HORMONAL-REGULATION OF COLLAGENOLYSIS IN UTERINE CERVICAL FIBROBLASTS - MODULATION OF SYNTHESIS OF PROCOLLAGENASE, PROSTROMELYSIN AND TISSUE INHIBITOR OF METALLOPROTEINASES (TIMP) BY PROGESTERONE AND ESTRADIOL-17-BETA

被引:141
作者
SATO, T
ITO, A
MORI, Y
YAMASHITA, K
HAYAKAWA, T
NAGASE, H
机构
[1] TOKYO COLL PHARM,DEPT BIOCHEM,HACHIOJI,TOKYO 19203,JAPAN
[2] AICHI GAKUIN UNIV,SCH DENT,DEPT BIOCHEM,CHIKUSA KU,NAGOYA 464,JAPAN
[3] UNIV KANSAS,MED CTR,DEPT BIOCHEM & MOLEC BIOL,KANSAS CITY,KS 66103
关键词
D O I
10.1042/bj2750645
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Rabbit uterine cervical fibroblasts produced a large amount of matrix metalloproteinases (MMPs) such as collagenase (MMP-1) and stromelysin (MMP-3) and a small relatively amount of tissue inhibitor of metalloproteinases (TIMP). When cells were treated with progesterone or oestradiol-17-beta, both steroids concurrently decreased the level of procollagenase and prostromelysin in the culture media and the steady-state levels of the respective mRNAs. On the other hand, the level of TIMP in the culture media and the steady-state level of its mRNA were simultaneously increased by these steroids. Similarly, the suppression of production of MMPs and the augmentation of TIMP production by both steroids were observed with interleukin 1 (IL-1)-treated cells, but the action of progesterone was more effective than that of oestradiol-17-beta in the IL-1-untreated and -treated cells. These results suggest that collagenolysis in uterine cervical fibroblasts is negatively regulated by steroid hormones via the acceleration of TIMP production and the suppression of synthesis of MMPs at the pretranslational level.
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页码:645 / 650
页数:6
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