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人胎盘线粒体中N-218 MLN64的熔球结构与类固醇生成活性

Molten globule structure and steroidogenic activity of N-218 MLN64 in human placental mitochondria.

作者信息

Tuckey Robert C, Bose Himangshu S, Czerwionka Inez, Miller Walter L

机构信息

Department of Biochemistry and Molecular Biology, School of Biomedical and Chemical Sciences, The University of Western Australia, Crawley, Australia.

出版信息

Endocrinology. 2004 Apr;145(4):1700-7. doi: 10.1210/en.2003-1034. Epub 2004 Jan 8.

Abstract

Progesterone synthesis by the human placenta requires the conversion of mitochondrial cholesterol to pregnenolone by cytochrome P450scc. Most steroidogenic tissues use the steroidogenic acute regulatory protein (StAR) to deliver cholesterol to the inner mitochondrial membrane where P450scc is located, but StAR is not expressed in the human placenta. However, the human placenta does express MLN64, which has a C-terminal domain homologous to StAR that can also transport cholesterol. We investigated the ability of bacterially expressed N-218 MLN64 and N-62 StAR to transport cholesterol between artificial membranes and to its inner membrane site of use in placental mitochondria. Urea denaturation experiments show that N-218 MLN64 undergoes a pH-dependent and denaturant-dependent structural transition to a molten globule state, as reported previously for N-62 StAR. N-218 MLN64 stimulated cholesterol transfer between artificial phospholipid vesicles with an initial rate of 6.5 mol/min.mol N-218 MLN64. Both N-218 MLN64 and N-62 StAR stimulated cholesterol transfer to the inner mitochondrial membrane, as evidenced by a 6-fold stimulation of pregnenolone synthesis with saturating transporter. This stimulation was seen only after the endogenous cholesterol in the steroidogenic pool of the isolated mitochondria was first depleted. No stimulation was observed by N-218 MLN64 or N-62 StAR when 20alpha-hydroxycholesterol was added as substrate for P450scc, confirming that these proteins stimulate P450scc activity by enhancing cholesterol transport. MLN64 levels in placental JEG-3 cells were unresponsive to stimulation by 8-bromo-cAMP over 24 h. These data show that human N-218 MLN64 and N-62 StAR have similar biophysical and functional properties and are able to stimulate steroidogenesis in a human placental system, which normally lacks StAR. The results reveal that with saturating MLN64, steroidogenesis by placental mitochondria proceeds at near-maximal rate.

摘要

人胎盘的孕酮合成需要细胞色素P450scc将线粒体胆固醇转化为孕烯醇酮。大多数类固醇生成组织利用类固醇生成急性调节蛋白(StAR)将胆固醇转运至P450scc所在的线粒体内膜,但人胎盘中不表达StAR。然而,人胎盘确实表达MLN64,其C端结构域与StAR同源,也能转运胆固醇。我们研究了细菌表达的N-218 MLN64和N-62 StAR在人工膜之间转运胆固醇以及将其转运至胎盘线粒体内膜使用位点的能力。尿素变性实验表明,如先前报道的N-62 StAR一样,N-218 MLN64经历了pH和变性剂依赖性的结构转变,形成熔球状态。N-218 MLN64刺激人工磷脂囊泡之间的胆固醇转移,初始速率为6.5 mol/min·mol N-218 MLN64。N-218 MLN64和N-62 StAR均刺激胆固醇向线粒体内膜的转移,饱和转运体使孕烯醇酮合成增加6倍即证明了这一点。这种刺激仅在分离线粒体的类固醇生成池中内源性胆固醇首先耗尽后才出现。当添加20α-羟基胆固醇作为P450scc的底物时,未观察到N-218 MLN64或N-62 StAR的刺激作用,证实这些蛋白通过增强胆固醇转运来刺激P450scc活性。胎盘JEG-3细胞中的MLN64水平在24小时内对8-溴-cAMP的刺激无反应。这些数据表明,人N-218 MLN64和N-62 StAR具有相似的生物物理和功能特性,并且能够在通常缺乏StAR的人胎盘系统中刺激类固醇生成。结果表明,在MLN64饱和的情况下,胎盘线粒体的类固醇生成以接近最大速率进行。

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