From vasopressin receptor to water channel: intracellular traffic, constraint and by-pass.
From vasopressin receptor to water channel: intracellular traffic, constraint and by-pass.
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从加压素受体到水通道：细胞内交通、约束和旁路。
DOI：
--
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发表时间：
1998
影响因子：
4
通讯作者：
Jacques Hanoune
中科院分区：
文献类型：
--
作者：
John Laycock;Jacques Hanoune
抗利尿激素加压素 (VP) 在位于下丘脑视上核和室旁核的大细胞神经元细胞体中合成，并从垂体后叶（神经垂体）的神经末梢释放到体循环中。 VP 合成和释放的生理控制主要与血浆渗透压的变化有关，血浆渗透压是由位于血脑屏障之外的下丘脑前部区域的专门渗透压感受器检测到的。穹窿下器官和终板血管器（例如 Thrasher 等人，1982 年；Yang 等人，1994 年）。尽管连接渗透压感受器激活与VP释放的精确途径仍有待确定，但一氧化氮是最近被证明是下丘脑-神经垂体系统响应渗透压刺激的抑制性调节剂的一种分子（Ota等人，1993年，Yasin等人，1993年，Kadowaki等人，1994年，Wang＆Morris，1996年）。此外，抑制途径将血压与 VP 的释放联系起来，因此压力感受器检测到的动脉血压或心脏容量感受器检测到的中心静脉压的增加会抑制通过腹外侧髓质的神经元投射释放激素（Head et al. 1987，McAllen & Blessing 1987）。其他中心预测也涉及总体 VP 监管。尽管 VP 在包括脉管系统和中枢神经系统在内的多个部位具有生理作用，但其主要生理作用是众所周知的水重吸收增加，在渗透梯度存在的情况下，肾集合管中会发生水重吸收，从而产生抗利尿作用，因此它的同义词是抗利尿激素 (ADH)。在与加压素的各种作用相关的三种主要受体（V1a、V1b 和 V2）中，V2 受体介导集合管中的抗利尿作用。该受体位于内髓集合管（起始段和终末段）和外髓集合管以及皮质拱廊的加压素敏感主细胞的基底外侧膜中。 V2 受体在大鼠（Lolait 等人，1992 年）和人类（Birnbaumer 等人，1992a）中克隆，是具有七个膜内片段、三个细胞外结构域和四个细胞内结构域的蛋白质家族的成员。该受体通过膜上的异三聚体 G 蛋白与腺苷酸环化酶 (AC) 连接；因此，AC 由于 VP 与其 V2 受体结合而被激活，导致第二信使环 AMP 的形成。随后的蛋白激酶 A 磷酸化与水重吸收的最后步骤相关。环 AMP 被细胞内磷酸二酯酶快速降解为 5*-AMP。虽然信号传导途径的各个中间阶段仍不清楚，但最近阐明了一个重要的最后步骤：将水通道插入靶细胞的顶（或腔）膜，介导快速跨膜水转运。在植物和动物中发现了一类称为水通道蛋白 (AQP) 的水通道。其中五种膜整合蛋白分布在从红细胞到眼睛晶状体的哺乳动物组织中，它们在其中介导水分运输（参见 Nielsen & Agre 1995，Knepper 1997），但只有一种（AQP2）对血管加压不敏感。这种最近克隆的分子（Fushimi 等人，1993）位于集合管细胞的顶膜和细胞质内，它们似乎储存在称为 aggraphores 的囊泡中（Harris 等人，1991；Nielsen 等人，1993）。在存在 VP 的情况下，顶膜中 AQP2 的存在立即增加，并且附菌孔向这些膜的运动增加，随后细胞内 AQP2 的产生长期增加，如免疫荧光测定（Marples 等人，1995a）。有证据表明微管可能与 VP 刺激的水运输有关（Phillips & Taylor 1989），可能与附菌孔向顶膜的运动有关。此外，VP 解聚大鼠内髓集合管细胞顶膜的肌动蛋白细胞骨架，这表明肌动蛋白网络可能与 Aggraphores 与顶膜的融合有关（Simon 等人，361）
The antidiuretic hormone vasopressin (VP) is synthesised in the magnocellular neurone cell bodies located in the hypothalamic supraoptic and paraventricular nuclei, and released into the general circulation from the nerve terminals in the posterior lobe of the pituitary gland (the neurohypophysis). Physiological control of the synthesis and release of VP is related mainly to changes in plasma osmolarity which are detected by specialised osmoreceptors in regions of the anterior hypothalamus which lie outside the blood–brain barrier e.g. in the subfornical organ and the organum vasculosa laminae terminalis (e.g. Thrasher et al. 1982, Yang et al. 1994). Although the precise pathways connecting osmoreceptor activation to VP release remain to be determined, nitric oxide is one molecule recently shown to be an inhibitory modulator of the hypothalamo–neurohypophysial system in response to osmotic stimuli (Ota et al. 1993, Yasin et al. 1993, Kadowaki et al. 1994, Wang & Morris 1996). In addition, an inhibitory pathway relates blood pressure to the release of VP, such that an increase either in arterial blood pressure detected by baroreceptors or in central venous pressure detected by cardiac volume receptors inhibits release of the hormone via a neuronal projection from the ventrolateral medulla (Head et al. 1987, McAllen & Blessing 1987). Other central projections are also involved in overall VP regulation. Although VP has physiological actions at multiple sites including the vasculature and the central nervous system, its principal physiological effect is the well-described increase in water reabsorption which takes place in the renal collecting ducts in the presence of an osmotic gradient resulting