title: The unique fibrillar arrangement of the bullfrog pressure-bearing tendon as an indicative of great functional deformability.
abstract: The fiber distribution and ultrastructure in the plantaris longus pressure-bearing tendon of the bullfrog were investigated. The tension region of the tendon showed a predominant parallel distribution of collagen fibers, but three main zones with different crimp parameters were identified with the use of the polarizing microscope. The compression region showed collagen fibers with aspects of disaggregation and were composed of disperse and undulating fibrils. These collagen fibers establish a three-dimensional network but showed a preferential distribution in planes disposed perpendicularly to the tendon's main axis. It is assumed that the convoluted and disaggregated collagen fibers must be distended before exerting any reinforcement on the tissue and that this only occurs after a great deformation of the tendon. Groups of 5-6 fibrils not associated in fibers are also dispersed in the compression region. The tissue is assumed to have a highly viscous fluid nature allowing for the deformation needed for collagen fibrils to reinforce the tendon structure. The convoluted and crimped structure of collagen fibers would be especially useful when the tendon is submitted to the sudden and strong mechanical loading expected to occur during jumping and to provide the tendon with the capacity of great functional deformability necessary for the high amplitude of feet movements attained on jumping and swimming.
authors.affiliation: Department of Cell Biology, CP 6109 Unicamp, Campinas SP, Brazil.
authors.forename: H F
authors.initials: HF
authors.lastname: de Carvalho
authors.forename: B de C
authors.initials: Bde C
authors.lastname: Vidal
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D003094:Collagen / Q000502:physiology / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D008859:Microscopy, Polarization; D011487:Protein Conformation; D011892:Rana catesbeiana / Q000033:anatomy & histology* / Q000502:physiology; D013710:Tendons / Q000502:physiology / Q000648:ultrastructure*
chemical_list: D003094:Collagen