Potential of collagen cross-linking therapies to mediate tendon mechanical properties

Fessel, Gion; Gerber, Christian; Snedeker, Jess G.

doi:10.1016/j.jse.2011.10.002

Cited by 51 publications

(56 citation statements)

References 79 publications

(90 reference statements)

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“…In all soft tissues, fibrils are embedded in highly hydrophilic proteoglycan-rich matrix. However, in tendon mid-substance small proteoglycans-decorin and biglycan-which decorate the fibrils at discrete binding sites are the most abundant [48,49], while in the adult menisci the proteoglycan matrix contains also large, highly hydrated aggrecan aggregates [50].…”

Section: Discussionmentioning

confidence: 99%

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Trębacz

Szczęsna

Arczewska

2018

J Therm Anal Calorim

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The aim of the work was to compare glycation-related changes in thermal denaturation of collagen in naturally ageing and in vitro ribosylated tissues. Samples of cornea, meniscus and Achilles tendon from young adult and from ageing rabbits were compared. Moreover, in vitro glycated samples (ribose, 100 mg mL -1 , 14 days) were prepared for both age groups. Collagen in tissues was characterized in terms of thermal denaturation parameters obtained from differential scanning calorimetry. The level of pentosidine and other fluorescent advanced glycation end products (AGEs) in the papain-digested tissue samples was evaluated using spectrofluorimetry (k ex/em : 335/385 and 370/440 nm). In naturally ageing tissues, changes in properties of extracellular matrix collagen expressed in terms of parameters of thermal denaturation and fluorescent AGEs levels were tissue dependent and were related to differences in organization of matrix components. No signs of increased level of AGEs were found in the naturally ageing cornea, unlike in the tendon and meniscus. In vitro ribation proved by gains of fluorescent AGEs affected thermal stability of collagen in all tissues, both in young adult and in the ageing ones. The effects of ribation were considerably greater than the effects of natural ageing. The increase in denaturation temperature was similarly strong in all tissues and did not correlate with the increase in fluorescent AGEs. As a conclusion, parameters of collagen thermal denaturation are tissue and age dependent and an amount of fluorescent AGEs is not the only determinant of increasing thermal stability of glycated collagen.

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Section: Discussionmentioning

confidence: 99%

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Trębacz

Szczęsna

Arczewska

2018

J Therm Anal Calorim

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“…Samples were subjected to a pre-load of 3 N to establish the initial length L 0 , which was used to normalize displacement measurements to nominal strain. Mid-substance strains were determined using video extensometry in order to avoid non-representative stress-strain behaviour in the immediate vicinity of the clamps (St. Venant's principle) as well as to compensate for eventual slippage at the clamps (Fessel et al, 2012a(Fessel et al, , 2012b. The apparatus consisted of a Basler Inc. ® type A622f digital video camera furnished with a high precision telecentric lens from Edmund Optics Inc., type NT62-921.…”

Section: Materials Propertiesmentioning

confidence: 99%

Changes in length of the plantar aponeurosis during the stance phase of gait – An in vivo dynamic fluoroscopic study

Fessel

Jacob²,

Wyss

et al. 2014

Annals of Anatomy - Anatomischer Anzeiger

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“…The structure and relative movements of stained GAGs during mechanical relaxation tests suggest interfibrillar force transfer through a ratchet mechanism (Cribb and Scott, 1995; Watanabe et al, 2007; Watanabe et al, 2012). However, studies with enzymatic removal of GAGs have provided conflicting evidence concerning the role of GAGs in tendon mechanics (Fessel et al, 2012; Fessel and Snedeker, 2009, 2011; Lujan et al, 2007; Lujan et al, 2009). Moreover, studies involving transgenic animals are controversial, with varied results in different species, tendons, and even regional variations within tendon (Connizzo et al, 2013; Dourte et al, 2012; Dunkman et al, 2013; Elliott et al, 2003; Robinson et al, 2005; Robinson et al, 2004b).…”

Section: Introductionmentioning

confidence: 99%

Determining the contribution of glycosaminoglycans to tendon mechanical properties with a modified shear-lag model

Ahmadzadeh

Connizzo

Freedman

et al. 2013

Journal of Biomechanics

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Tendon has a complex hierarchical structure composed of both a collagenous and a non-collagenous matrix. Despite several studies that have aimed to elucidate the mechanism of load transfer between matrix components, the roles of glycosaminoglycans (GAGs) remain controversial. Thus, this study investigated the elastic properties of tendon using a modified shear-lag model that accounts for the structure and non-linear mechanical response of the GAGs. Unlike prior shear-lag models that are solved either in two dimensions or in axially symmetric geometries, we present a closed-form analytical model for three-dimensional periodic lattices of fibrils linked by GAGs. Using this approach, we show that the non-linear mechanical response of the GAGs leads to a distinct toe region in the stress-strain response of the tendon. The critical strain of the toe region is shown to decrease inversely with fibril length. Furthermore, we identify a characteristic length scale, related to microstructural parameters (e.g. GAG spacing, stiffness, and geometry) over which load is transferred from the GAGs to the fibrils. We show that when the fibril lengths are significantly larger than this length scale, the mechanical properties of the tendon are relatively insensitive to deletion of GAGs. Our results provide a physical explanation for the insensitivity for the mechanical response of tendon to the deletion of GAGs in mature tendons, underscore the importance of fibril length in determining the elastic properties of the tendon, and are in excellent agreement with computationally intensive simulations.

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Potential of collagen cross-linking therapies to mediate tendon mechanical properties

Cited by 51 publications

References 79 publications

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Changes in length of the plantar aponeurosis during the stance phase of gait – An in vivo dynamic fluoroscopic study

Determining the contribution of glycosaminoglycans to tendon mechanical properties with a modified shear-lag model

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