Thermal stability, mechanical properties and reducible cross-links of rat tail tendon in experimental diabetes.
Thermal stability (measured as isometric contraction force), biomechanical properties and reducible cross-links were measured in tail tendons from streptozotocin diabetic rats, with and without insulin treatment. After 10 days of diabetes the maximum thermal contraction force was unchanged, but the relaxation following the maximal contraction was retarded. After 30 days the maximum contraction force was increased and the relaxation rate was decreased. The maximum strength and stiffness of the tendons were increased after 10 days of diabetes and even more after 30 days. There was no change in the density of reducible cross-links. However, diabetes increased the amount of glucose attached to the lysine and hydroxylysine residues of collagen. Insulin treatment prevented all changes in thermal stability and mechanical properties. The results indicate that stabilization of collagen fibres in diabetes does not follow the same pattern as that seen in normal ageing.
D000818:Animals; D001696:Biomechanical Phenomena; D055598:Chemical Phenomena; D002621:Chemistry; D003094:Collagen / Q000502:physiology*; D003921:Diabetes Mellitus, Experimental / Q000503:physiopathology*; D006358:Hot Temperature; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013710:Tendons / Q000503:physiopathology*; D013997:Time Factors
D003094:Collagen