Maciewicz R A, Wotton S F, Etherington D J, Duance V C
AFRC Institute of Food Research, Bristol Laboratory, Langford, Avon, UK.
FEBS Lett. 1990 Aug 20;269(1):189-93. doi: 10.1016/0014-5793(90)81151-d.
We have investigated the susceptibility of both the helical and non-helical regions of isolated rat chondrosarcoma collagens, types II, IX and XI, to degradation by the cysteine proteinases, cathepsins B and L. Both enzymes degrade these collagens at temperatures from 20 to 37 degrees C and pH values from 3.5 to 7.0. Cleavage occurs only within the non-helical domains unless the helix is destabilized. Cathepsin L is more effective than cathepsin B on a molar basis and they appear to cleave at different sites. Since these cathepsins can degrade cartilage collagens at pH values near neutrality, they may contribute to the destruction of cartilage observed in arthritis.
我们研究了分离出的大鼠软骨肉瘤II型、IX型和XI型胶原的螺旋区和非螺旋区被半胱氨酸蛋白酶组织蛋白酶B和L降解的敏感性。这两种酶在20至37摄氏度的温度和3.5至7.0的pH值下都会降解这些胶原。除非螺旋结构不稳定，否则切割仅发生在非螺旋结构域内。按摩尔比计算，组织蛋白酶L比组织蛋白酶B更有效，而且它们似乎在不同位点进行切割。由于这些组织蛋白酶能在接近中性的pH值下降解软骨胶原，它们可能导致了在关节炎中观察到的软骨破坏。
