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首页> 外文期刊>Journal of Cellular Physiology >Tissue inhibitor of metalloproteinase-2 (TIMP-2) expression is strongly induced by ACTH in adrenocortical cells.
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Tissue inhibitor of metalloproteinase-2 (TIMP-2) expression is strongly induced by ACTH in adrenocortical cells.

机译：组织抑制剂metalloproteinase-2 (TIMP-2)表达强烈诱导ACTH的肾上腺皮质细胞。

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Besides its acute and chronic effects on corticosteroid synthesis, the pituitary adrenocorticotropic hormone (ACTH) regulates diverse adrenocortical biological functions including the synthesis of a number of mitochondrial, cytoplasmic, and secreted proteins. ACTH-induced secreted proteins are candidates to act as local extracellular relays of the hormone in either an autocrine or a paracrine manner. In the present study, we report that stimulation of primary cultures of bovine adrenocortical (BAC) fasciculata cells with 10 nM ACTH for 24 h results in a mean 8 +/- 4-fold induction of the synthesis of a secreted protein presenting an apparent Mr of 21 kDa. Peptide microsequencing and Western blotting allowed us to identify this 21-kDa ACTH-induced protein as the tissue inhibitor of metalloproteinase-2 (TIMP-2). The induction of TIMP-2 by ACTH required transcription, was mimicked by 8-bromo cyclic 3'-5' adenosine monophosphate, but was not observed in response to angiotensin II, IGF-1, fibroblast growth factor-2, transforming growth factor-beta1, or cortisol treatments. ACTH stimulated TIMP-2 mRNA levels by a factor 4, whereas TIMP-1 mRNA levels were not affected and TIMP-3 mRNA remained undetectable. The biological activity of TIMP-2 varied accordingly, as we observed that the conditioned medium of ACTH-treated BAC cells was four times more potent at inhibiting gelatinolytic activity than was the conditioned medium of control cells. Because the proteolytic activity of both progelatinase-B and progelatinase-A secreted by BAC cells remained latent, whether in the presence or in the absence of ACTH, a paracrine rather than autocrine role is proposed for TIMP-2 in the adrenal cortex.
机译：除了它的急性和慢性影响皮质类固醇合成、垂体促肾上腺皮质激素(ACTH)调节不同的肾上腺皮质的生物功能包括合成的线粒体、胞质和分泌蛋白质。候选人作为局部细胞外的继电器一个自分泌或激素的旁分泌方式。刺激的牛的主要文化肾上腺皮质细胞(BAC)下方10纳米ACTH 24 h平均8 + / - 4倍诱导分泌蛋白的合成呈现一个明显21 kDa的先生。microsequencing和免疫印迹允许我们确定这个21-kDa ACTH-induced蛋白质metalloproteinase-2组织抑制剂(TIMP-2)。所需的转录,被8-bromo模仿循环3 ' 5 '磷酸腺苷,但不是观察血管紧张素ⅱ,igf - 1,纤维母细胞生长因子2,将增长factor-beta1或皮质醇治疗。刺激TIMP-2 mRNA水平4倍,而TIMP-1 mRNA水平没有影响TIMP-3 mRNA仍然发现不了的。TIMP-2各种相应的活动,因为我们观察到的条件培养基ACTH-treated BAC细胞更有效的四倍在抑制比是gelatinolytic活动控制细胞条件培养基。蛋白水解progelatinase-B和活动progelatinase-A仍由BAC分泌细胞潜在的,是否存在或没有ACTH的旁分泌而不是自分泌作用提出了TIMP-2肾上腺皮质。

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