Signal transduction from bradykinin, angiotensin, adrenergic and muscarinic receptors to effector enzymes, including ADP-ribosyl cyclase
| Autor: | Hiroto Takahashi, Haruhiro Higashida, Alla Egorova, Naoto Hoshi, Yasuhiro Kimura, Mami Noda, Shigeru Yokoyama, Jiasheng Zhang, Zhen-Guo Zhong, Xiao-Liang Chen, Minako Hashii, Rimma Knijnik, Megumi Taketo, Yeonsook Shin, Mohammad Shahidullah |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
ADP-ribosyl Cyclase
Angiotensin receptor Angiotensins G protein Clinical Biochemistry Bradykinin Biochemistry Adenylyl cyclase chemistry.chemical_compound NAD+ Nucleosidase Antigens CD Animals Humans Bradykinin receptor Receptor Molecular Biology Membrane Glycoproteins Ryanodine receptor ADP-ribosyl Cyclase 1 Antigens Differentiation Receptors Muscarinic Cell biology Enzymes Receptors Adrenergic chemistry Signal transduction Signal Transduction |
| Zdroj: | Biological chemistry. 382(1) |
| ISSN: | 1431-6730 |
| Popis: | Muscarinic acetylcholine receptors in NG108-15 neuroblastoma x glioma cells, and beta-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 beta-NAD+. This signal cascade is analogous to the previously established transduction pathways from bradykinin receptors to phospholipase Cbeta and beta-adrenoceptors to adenylyl cyclase via G proteins. Upon receptor stimulation, the newly-formed 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-binding-protein, and calcineurin, or ryanodine receptors. cADPR also functions through activating calcineurin released from A-kinase anchoring protein (AKAP79). Thus, some G(q/11)-coupled receptors can control cADPR-dependent modulation in Ca2+ signaling. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|