Marbaix E, Donnez J, Courtoy P J, Eeckhout Y
Cell Biology Unit, International Institute of Cellular and Molecular Pathology, Bruxelles, Belgium.
Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11789-93. doi: 10.1073/pnas.89.24.11789.
Explants of human endometrium were cultured to study the release of matrix metalloproteinases (MMPs). Analysis of conditioned media by zymography revealed latent and active forms of collagenase (MMP-1, EC 3.4.24.7), 72-kDa gelatinase A (MMP-2, EC 3.4.24.24), and 92-kDa gelatinase B (MMP-9, EC 3.4.24.35). These proteinases were identified by their M(r), their inhibition by tissue inhibitor of metalloproteinases, and the activation of their zymogens by trypsin or aminophenylmercuric acetate. In the absence of sex hormone, explants released large amounts of enzyme activities, as measured by densitometry of zymograms or in soluble assays. Physiological concentrations of progesterone (10-200 nM) almost totally abolished the release of collagenase, of total gelatinase activity, and of the active form of gelatinase B and largely inhibited the release of the active form of gelatinase A. These effects, which were antagonized by mifepristone (RU 38486), suggest that progesterone restrains endometrial tissue breakdown by blocking the secretion and activation of MMPs.
培养人子宫内膜外植体以研究基质金属蛋白酶（MMPs）的释放。通过酶谱法分析条件培养基，发现了胶原酶（MMP-1，EC 3.4.24.7）、72 kDa明胶酶A（MMP-2，EC 3.4.24.24）和92 kDa明胶酶B（MMP-9，EC 3.4.24.35）的潜伏形式和活性形式。这些蛋白酶通过其相对分子质量、金属蛋白酶组织抑制剂对其的抑制作用以及胰蛋白酶或氨基苯基汞乙酸对其酶原的激活作用来鉴定。在没有性激素的情况下，通过酶谱密度测定法或可溶性测定法测量，外植体释放大量的酶活性。生理浓度的孕酮（10 - 200 nM）几乎完全消除了胶原酶、总明胶酶活性以及明胶酶B活性形式的释放，并在很大程度上抑制了明胶酶A活性形式的释放。米非司酮（RU 38486）可拮抗这些作用，提示孕酮通过阻断MMPs的分泌和激活来抑制子宫内膜组织分解。
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