作者
Volker Henn, Bayram Edemir, Eduard Stefan, Burkhard Wiesner, Dorothea Lorenz, Franziska Theilig, Roland Schmitt, Lutz Vossebein, Grazia Tamma, Michael Beyermann, Eberhard Krause, Friedrich W Herberg, Giovana Valenti, Sebastian Bachmann, Walter Rosenthal, Enno Klussmann
发表日期
2004/6/18
期刊
Journal of Biological Chemistry
卷号
279
期号
25
页码范围
26654-26665
出版商
Elsevier
简介
Arginine vasopressin (AVP) increases the water permeability of renal collecting duct principal cells by inducing the fusion of vesicles containing the water channel aquaporin-2 (AQP2) with the plasma membrane (AQP2 shuttle). This event is initiated by activation of vasopressin V2 receptors, followed by an elevation of cAMP and the activation of protein kinase A (PKA). The tethering of PKA to subcellular compartments by protein kinase A anchoring proteins (AKAPs) is a prerequisite for the AQP2 shuttle. During the search for AKAP(s) involved in the shuttle, a new splice variant of AKAP18, AKAP18δ, was identified. AKAP18δ functions as an AKAP in vitro and in vivo. In the kidney, it is mainly expressed in principal cells of the inner medullary collecting duct, closely resembling the distribution of AQP2. It is present in both the soluble and particulate fractions derived from renal inner medullary tissue. Within the …
引用总数
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