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. Author manuscript; available in PMC: 2021 Jan 1.
Published in final edited form as: Matrix Biol. 2019 Oct 23;85-86:47–67. doi: 10.1016/j.matbio.2019.10.001

Figure 7.

Figure 7

Impact of collagen III reduction on the covalent cross-linking in the collagen fibrils of articular cartilage (AC) and meniscus (M). a,b) Comparisons of collagen amount and cross-linking between wild-type (+/+) and Col3a1+/− (+/−) tissues, a) total collagen amount, and b) cross-linking analysis of the immature cross-link dihydroxylysinonorleucine (DHLNL), mature cross-link pyrodinoline (Pyd) and deoxy-pyrodinoline (de-Pyd) and total LOX-mediated aldehyde densities. c) Western blot on the expression of LOX and associated semi-quantitative levels of LOX content, as normalized to the internal GAPDH control. All the results were obtained from 2-month-old tissues (mean ± SD, n = 4 biological repeats for articular cartilage, and n = 3 for meniscus). Each data point represents one biological repeat measured from tissues pooled from 3 animals.