COLLAGENASES IN HUMAN SYNOVIAL FLUID
COLLAGENASES IN HUMAN SYNOVIAL FLUID
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DOI：
10.1172/jci106177
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发表时间：
1969-01-01
影响因子：
15.9
通讯作者：
KRANE, SM
中科院分区：
文献类型：
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作者：
HARRIS, ED;DIBONA, DR;KRANE, SM
在中性pH下降解天然胶原的酶已从体外类风湿性滑膜培养物中分离出来，但在新鲜类风湿性滑膜匀浆中发现很少或没有胶原溶解活性。与大多数其他哺乳动物胶原酶相似，这种滑液酶容易被血清蛋白抑制。滑液中的蛋白质主要来自血清，发现非炎症关节的滑液可抑制滑液胶原酶;胰蛋白酶可破坏该抑制剂，但透明质酸酶不能。类风湿性关节炎患者的大约一半液体中的抑制活性降低。在总共9种滑液中，可检测到胶原溶解活性。这种活性在同一患者不同时间抽取的滑液中不存在恒定的量，并且倾向于与抑制蛋白的滴度成反比。不同患者滑液中的胶原溶解活性被血清蛋白抑制。两种不同的胶原酶检测到一些类风湿关节液和分离的凝胶过滤。一种标记为“B”的酶，估计分子量为20，000 - 25，000，类似于从滑膜培养物中获得的胶原酶。另一种标记为“A”的酶降解胶原纤维以及溶液中的胶原。在丙烯酰胺凝胶上的圆盘电泳和在27°C下酶的反应产物的片段长间距（SLS）聚集体的电子显微镜显示，“A”和“B”酶都在距离分子的氨基末端四分之三的点处切割胶原分子。因此，类风湿性关节炎中的胶原降解可能是由这两种胶原酶的作用引起的。图片
An enzyme which degrades native collagen at neutral pH has been isolated from cultures of rheumatoid synovium in vitro, but little or no collagenolytic activity has been found in homogenates of fresh rheumatoid synovium. Similar to most other mammalian collagenases this synovial enzyme is readily inhibited by serum proteins. Proteins of synovial fluid are derived largely from serum and synovial fluid from noninflamed joints was found to inhibit synovial collagenase; the inhibitor was destroyed by trypsin, but not by hyaluronidase. Inhibitory activity was reduced in approximately one-half of the fluids from patients with rheumatoid arthritis. In a total of nine synovial fluids, collagenolytic activity was detectable. This activity was not present in constant amounts in synovial fluids aspirated at different times from the same patient and tended to vary inversely with the titer of inhibitory proteins. The collagenolytic activity in the synovial fluids from different patients was variably inhibited by serum proteins. Two distinct collagenases were detected in some rheumatoid synovial fluids and separated by gel filtration. One, labeled “B” enzyme, with an estimated molecular weight 20,000-25,000 resembled the collagenase obtained from synovial cultures. The other, labeled “A” enzyme degraded collagen fibrils as well as collagen in solution. Disc electrophoresis on acrylamide gels and electron microscopy of segment long spacing (SLS) aggregates of reaction products of the enzymes at 27°C demonstrated that both “A” and “B” enzymes cleaved collagen molecules at a point three-quarters from the amino terminal end of the molecule. Thus collagen degradation in rheumatoid arthritis could result from the operation of these two collagenases.Images