Day-old White Leghorn cockerels were fed skim-milk-based diets containing 0, 2, 4, 8, or 16 ppm added copper as CuSO4 for 21 days. Lysyl oxidase was extracted from bone and tendon. The recovery of activity from the extracts was linearly correlated with dietary copper (r greater than 0.90). Tests of the mechanical properties of tendon and bone indicated that tendon viscoelasticity (as measured by stress--relaxation) may not be significantly influenced by copper, whereas the ultimate torsional strength of bone is markedly decreased when the dietary copper level is below 1 ppm. Furthermore the torsional fracture characteristics of bone from copper-deficient birds demonstrated a lack of plastic deformation prior to failure that was normally seen in bone from control birds. The change in the mechanical properties of bone from copper-deficient birds appeared to be related to a decrease in the amounts of dihydroxylysinonorleucine and other lysine-derived cross-linking amino acids in bone collagen. The data indicate that the requirement for optimal growth of chicks fed skim-milk-based diets is 6--8 ppm copper, however, the requirement for normal cross-link formation in bone is less than 2 ppm copper.
Increased bone fragility was observed in chickens fed diets containing less than 1 ppm copper. Using a device that was designed to measure torsion during fracture, it could be demonstrated that bone from copper-deficient chicks fractured with less deformation and torque than bone from control chicks. The collagen of bone from copper-deficient chicks appeared to contain fewer cross-links than normal bone. The introduction of artificial cross-links into collagen from copper-deficient chick bone by formaldehyde and NaBH4 treatments improved bone strength and strain (deformation) so that it was comparable with normal bone. Copper deficiency blocks the formation of cross-links in collagens and elastin from various tissues. It is felt that the bone fragility related to nutritional copper deficiency is the result of decreased bone collagen cross linking. Arterial elastin metabolism was also investigated. By radioactively labeling arterial soluble elastin (tropoelastin) in vivo by an intraperitoneal injection of [G-3H]valine, it could be demonstrated that copper deficiency appeared to reduce its rate of metabolic turnover. Soluble elastin or tropoelastin is assumed to be the precursor of mature or insoluble elastin. The observations presented here are consistent with the view that by retarding the steps associated with elastin cross-link formation, the incorporation of soluble elastin into mature elastin may be retarded as well.
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