Maciewicz R A, Wotton S F
Department of Veterinary Medicine, School of Veterinary Science, Langford, Bristol, UK.
Biomed Biochim Acta. 1991;50(4-6):561-4.
Rat chondrosarcoma chondrocytes are able to secrete both the precursor and mature forms of cathepsins B and L. When these two cysteine proteinases were added to a native cartilaginous matrix near neutral pH they were found to release and degrade both the proteoglycan and collagen components. One cleavage site in the proteoglycan monomer was found to be near the amino terminal globular domain. Collagen types II, IX, and XI in the matrix were also released and partially degraded. Ultimately these proteinases act as matrix depolymerases as they attacked the regions which are involved in collagen crosslinking. We conclude that these enzymes may play a role in matrix destruction as seen in arthritis.
大鼠软骨肉瘤软骨细胞能够分泌组织蛋白酶B和L的前体形式和成熟形式。当将这两种半胱氨酸蛋白酶添加到接近中性pH的天然软骨基质中时，发现它们会释放并降解蛋白聚糖和胶原蛋白成分。发现蛋白聚糖单体中的一个切割位点靠近氨基末端球状结构域。基质中的II型、IX型和XI型胶原蛋白也被释放并部分降解。最终，这些蛋白酶作为基质解聚酶，攻击参与胶原蛋白交联的区域。我们得出结论，这些酶可能在关节炎中所见的基质破坏中起作用。
