Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Curr Med Chem. 2004 Apr;11(7):847-55.

Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR).

Author information

  • University Hospital Hamburg-Eppendorf, Center of Experimental Medicine, Institute of Biochemistry and Molecular Biology I: Cellular Signal Transduction, Martinistr. 52, 20246 Hamburg, Germany. guse@uke.uni-hamburg.de

Abstract

Cyclic adenosine diphosphoribose (cADPR) is an endogenous Ca2+ mobilizing nucleotide in many cell types and different species covering protozoa, plants and animals, including humans. cADPR is formed by ADP-ribosyl cyclases from nicotinamide adenine dinucleotide (NAD). Since at least some of the ADP-ribosyl cyclases are under the control of receptors for exogenous ligands, cADPR is regarded as a second messenger for Ca2+ signaling. The main intracellular target for cADPR is the ryanodine receptor, but it is unclear whether cADPR elicits Ca2+ release by direct binding or via a binding protein. Derivatives of NAD and cADPR are potent ADP-ribosyl cyclase inhibitors and cADPR antagonists. Since Ca2+ ions are regulators of many diverse cell functions, e.g. muscle contraction, secretion of neurotransmitters, hormones and enzymes, fertilization of oocytes, and lymphocyte activation and proliferation, the cADPR signaling pathway may become a valuable target for pharmaceutical intervention.

PMID:
15078169
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Bentham Science Publishers Ltd.
    Loading ...
    Write to the Help Desk