-link-deficient collagen can be reproduced within this model. This complements earlier models that considered the next smallest level of hierarchy, describing the deformation of collagen fibrils in terms of changes in their molecular packing.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Viscoelastic properties of collagen: synchrotron radiation investigations and structural model

Puxkandl

Zizak

Paris

et al. 2002

Phil. Trans. R. Soc. Lond. B

465

390

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“…Ultimately the brunt of tensile load is borne by small diameter (20 -500 nm) collagen fibrils that constitute the major part of tendon dry weight (75%). While there is an active debate regarding the relative continuity/interconnectivity of collagen fibrils and how collagen fibrils are effectively cross-linked and/or interwoven to provide structural integrity (Provenzano and Vanderby, 2006), a large number of studies suggest that collagen fibrils are relatively short and assume a discontinuous fibril network (Birk et al, 1997;Dahners et al, 2000;Mosler et al, 1985;Thurmond and Trotter, 1994;Trotter and Koob, 1989). Thus tendon is widely modeled as a fiber reinforced composite material in which force is laterally transferred between neighboring fibrils (Ciarletta et al, 2008;Haut, 1986;Humphrey and Yin, 1987;Korhonen et al, 2003;Lanir, 1978;Mommersteeg et al, 1996;Preston and Meyer, 1971;Wren et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Evidence against proteoglycan mediated collagen fibril load transmission and dynamic viscoelasticity in tendon

Fessel¹,

Snedeker²

2009

Matrix Biology

140

112

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Evidence against proteoglycan mediated collagen fibril load transmission and dynamic viscoelasticity in tendon Fessel, G; Snedeker, J G Fessel, G; Snedeker, J G (2009 The glycosaminoglycan (GAG) dermatan sulphate and chondroitin sulphate side-chains of small leucine-rich proteoglycans have been increasingly posited to act as molecular cross links between adjacent collagen fibrils and to directly contribute to tendon elasticity. GAGs have also been implicated in tendon viscoelasticity, supposedly affecting frictional loss during elongation or fluid flow through the extra cellular matrix.The current study sought to systematically test these theories of tendon structure-function by investigating the mechanical repercussions of enzymatic depletion of GAG complexes by chondroitinase ABC in a reproducible tendon structure-function model (rat tail fascicles). The extent of GAG removal (at least 93%) was verified by relevant spectrophotometric assays and transmission electron microscopy. Dynamic viscoelastic tensile tests on GAG depleted rat tail tendon fascicle were not mechanically different from controls in storage modulus (elastic behavior) over a wide range of strain-rates (0.05, 0.5, and 5% change in length per second) in either the linear or nonlinear regions of the material curve. Loss modulus (viscoelastic behavior) was only affected in the nonlinear region at the highest strain rate, and even this effect was marginal (19% increased loss modulus, p=0.035). Thus glycosaminoglycan chains of small leucine rich proteoglycans do not appear to mediate dynamic elastic behavior nor do they appear to regulate the dynamic viscoelastic properties in rat tail tendon fascicles.

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“…It points out that knowledge of the viscoelastic properties of one of the constituents is not sufficient to gain an understanding of the response of the muscle composite system. This motivates the need for separate experiments on the muscle fibres and the ECM, along the lines of those attempted by Mosler et al (1985) and Purslow et al (1998). Figure 8 shows that the response of the muscle composite system also depends on the characteristic time of a strain history relative to the characteristic relaxation time of the ECM.…”

Section: Summary and Concluding Remarksmentioning

confidence: 99%

Time-dependent lateral transmission of force in skeletal muscle

2009

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There is experimental evidence to suggest that extensible connective tissues are mechanically time-dependent. In view of this, the mechanics of time-dependent lateral stress transfer in skeletal muscle is investigated by employing a viscoelastic shear lag model for the transfer of tensile stress between muscle fibres and the surrounding extracellular matrix (ECM) by means of shear stresses at the interface between the muscle fibre and the ECM. The model allows for both mechanical strains in the muscle as well as the strain owing to muscle contraction. Both the ECM and the muscle fibre are modelled as viscoelastic solids. As a result, time-dependent lateral stress transfer can be studied under a variety of loading and muscle stimulation conditions. The results show that the larger the muscle fibre creep time relative to the ECM relaxation time, the longer it takes for the muscle fibre stress to relax. It also shows that the response of the muscle-ECM composite system also depends on the characteristic time of a strain history relative to the characteristic relaxation time of the ECM. The results from the present model provide significant insight into the role of the parameters that characterize the response of the muscle composite system.

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Stress-induced molecular rearrangement in tendon collagen

Cited by 194 publications

References 12 publications

Viscoelastic properties of collagen: synchrotron radiation investigations and structural model

Viscoelastic properties of collagen: synchrotron radiation investigations and structural model

Evidence against proteoglycan mediated collagen fibril load transmission and dynamic viscoelasticity in tendon

Time-dependent lateral transmission of force in skeletal muscle

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