in an antidiuresis, hence its synonym antidiuretic hormone (ADH). Of the three principal receptors (V1a, V1b and V2) associated with the various effects of vasopressin, it is the V2 receptor which mediates the antidiuretic action in the collecting ducts. This receptor is located in the basolateral membranes of the vasopressin-sensitive principal cells of the inner (initial and terminal segments) and outer medullary collecting duct as well as the cortical arcades. The V2 receptor, cloned in the rat (Lolait et al. 1992) and in the human (Birnbaumer et al. 1992a), is a member of a family of proteins having seven intramembranous segments and three extracellular and four intracellular domains. The receptor is linked to adenylyl cyclase (AC) enzymes via heterotrimeric G proteins in the membrane; thus, AC is activated as a consequence of VP binding to its V2 receptor resulting in the formation of the second messenger cyclic AMP. Subsequent phosphorylation of protein kinase A is associated with the final step of water reabsorption. Cyclic AMP is rapidly degraded to 5*-AMP by intracellular phosphodiesterase enzymes. While various intermediate stages in the signalling pathway remain unclear, an important final step has recently been elucidated: the insertion of water channels into the apical (or luminal) membrane of the target cell, mediating rapid cross-membrane water transport. There is a family of water channels called aquaporins (AQP) which have been identified in plants and animals. Five of these membrane integral proteins are distributed in mammalian tissues ranging from erythrocytes to the lens of the eye where they mediate water transport (see Nielsen & Agre 1995, Knepper 1997), but only one (AQP2) is vasopressinsensitive. This recently cloned molecule (Fushimi et al. 1993) is located in the apical membranes of collecting duct cells, and within the cytoplasm, where they appear to be stored in vesicles called aggraphores (Harris et al. 1991, Nielsen et al. 1993). In the presence of VP there is an immediate increase in the presence of AQP2 in the apical membranes and an increased movement of aggraphores towards these membranes, followed by a longer-term increase in AQP2 production within the cells, as determined by immunofluorescence (Marples et al. 1995a). There is evidence that microtubules might be implicated in VP-stimulated water transport (Phillips & Taylor 1989), perhaps associated with the movement of aggraphores to the apical membrane. Furthermore, VP depolymerises the actin cytoskeleton of the apical membrane of rat inner medullary collecting duct cells, suggesting the possibility that the actin network might be associated with the fusion of aggraphores with the apical membrane (Simon et al. 361
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影响因子：
4.8
作者：
T. Thrasher;L. Keil;D. Ramsay
通讯作者：
T. Thrasher;L. Keil;D. Ramsay
DOI：
10.1152/ajprenal.1991.261.2.f345
发表时间：
1991-08
期刊：
The American journal of physiology
影响因子：
--
作者：
S. Homma;S. Gapstur;A. Coffey;H. Valtin;T. P. Dousa
通讯作者：
S. Homma;S. Gapstur;A. Coffey;H. Valtin;T. P. Dousa
培养的大鼠内髓集合管细胞中加压素刺激的磷酸肌醇水解是由催产素受体介导的。
DOI：
10.1172/jci115243
发表时间：
1991
期刊：
The Journal of clinical investigation
影响因子：
--
作者：
Teitelbaum,I
通讯作者：
Teitelbaum,I
加压素解聚大鼠内髓集合管中的顶端 F-肌动蛋白。
DOI：
10.1152/ajpcell.1993.265.3.c757
发表时间：
1993
期刊：
The American journal of physiology
影响因子：
--
作者：
Simon,H;Gao,Y;Franki,N;Hays,RM
通讯作者：
Hays,RM
双重信号传导潜力在 Gs 偶联受体中很常见，并且取决于受体密度。
影响因子：
3.6
作者：
Zhu,X;Gilbert,S;Birnbaumer,M;Birnbaumer,L
通讯作者：
Birnbaumer,L