PURPOSE: To study collagen fibre thickness and crimp formation in healthy and ruptured human tendons. METHODS: The thickness, crimp angle and wavelength of the collagen fibres were analyzed by interference and polarization microscopy and the samples were studied by transmission and scanning electron microscopy in four different healthy human tendons (Achilles, Quadriceps, Biceps brachii and Extensor pollicis longus) and in 66 spontaneously ruptured tendons. RESULTS: In the normal (healthy) tendons, the diameter and crimp angle of the collagen fibres varied greatly between the four different tendons, the thickest fibres with the largest crimp angle being in the Achilles and Quadriceps tendons, whereas the Biceps brachii and Extensor pollicis longus, tendons that bear lighter strains but carry functions of high specificity, were found to have substantially smaller collagen fibres with lower crimp angle. Ruptured tendons had significantly smaller collagen fibre diameter than the normal tendons, the fibre diameter being -36% in comparison to their healthy counterparts in the Achilles tendons (P < 0.0001), -24% in the Quadriceps tendons (P < 0.0001), -37% in the Biceps brachii (P < 0.0001) and -14% in the Extensor pollicis longus (P = 0.10), respectively. Similarly, the crimp angle of the collagen fibres was also found to be lower in the ruptured tendons than in healthy, normal tendons. Further, the collagen fibres in the ruptured human tendons showed great variation in the crimp angle between the adjacent fibres and in the successive crimps of the same fibre. CONCLUSION: Our results show that spontaneously ruptured tendons display focal regions with decreased collagen fibre thickness, decreased crimp angle and disrupted crimp continuity, microscopic alterations that possibly result in reduced strength of the tendons being less resistant to tensile forces, and thus, place them at increased risk of ruptures.
PURPOSE: To study collagen fibre thickness and crimp formation in healthy and ruptured human tendons. METHODS: The thickness, crimp angle and wavelength of the collagen fibres were analyzed by interference and polarization microscopy and the samples were studied by transmission and scanning electron microscopy in four different healthy human tendons (Achilles, Quadriceps, Biceps brachii and Extensor pollicis longus) and in 66 spontaneously ruptured tendons. RESULTS: In the normal (healthy) tendons, the diameter and crimp angle of the collagen fibres varied greatly between the four different tendons, the thickest fibres with the largest crimp angle being in the Achilles and Quadriceps tendons, whereas the Biceps brachii and Extensor pollicis longus, tendons that bear lighter strains but carry functions of high specificity, were found to have substantially smaller collagen fibres with lower crimp angle. Ruptured tendons had significantly smaller collagen fibre diameter than the normal tendons, the fibre diameter being -36% in comparison to their healthy counterparts in the Achilles tendons (P < 0.0001), -24% in the Quadriceps tendons (P < 0.0001), -37% in the Biceps brachii (P < 0.0001) and -14% in the Extensor pollicis longus (P = 0.10), respectively. Similarly, the crimp angle of the collagen fibres was also found to be lower in the ruptured tendons than in healthy, normal tendons. Further, the collagen fibres in the ruptured human tendons showed great variation in the crimp angle between the adjacent fibres and in the successive crimps of the same fibre. CONCLUSION: Our results show that spontaneously ruptured tendons display focal regions with decreased collagen fibre thickness, decreased crimp angle and disrupted crimp continuity, microscopic alterations that possibly result in reduced strength of the tendons being less resistant to tensile forces, and thus, place them at increased risk of ruptures.
Authors: Andreas Herchenhan; Nicholas S Kalson; David F Holmes; Patrick Hill; Karl E Kadler; Lee Margetts Journal: Biomech Model Mechanobiol Date: 2011-07-07