Kresina T F, Malemud C J
Coll Relat Res. 1984 Dec;4(6):453-65. doi: 10.1016/s0174-173x(84)80012-6.
Conditioned culture media from confluent rabbit articular chondrocytes maintained in serum-free monolayer culture contained metal-dependent neutral pH collagenolytic activity degrading Type I, II and III rabbit [125I]-labeled collagens. This collagenolytic activity degraded Type II collagen more slowly than Type I collagen and Type III collagen at 37 degrees C. By contrast, collagenolysis by chondrocyte cytosolic protein, lysosomal granule protein and residual lysosomal membrane protein was highly specific for Type II collagen. Although collagenolytic activity against all the collagen isotypes tested was predominantly in a latent form after 24 h of culture, increasing levels of constitutive collagenolytic activity was measured with increasing culture time. These results are consistent with a differential degradation of rabbit interstitial collagens by rabbit chondrocyte collagenase. The data suggest a cellular compartmentalization of collagenolytic activity with specificity toward Type II collagen.
在无血清单层培养中维持的汇合兔关节软骨细胞的条件培养基含有金属依赖性中性pH胶原酶活性，可降解I型、II型和III型兔[125I]标记的胶原。在37℃下，这种胶原酶活性降解II型胶原的速度比I型胶原和III型胶原慢。相比之下，软骨细胞胞质蛋白、溶酶体颗粒蛋白和残余溶酶体膜蛋白的胶原酶解对II型胶原具有高度特异性。尽管在培养24小时后，针对所有测试胶原同型的胶原酶活性主要以潜伏形式存在，但随着培养时间的增加，组成型胶原酶活性水平也在增加。这些结果与兔软骨细胞胶原酶对兔间质胶原的差异降解一致。数据表明胶原酶活性在细胞内存在区室化，且对II型胶原具有特异性。
