Signal transduction from bradykinin, angiotensin, adrenergic and muscarinic receptors to effector enzymes, including ADP-ribosyl cyclase

H. Higashida, S. Yokoyama, N. Hoshi, M. Hashii, A. Egorova, Z. G. Zhong, M. Noda, M. Shahidullah, M. Taketo, R. Knijnik, Y. Kimura, H. Takahashi, X. L. Chen, Y. Shin, J. S. Zhang

Research output: Contribution to journalReview article

20 Citations (Scopus)

Abstract

Muscarinic acetylcholine receptors in NG108-15 neuroblastoma x glioma cells, and β-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 β-NAD+. This signal cascade is analogous to the previously established transduction pathways from bradykinin receptors to phospholipase Cβ and β-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 Gq/11-coupled receptors can control cADPR-dependent modulation in Ca2+ signaling.

Original languageEnglish
Pages (from-to)23-30
Number of pages8
JournalBiological chemistry
Volume382
Issue number1
DOIs
Publication statusPublished - 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry

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    Higashida, H., Yokoyama, S., Hoshi, N., Hashii, M., Egorova, A., Zhong, Z. G., Noda, M., Shahidullah, M., Taketo, M., Knijnik, R., Kimura, Y., Takahashi, H., Chen, X. L., Shin, Y., & Zhang, J. S. (2001). Signal transduction from bradykinin, angiotensin, adrenergic and muscarinic receptors to effector enzymes, including ADP-ribosyl cyclase. Biological chemistry, 382(1), 23-30. https://doi.org/10.1515/BC.2001.004