Age-related changes in organization and content of the collagen matrix in rabbit cortical bone.

The organization and composition of the collagen matrix of cortical bone changes as the bone matures due to growth and mechanical loading. We aimed to investigate the composition and organization of the collagen matrix in rabbit cortical bone during maturation using Fourier transform infrared (FTIR) microspectroscopy and polarized light microscopy (PLM). FTIR and PLM findings were compared to biochemical analysis from an earlier study. Mid-diaphyseal samples from left femora of female New Zealand White rabbits were used. The animal age ranged from newborn to 18-month old (5 age groups, n = 10 per group). The bones had earlier been decalcified and evaluated with biochemistry. In this study, collagen content, orientation, collagen cross-linking and spatial heterogeneity of all parameters was evaluated. Similar results were obtained when collagen content was evaluated with FTIR and PLM compared to the collagen content assessed with BA. Collagen content, orientation and collagen maturity increased significantly until the age of 3 months and remained similar thereafter. Simultaneously, spatial heterogeneity of the measured parameters decreased. Based on these findings, it seems that the collagen matrix of rabbit bone attains its mature state around 3 months of age, which is before the overall skeletal maturity is reached.