Liu J, Roughley P J, Mort J S
Joint Diseases Laboratory, Shriners Hospital for Crippled Children, Montreal, Quebec, Canada.
J Orthop Res. 1991 Jul;9(4):568-75. doi: 10.1002/jor.1100090413.
Human intervertebral disc when maintained in organ culture released a latent casein-degrading metalloproteinase into the medium in a manner analogous to cultures of human cartilage. This enzyme was demonstrated to be immunologically identical to prostromelysin. It was also found that the amount of procollagenase secreted by both cartilage and disc cells was considerably less than that of prostromelysin. Tissue extraction confirmed that the low level of procollagenase observed was not due to retention of the enzyme within the tissue. Human intervertebral disc link proteins were found to possess the same N-termini as those of their counterparts in human articular cartilage, where it appears that stromelysin is responsible for generating molecular heterogeneity. These results suggest that intervertebral disc cells are capable of secreting prostromelysin, which can become activated within the extracellular matrix and hence contribute to the age-related and degenerative changes in the disc.
当在器官培养中维持时，人类椎间盘会以类似于人类软骨培养的方式将一种潜在的酪蛋白降解金属蛋白酶释放到培养基中。这种酶经证实与前基质溶解素在免疫学上是相同的。还发现软骨细胞和椎间盘细胞分泌的原胶原酶的量远少于前基质溶解素。组织提取证实，观察到的原胶原酶水平较低并非由于该酶在组织内的滞留。发现人类椎间盘连接蛋白具有与人类关节软骨中对应蛋白相同的N端，在关节软骨中似乎基质溶解素负责产生分子异质性。这些结果表明，椎间盘细胞能够分泌前基质溶解素，其可在细胞外基质内被激活，从而导致椎间盘的年龄相关和退行性变化。
