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Collagen biochemistry of avian bone: comparison of bone type and skeletal site.
Authors:L Knott  A J Bailey
Institution:Division of Molecular and Cellular Biology, University of Bristol, Langford, England, UK.
Abstract:1. Skeletal disorders in poultry are of considerable welfare and economic importance. The collagenous matrix in bone is involved in many human skeletal disorders, however little is known about the nature of the collagenous matrix in avian bone. 2. This paper describes an investigation of the collagen and mineral biochemistry together with the biomechanics of bone from different sites (humerus and tibiotarsus) and with differing functions (medullary and cortical bone). In vivo and in vitro studies of immature bone assessed the changes in collagen biochemistry during bone maturation. 3. The material strength of the humerus was greater than the tibiotarsus; this difference in strength was reflected in both the collagen and mineral matrix biochemistry. 4. The bone matrix of the humerus was more mature than that of the tibiotarsus, suggesting a higher level of matrix turnover in the tibiotarsus. The pyrrole collagen cross-link concentrations were positively correlated with breaking stress, in contrast to the pyridinoline cross-link concentrations, neither of which showed any correlation with bone strength. 5. The in vivo and in vitro maturation studies underline the importance of the pyrrole cross-link in avian bone and support the mechanism postulated by Kuypers et al. (1992) for the formation of the pyrrole cross-link from a lysine aldehyde and the immature cross-links HLKNL or LKNL. 6. Medullary bone had no biomechanical influence on the breaking stress of the bone. The biochemistry of the matrix was dramatically different. The high level of collagen lysine hydroxylation affected the cross-link profile and may be responsible for the narrow fibrils and disorganised matrix of this bone. 7. Avian bone matrix varies greatly with skeletal site and reflects the differing functions of bone. Further investigation of the collagenous matrix of both normal and diseased avian bone has the potential to aid our understanding of the aetiology of avian skeletal disease.
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