Sapolsky A I, Sheff M F, Matsuta K, Howell D S, Moskowitz R W, Goldberg V M, Norby D P, Malemud C J
Biochim Biophys Acta. 1983 Apr 5;762(2):227-31. doi: 10.1016/0167-4889(83)90075-7.
In addition to releasing collagenase and proteoglycanase activity, rabbit articular chondrocytes in monolayer culture released into the culture medium, latent, neutral enzyme activity which when activated by p-aminophenylmercuric acetate degraded fluorescein-labeled polymeric rat tail tendon Type I collagen and the tropocollagen TCA and TCB fragments of human Type II collagen into smaller peptides at 37 degrees C. Enzyme activity was abolished if p-aminophenylmercuric acetate-activated culture medium was preincubated with 1.10-phenanthroline, a metal chelator. Thus, articular chondrocytes in monolayer culture are capable of producing neutral proteinases which acting together can result in complete degradation of tendon and cartilage collagen to small peptides.
除了释放胶原酶和蛋白聚糖酶活性外，单层培养的兔关节软骨细胞还向培养基中释放潜在的中性酶活性。当用对氨基苯基汞乙酸酯激活时，这种活性在37℃下可将荧光素标记的聚合大鼠尾腱I型胶原以及人II型胶原的原胶原TCA和TCB片段降解为更小的肽段。如果将对氨基苯基汞乙酸酯激活的培养基与金属螯合剂1,10 - 菲咯啉预孵育，酶活性就会被消除。因此，单层培养的关节软骨细胞能够产生中性蛋白酶，这些蛋白酶共同作用可导致肌腱和软骨胶原完全降解为小肽。
