NITRIC-OXIDE ACTIVATES METALLOPROTEASE ENZYMES IN ARTICULAR-CARTILAGE
NITRIC-OXIDE ACTIVATES METALLOPROTEASE ENZYMES IN ARTICULAR-CARTILAGE
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DOI：
10.1006/bbrc.1995.1003
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发表时间：
1995-01-05
影响因子：
3.1
通讯作者：
WILLIAMS, RJ
中科院分区：
文献类型：
--
作者：
MURRELL, GAC;JANG, D;WILLIAMS, RJ
一氧化氮（NO.）是由统称为一氧化氮合酶的酶家族产生的多功能信使分子。我们研究了NO在调节两种金属依赖性蛋白水解酶（胶原酶和基质溶解素）中的作用，这两种酶在炎症和感染性关节炎期间被激活。炎症介质白细胞介素-1 β（IL-1 β），肿瘤坏死因子-α（TNF-α）和细菌细胞壁片段内毒素，诱导一氧化氮合酶活性和基质溶解素和胶原酶活性在全细胞制剂和条件培养基从牛和人软骨外植体。两个NO2。(the稳定的最终产物）和金属蛋白酶活性被一氧化氮合酶的竞争性抑制剂抑制。NO供体S-亚硝基-N-乙酰基-D，L-青霉胺（SNAP）也以剂量依赖性方式诱导金属蛋白酶活性。这些数据提供了证据，NO.在关节软骨细胞和软骨中金属依赖性蛋白酶的激活中起调节作用。(C)北京：科学出版社. Inc.
Nitric oxide (NO.) is a multifunctional messenger molecule generated by a family of enzymes, collectively termed the nitric oxide synthases. We investigated the role of NO. in the modulation of two metal-dependent proteolytic enzymes (collagenase and stromelysin) which are activated during inflammatory and infective arthritis. The inflammatory mediators interleukin-1 beta (IL-1 beta), tumor necrosis factor-alpha (TNF-alpha) and the bacterial cell wall fragment endotoxin, induced both nitric oxide synthase activity and stromelysin and collagenase activity in whole cell preparations and in conditioned media from explants of bovine and human cartilage. Both NO2. (the stable end-product of NO.) and metalloprotease activity were inhibited by competitive inhibitors of nitric oxide synthase. The NO. donor, S-nitroso-N-acetyl-D,L-penicillamine (SNAP) also induced metalloprotease activity in a dose-dependent fashion. These data provide evidence that NO. plays a regulatory role in the activation of metal-dependent proteases in articular chondrocytes and cartilage. (C) 1995 Academic Press. Inc.