FEBS Letters | |
Tumor necrosis factor bifunctionally regulates matrix metalloproteinases and tissue inhibitor of metalloproteinases (TIMP) production by human fibroblasts | |
Mori, Yo1  Iga, Tatsuya1  Sato, Takashi1  Ito, Akira1  | |
[1]Department of Biochemistry, Tokyo College of Pharmacy, Horinouchi, Hachioji, Tokyo 192-03, Japan | |
关键词: Tumor necrosis factor; Matrix metalloproteinase; Collagenase; Stromelysin; Tissue inhibitor of metalloproteinase; Interleukin-1; Human fibroblast; TNF; tumor necrosis factor; hrTNF; human recombinant TNFα; TIMP; tissue inhibitor of metalloproteinases; MMP; matrix metalloproteinase; IL-1; interleukin-1; hrIL-1; human recombinant IL-1α; MEM; Eagle's minimum essential medium; FBS; fetal bovine serum; LAH; lactalbumin hydrolysate; SDS-PAGE; sodium dodecyl sulfate-polyacrylamide gel electrophoresis; | |
DOI : 10.1016/0014-5793(90)81127-A | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The production of tissue inhibitor of metalloproteinases (TIMP) in human uterine cervical fibroblasts was increased by human recombinant tumor necrosis factor α (hrTNF) at a low concentration (0.005 ) but the elevated synthesis was suppressed in a dose-dependent manner at higher concentrations (up to 50 ). In contrast, the production of collagenase (EC 3.4.24.7) and stromelysin was stimulated at all the corresponding concentrations. In contrast, human recombinant interleukin-1α (hrIL-1, 10 ) coordinately induced these enzymes and TIMP production. The reduction of the elevated TIMP production by TNF was not due to the inhibition of TIMP secretion. These results suggest that TNF modulates the extracellular matrix degradation in human fibroblasts bifunctionally by the suppression of TIMP production in addition to the acceleration of matrix metalloproteinases production. Furthermore, the fact that TNF and IL-1 differently controlled the production of TIMP suggests that the signal pathway of TNF for TIMP production is different from that of IL-1.
【 授权许可】
Unknown
【 预 览 】
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