title: An age-related study of morphology and cross-link composition of collagen fibrils in the digital flexor tendons of young thoroughbred horses.
abstract: The superficial digital flexor tendon is the most commonly injured tendon in the racing Thoroughbred. Despite the clinical significance of this structure, only limited data exist regarding normal age-related morphology of the tensile units, the collagen fibrils. The age at which these collagen fibrils become mature in composition and structure may be of importance. Consequently, the association of age and collagen fibril crosslink composition, diameter distribution and crimp morphology in the superficial and deep digital flexor tendons of Thoroughbreds up to and including three years of age has been studied. Replacement of immature crosslinks, peaking of the collagen fibril mass-average diameter and collagen fibril index, and stabilization of collagen crimp morphology changes supported the hypothesis that both digital flexor tendons become mature in structure by two years of age.
authors.affiliation: Department of Veterinary Clinical Sciences, Massey University Palmerston North, New Zealand.
authors.forename: J C
authors.initials: JC
authors.lastname: Patterson-Kane
authors.forename: D A
authors.initials: DA
authors.lastname: Parry
authors.forename: H L
authors.initials: HL
authors.lastname: Birch
authors.forename: A E
authors.initials: AE
authors.lastname: Goodship
authors.forename: E C
authors.initials: EC
authors.lastname: Firth
mesh_terms: D000375:Aging / Q000378:metabolism*; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D003432:Cross-Linking Reagents; D006736:Horses; D007089:Image Enhancement; D008854:Microscopy, Electron; D008859:Microscopy, Polarization / Q000379:methods; D013710:Tendons / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D003432:Cross-Linking Reagents; D003094:Collagen