Buckwalter J A, Ehrlich M G, Armstrong A L, Mankin H J
J Orthop Res. 1987;5(1):128-32. doi: 10.1002/jor.1100050116.
To assess the effect of intracellular growth plate chondrocyte enzymes on proteoglycan structure, we examined enzyme-treated articular cartilage proteoglycans and untreated articular cartilage proteoglycans with the electron microscopic monolayer technique. The untreated proteoglycan monomers ranged in length from less than 20 nm to more than 700 nm, with a mean length of 224.5 +/- 101.6 nm in one experiment and 224.6 +/- 95.7 nm in a second experiment. Incubation with growth plate enzymes reduced proteoglycan monomers to fragments with lengths that varied from less than 5 nm to 143 nm, increased the variability in monomer length, and destroyed proteoglycan aggregates. The enzyme treated monomers had an average length of 29.5 +/- 17.9 nm in one experiment and 35.2 +/- 17.0 nm in a second experiment. The smallest common fragments were 15 nm long and would be expected to contain about 15 glycosaminoglycan chains. This experiment demonstrates that enzymes extracted from growth plate chondrocytes can degrade the chondroitin sulfate-rich region of proteoglycan monomer core proteins, produce a range of monomer fragment sizes with less than 2% of the fragments shorter than 5 nm or longer than 100 nm, increase the variability in monomer length, and degrade proteoglycan aggregates.
为了评估细胞内生长板软骨细胞酶对蛋白聚糖结构的影响，我们使用电子显微镜单层技术检测了经酶处理的关节软骨蛋白聚糖和未经处理的关节软骨蛋白聚糖。未经处理的蛋白聚糖单体长度范围从小于20nm到超过700nm，在一次实验中平均长度为224.5±101.6nm，在第二次实验中为224.6±95.7nm。用生长板酶孵育后，蛋白聚糖单体被降解为长度从小于5nm到143nm不等的片段，增加了单体长度的变异性，并破坏了蛋白聚糖聚集体。在一次实验中，经酶处理的单体平均长度为29.5±17.9nm，在第二次实验中为35.2±17.0nm。最小的共同片段长15nm，预计包含约15条糖胺聚糖链。该实验表明，从生长板软骨细胞中提取的酶可以降解蛋白聚糖单体核心蛋白中富含硫酸软骨素的区域，产生一系列单体片段大小，其中小于5nm或大于100nm的片段不到2%，增加单体长度的变异性，并降解蛋白聚糖聚集体。
