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性附属组织中激素反应的组织特异性与核基质蛋白模式相关。

Tissue specificity of the hormonal response in sex accessory tissues is associated with nuclear matrix protein patterns.

作者信息

Getzenberg R H, Coffey D S

机构信息

Department of Urology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

出版信息

Mol Endocrinol. 1990 Sep;4(9):1336-42. doi: 10.1210/mend-4-9-1336.

Abstract

The DNA of interphase nuclei have very specific three-dimensional organizations that are different in different cell types, and it is possible that this varying DNA organization is responsible for the tissue specificity of gene expression. The nuclear matrix organizes the three-dimensional structure of the DNA and is believed to be involved in the control of gene expression. This study compares the nuclear structural proteins between two sex accessory tissues in the same animal responding to the same androgen stimulation by the differential expression of major tissue-specific secretory proteins. We demonstrate here that the nuclear matrix is tissue specific in the rat ventral prostate and seminal vesicle, and undergoes characteristic alterations in its protein composition upon androgen withdrawal. Three types of nuclear matrix proteins were observed: 1) nuclear matrix proteins that are different and tissue specific in the rat ventral prostate and seminal vesicle, 2) a set of nuclear matrix proteins that either appear or disappear upon androgen withdrawal, and 3) a set of proteins that are common to both the ventral prostate and seminal vesicle and do not change with the hormonal state of the animal. Since the nuclear matrix is known to bind androgen receptors in a tissue- and steroid-specific manner, we propose that the tissue specificity of the nuclear matrix arranges the DNA in a unique conformation, which may be involved in the specific interaction of transcription factors with DNA sequences, resulting in tissue-specific patterns of secretory protein expression.

摘要

间期细胞核的DNA具有非常特定的三维结构组织,这种结构在不同细胞类型中有所不同,而且这种不同的DNA组织有可能是基因表达的组织特异性的原因。核基质组织着DNA的三维结构,并被认为参与基因表达的调控。本研究通过主要组织特异性分泌蛋白的差异表达,比较了同一动物中两种性附属组织在相同雄激素刺激下的核结构蛋白。我们在此证明,大鼠腹侧前列腺和精囊中的核基质具有组织特异性,并且在雄激素撤除后其蛋白质组成会发生特征性改变。观察到三种类型的核基质蛋白:1)在大鼠腹侧前列腺和精囊中不同且具有组织特异性的核基质蛋白;2)一组在雄激素撤除后出现或消失的核基质蛋白;3)一组腹侧前列腺和精囊共有的、且不随动物激素状态改变的蛋白质。由于已知核基质以组织和类固醇特异性的方式结合雄激素受体,我们提出核基质的组织特异性将DNA排列成独特的构象,这可能参与转录因子与DNA序列的特异性相互作用,从而导致分泌蛋白表达的组织特异性模式。

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