STIMULATION BY HUMAN INTERLEUKIN-1 OF CARTILAGE BREAKDOWN AND PRODUCTION OF COLLAGENASE AND PROTEOGLYCANASE BY HUMAN CHONDROCYTES BUT NOT BY HUMAN OSTEOBLASTS INVITRO
STIMULATION BY HUMAN INTERLEUKIN-1 OF CARTILAGE BREAKDOWN AND PRODUCTION OF COLLAGENASE AND PROTEOGLYCANASE BY HUMAN CHONDROCYTES BUT NOT BY HUMAN OSTEOBLASTS INVITRO
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DOI：
10.1016/0304-4165(84)90121-1
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发表时间：
1984-01-01
期刊：
影响因子：
--
通讯作者：
RUSSELL, RGG
中科院分区：
文献类型：
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作者：
GOWEN, M;WOOD, DD;RUSSELL, RGG
培养的人关节软骨细胞在加入培养的人单核细胞产生的12-17 kDa（千道尔顿）蛋白后，可合成胶原酶和中性蛋白聚糖酶。在凝胶过滤层析和等电聚焦上，通过淋巴细胞活化因子活性评估，该因子与白细胞介素1 （IL-1）结合。IL-1和促软骨细胞活性被苯乙二醛预处理的材料破坏。同样的材料也促进了完整牛鼻软骨培养物中糖胺聚糖的释放。从软骨细胞释放的蛋白聚糖酶活性似乎是一种金属蛋白酶，因为它受EDTA抑制，而不受苯基甲基磺酰氟（PMSF）的抑制，并且因为其活性的检测依赖于4-氨基苯基醋酸汞的存在。人类成骨细胞样细胞对该因子的反应不是增加蛋白酶的产生，而是被刺激产生前列腺素。显然，IL-1对非免疫细胞具有促进结缔组织基质降解的活性。人类成骨细胞不合成中性胶原蛋白和蛋白聚糖降解酶，因此不太可能直接导致骨吸收过程中发生的基质降解。
Human articular chondrocytes in culture synthesize collagenase and neutral proteoglycanase in response to addition of a 12-17 kDa [kiloDalton] protein produced by cultured human monocytes. This factor copurifies with interleukin 1 [IL-1], as assessed by lymphocyte activating factor activity, on gel filtration chromatography and isoelectric focusing. The IL-1 and chondrocyte-stimulating activities are destroyed by pretreatment of the material with phenylglyoxal. The same materials also promote the release of glycosaminoglycan from cultures of intact bovine nasal cartilage. The proteoglycanase activity released from chondrocytes appears to be a metalloproteinase because it is inhibited by EDTA and not by phenylmethylsulphonyl fluoride (PMSF), and because detection of its activity is dependent on the presence of 4-aminophenylmercuric acetate. Human osteoblast-like cells do not respond to this factor by increased proteinase production but are stimulated to produce prostaglandins. Evidently, IL-1 has activities upon non-immune cells which promote the degradation of connective tissue matrices. Human osteoblasts do not synthesize neutral collagen- and proteoglycan-degrading enzymes and thus are unlikely to be directly responsible for the matrix degradation which occurs during bone resorption.