Molecular biology and biomechanics of normal and healing ligaments—a review

Frank, Cyril B.; Hart, David A.; Shrive, Nigel G.

doi:10.1053/joca.1998.0168

Cited by 124 publications

(106 citation statements)

References 12 publications

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“…Remodeling and maintenance of ligament tissues are influenced by several factors including cellular response, ECM structure, vascularization, and growth factors [21,22]. However, the difference in chondrogenic property between ACL-and MCL-derived cells has not been elucidated.…”

Section: Discussionmentioning

confidence: 99%

Anterior cruciate ligament-derived cells have high chondrogenic potential

Furumatsu

Hachioji

Saiga

et al. 2010

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 99%

Anterior cruciate ligament-derived cells have high chondrogenic potential

Furumatsu

Hachioji

Saiga

et al. 2010

Biochemical and Biophysical Research Communications

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“…Proteoglycans are thought to organize and orientate the collagen fibers within the extracellular matrix, 24 and both proteoglycans and water are believed to play a part in determining the viscoelastic properties of tendons and ligaments. 25 The higher GAG content in the PCL therefore suggests that it may have unique mechanical properties. In quadrapeds such as the sheep the knee is kept in a position of flexion, thus resulting in high continuous loads when the animal is standing.…”

Section: Discussionmentioning

confidence: 99%

Tendons and ligaments are anatomically distinct but overlap in molecular and morphological features—a comparative study in an ovine model

Rumian

Wallace

Birch

2007

Journal Orthopaedic Research

135

113

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Tendons and ligaments are similar in composition but differ in function. Simple anatomical definitions do not reflect the fact individual tendons and ligaments have unique properties due to their adaptation to a specific role. The patellar tendon is a structure of particular clinical interest. A null hypothesis was declared stating that the patellar tendon is not significantly different in terms of matrix composition and collagen fibril diameter to other tendons. The lateral and medial collateral ligaments (LCL, MCL), anterior and posterior cruciate ligaments (ACL, PCL), together with the long digital extensor, superficial digital extensor, and patellar tendons (LDET, SDFT, PT) were harvested from three cadaveric ovine hindlimbs. The extracellular matrix was assessed in terms of water, collagen, and total sulphated glycosaminoglycan (GAG) content. The organization of the collagen component was determined by an ultrastructural analysis of collagen fibril diameter distributions, together with values for the collagen fibril index (CFI) and massaverage diameter (MAD). There were significant differences between ligaments and tendons. The PT had a bimodal collagen fibril diameter distribution with CFI 72.9%, MAD 202 nm, water content 53.1%, GAG content 2.3 mg/mg, and collagen content 73.7%, which was not significantly different from the other tendons. The results of this study support the null hypothesis suggesting that the patellar tendon is similar to other tendons and demonstrate that tendons have different characteristics to ligaments. ß

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“…Tendon CSA relative to body size does not differ between sexes (33), but tendon collagen synthesis is significantly lower in women than men (38). Estrogen directly alters collagen kinetics (8,15,17), and inherently higher estrogen levels in women may therefore chronically depress collagen production, as tendon cells have estrogen receptors (8,17). Thus, blunted collagen production via estrogen could explain the lower amount of dry mass in female tendons, as collagen comprises ϳ90% of dry mass.…”

Section: Discussionmentioning

confidence: 99%

Impact of sex and chronic resistance training on human patellar tendon dry mass, collagen content, and collagen cross-linking

LeMoine

Lee²,

Trappe³

2009

American Journal of Physiology-Regulatory, Integrative and Comp

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LeMoine JK, Lee JD, Trappe TA. Impact of sex and chronic resistance training on human patellar tendon dry mass, collagen content, and collagen cross-linking. Am J Physiol Regul Integr Comp Physiol 296: R119 -R124, 2009. First published October 22, 2008 doi:10.1152/ajpregu.90607.2008.-Collagen content and cross-linking are believed to be major determinants of tendon structural integrity and function. Sex and chronic resistance training have been shown to alter tendon function and may also alter the key structural features of tendon. Patellar tendon biopsies were taken from untrained men [n ϭ 8, 1 repetition maximum (RM) ϭ 53 Ϯ 3 kg], untrained women (n ϭ 8, 1 RM ϭ 29 Ϯ 2 kg), and resistance-trained (10 Ϯ 1 yr of training) men (n ϭ 8, 1 RM ϭ 71 Ϯ 6 kg). Biopsies were analyzed for dry mass, collagen content, and collagen cross-linking (hydroxylysylpyridinoline). We hypothesized that these elements of tendon structure would be lower in women than men, whereas chronic resistance training would increase these parameters in men. Tendon dry mass was significantly lower in women than men (343 Ϯ 5 vs. 376 Ϯ 8 g dry mass/mg tendon wet wt, P Ͻ 0.01) and was not influenced by chronic resistance training (P Ͼ 0.05). The lower tendon dry mass in women tended to reduce (P ϭ 0.08) collagen content per tendon wet weight. Collagen content of the tendon dry mass was not influenced by sex or resistance training (P Ͼ 0.05). Similarly, cross-linking of collagen was unaltered (P Ͼ 0.05) by sex or training. Although sex alters the water content of patellar tendon tissue, any changes in tendon function with sex or chronic resistance training in men do not appear to be explained by alterations in collagen content or cross-linking of collagen within the dry mass component of the tendon. human tendon; water content; hydroxyproline; hydroxylysylpyridinoline TENDONS ARE THE FIBROELASTIC structures that connect muscle to bone and convey muscular force (5,22,23). The tensile strength of tendon tissue is estimated to be 50 -100 N/mm 2 (5), a key feature as tendons are subjected daily to high forces. The composition of tendon tissue influences its strength and integrity, playing a key role in force transmission through the muscle-tendon complex (23). Animal and human cadaver studies indicate that tendon tissue is ϳ55-70% water (5, 23), with the remaining dry mass containing the extracellular matrix and tendon cells (5,22). Collagen is the main protein component of tendon tissue, comprising ϳ65-75% of the dry mass (5,22,23). Collagen molecules are joined into fibrils and fibers by lysine-based cross-links [hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP)] (7,22,23,30). Tendon dry mass, collagen content, and cross-links have been shown to impact tendon strength and mechanical properties (22,23,30,52).Tendon tissue is dynamic, highly metabolic, and quite responsive to exercise (23,24,29,34). Tendons should therefore adapt in a positive manner to long-term loading, becoming more damage resistant and ensuring optimal muscular force transmissi...

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Molecular biology and biomechanics of normal and healing ligaments—a review

Cited by 124 publications

References 12 publications

Anterior cruciate ligament-derived cells have high chondrogenic potential

Anterior cruciate ligament-derived cells have high chondrogenic potential

Tendons and ligaments are anatomically distinct but overlap in molecular and morphological features—a comparative study in an ovine model

Impact of sex and chronic resistance training on human patellar tendon dry mass, collagen content, and collagen cross-linking

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