Abstract
Tendons are parallel arrays of collagenous fibres which are specialised to resist and transmit tensile stresses. The response of tendon fibres to tensile stress is age-dependent and complex. Elastic elongation at low stress is accompanied by the disappearance of alternate light and dark bands seen in transmitted polarised light. This region of the stress/strain curve is associated with straightening of fibre 'crimps'. At higher stress, elongation is still elastic and reversible until break point is reached. This behaviour may be associated with straightening of a helical arrangement of collagen fibrils. In addition to the collagen fibrils, there are transverse and longitudinal proteoglycan filaments, many of which bridge and link between the fibrils. We have investigated the effect of various levels of stress from very low up to breaking point on the appearance of the proteoglycan filaments and their relationships with the collagen fibrils. Proteoglycan-collagen fibril interactions in rat and mouse tail and flexor digitorum tendons were visualised by Cupromeronic blue staining, applied to dissected fibres in the resting state and at stresses up to breaking. Proteoglycan filaments were seen to be orthogonally arranged in every D period, probably at the d band in mature tendons. In immature tendons proteoglycan filaments took up more varied orientations, but were mainly orthogonal or axially arranged with respect to the collagen fibrils. Both pictures appeared unchanged after application of stress of any level up to breaking point. Young tendons ruptured at lower stresses than mature tendons. It is suggested that PG bridges between collagen fibrils play a part in transmitting and resisting tensile stresses in tendons, contributing to the strength of the tissue.
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