chondroitin-sulfates and pyridinoline

Male white Leghorn chickens were exercised on a treadmill at 70-80% of their maximal oxygen consumption starting at 4 weeks and continuing up to 20 weeks of age. The effect of the strenuous exercise regime on the extracellular matrix of menisci was followed through studies of proteoglycans and collagen. Avian menisci contain type I collagen, chondroitin sulfate proteoglycans, which increase with age in amount and degree of aggregation, and dermatan sulfate proteoglycans, which decrease with age. Five weeks of exercise cause a premature decrease of dermatan sulfate proteoglycans, while the chondroitin sulfate-containing molecules become significantly more aggregated than those of the tissue of age-matched controls. Strenuous exercise also causes a significant decrease in the number of pyridinoline crosslinks per mole of collagen in the menisci of young runners. The exercise-induced changes of proteoglycan and collagen occur only during the period of active growth, and all parameters return to normal when the animals reach skeletal maturity. The early proteoglycan aggregation and dermatan sulfate decrease induced by exercise are probably an adaptation to the increased loading. Although the mechanism by which strenuous exercise reduces or delays the formation of collagen pyridinoline crosslinks in menisci of skeletally immature animals is unknown, their decrease could negatively affect the mechanical properties of the tissue during the period of active growth.

Topics: Adaptation, Physiological; Aging; Amino Acids; Animals; Chickens; Chondroitin Sulfates; Chromatography, Gel; Collagen; Dermatan Sulfate; Freeze Drying; Hexuronic Acids; Hyaluronic Acid; Male; Menisci, Tibial; Models, Biological; Physical Exertion; Proteoglycans; Random Allocation; Running