Hormonal regulation of collagenolysis in uterine cervical fibroblasts. Modulation of synthesis of procollagenase, prostromelysin and tissue inhibitor of metalloproteinases (TIMP) by progesterone and oestradiol-17 β

Takashi Sato, Akira Itô, Yo Mori, Kyoko Yamashita, Taro Hayakawa, Hideaki Nagase
In: Biochemical Journal · 1991 · vol. 275(3) , pp. 645–650 · doi:10.1042/bj2750645 · PMID:1645518 · W1823810252
article OA: bronze CC0 ⤵ 3 in-corpus citations
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Progesterone and estradiol-17 beta decreased procollagenase and prostromelysin synthesis while increasing TIMP production in rabbit uterine cervical fibroblasts.

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Abstract

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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