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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year



Signal Transduction from Bradykinin, Angiotensin, Adrenergic and Muscarinic Receptors to Effector Enzymes, Including ADP-Ribosyl Cyclase

Haruhiro Higashida / Shigeru Yokoyama / Naoto Hoshi / Minako Hashii / Alla Egorova / Zhen-Guo Zhong / Mami Noda / Mohammad Shahidullah / Megumi Taketo / Rimma Knijnik / Yasuhiro Kimura / Hiroto Takahashi / Xiao-Liang Chen / Yeonsook Shin / Jia-Sheng Zhang

Citation Information: Biological Chemistry. Volume 382, Issue 1, Pages 23–30, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2001.004, July 2005

Publication History

Published Online:


Muscarinic acetylcholine receptors in NG108-15 neuroblastoma x glioma cells, and ?-adrenergic or angiotensin II receptors in cortical astrocytes and/or ventricular myocytes, utilize the direct signaling pathway to ADP-ribosyl cyclase within cell membranes to produce cyclic ADP-ribose (cADPR) from ?-NAD+. This signal cascade is analogous to the previously established transduction pathways from bradykinin receptors to phospholipase C? and ?-adrenoceptors to adenylyl cyclase via G proteins. Upon receptor stimulation, the newlyformed cADPR may coordinately function to upregulate the release of Ca2+ from the type II ryanodine receptors as well as to facilitate Ca2+ influx through voltage-dependent Ca2+ channels. cADPR interacts with FK506, an immunosuppressant, at FKBP12.6, FK506-bindingprotein, and calcineurin, or ryanodine receptors. cADPR also functions through activating calcineurin released from Akinase anchoring protein (AKAP79). Thus, some Gq/11coupled receptors can control cADPR-dependent modulation in Ca2+ signaling.

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