title: Inflammatory cells do not decrease the ultimate tensile strength of intact tendons in vivo and in vitro: protective role of mechanical loading.
abstract: Although inflammatory cells and their products are involved in various pathological processes, a possible role in tendon dysfunction has never been convincingly confirmed and extensively investigated. The goal of this study was to determine whether or not an acute inflammatory process deprived of mechanical trauma can induce nonspecific damages to intact collagen fibers. To induce leukocyte accumulation, carrageenan was injected into rat Achilles tendons. We first tested the effect of leukocyte recruitment on the concentrations or activities of matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases. Second, we analyzed at the biochemical, histological, and biomechanical levels the impact of leukocyte invasion on tendons. Finally, collagen bundles isolated from rat-tail tendons were exposed in vitro to mechanical stress and/or inflammatory cells to determine if mechanical loading could protect tendons from the leukocyte proteolytic activity. Carrageenan-induced leukocyte accumulation was associated with an increased matrix metalloproteinase activity and a decreased content of tissue inhibitors of matrix metalloproteinases. However, hydroxyproline content and load to failure did not change significantly in these tendons. Interestingly, mechanical stress, when applied in vitro, protected collagen bundles from inflammatory cell-induced deterioration. Together, our results suggest that acute inflammation does not induce damages to intact and mechanically stressed collagen fibers. This protective effect would not rely on increased tissue inhibitors of matrix metalloproteinases content but would rather be conferred to the intrinsic resistance of mechanically loaded collagen fibers to proteolytic degradation.
authors.affiliation: Centre de Recherche du Centre Hospitalier Universitaire de Québec, Quebec City, Quebec, Canada.
authors.forename: David
authors.initials: D
authors.lastname: Marsolais
authors.forename: Elise
authors.initials: E
authors.lastname: Duchesne
authors.forename: Claude H
authors.initials: CH
authors.lastname: Côté
authors.forename: Jérôme
authors.initials: J
authors.lastname: Frenette
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D002351:Carrageenan; D003094:Collagen / Q000378:metabolism*; D005260:Female; D006909:Hydroxyproline / Q000378:metabolism; D007249:Inflammation / Q000139:chemically induced / Q000473:pathology* / Q000503:physiopathology; D007962:Leukocytes / Q000378:metabolism / Q000473:pathology; D020782:Matrix Metalloproteinases / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013314:Stress, Mechanical; D052256:Tendinopathy / Q000139:chemically induced / Q000473:pathology* / Q000503:physiopathology; D013708:Tendon Injuries / Q000209:etiology / Q000473:pathology / Q000503:physiopathology; D013710:Tendons / Q000378:metabolism / Q000473:pathology* / Q000503:physiopathology*; D013718:Tensile Strength / Q000502:physiology*; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000378:metabolism; D019716:Tissue Inhibitor of Metalloproteinase-2 / Q000378:metabolism; D016474:Weight-Bearing
chemical_list: D019715:Tissue Inhibitor of Metalloproteinase-1; D019716:Tissue Inhibitor of Metalloproteinase-2; D002351:Carrageenan; D003094:Collagen; D020782:Matrix Metalloproteinases; D006909:Hydroxyproline