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Related Experiment Videos

NAADP receptors.

Antony Galione1, Margarida Ruas

  • 1Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, UK. antony.galione@pharm.ox.ac.uk

Cell Calcium
|August 23, 2005
PubMed
Summary
This summary is machine-generated.

Nicotinic acid adenine dinucleotide phosphate (NAADP) mobilizes Ca2+ via a novel channel, likely in acidic stores separate from the ER. Research in sea urchin eggs and mammalian cells advances understanding of this messenger.

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Area of Science:

  • Cellular biology
  • Molecular signaling
  • Calcium signaling

Background:

  • Nicotinic acid adenine dinucleotide phosphate (NAADP) is a potent Ca2+ messenger.
  • Its cellular levels fluctuate with agonist stimulation, confirming its signaling role.
  • NAADP interacts with other messengers like IP3 and cADPR to shape Ca2+ signals.

Purpose of the Study:

  • To elucidate the molecular identity and subcellular localization of the NAADP-sensitive Ca2+ release mechanism.
  • To review recent progress in understanding NAADP signaling, particularly in sea urchin eggs.
  • To discuss strategies for identifying NAADP-binding proteins.

Main Methods:

  • Review of recent scientific literature on NAADP signaling.
  • Focus on studies using sea urchin eggs as a model system.

Related Experiment Videos

  • Comparison of findings in sea urchin eggs with data from mammalian cells.

    • Main Results:

    • NAADP activates a novel Ca2+ release channel distinct from IP3 and ryanodine receptors.
    • The NAADP-sensitive Ca2+ store is likely an acidic compartment, separate from the endoplasmic reticulum (ER).
    • Evidence suggests similar mechanisms may operate in mammalian cells.

    Conclusions:

    • NAADP-mediated Ca2+ signaling involves a unique release channel and acidic intracellular stores.
    • Further characterization of NAADP-binding proteins is crucial for understanding its precise role.
    • Developing selective tools will enhance the study of NAADP-mediated Ca2+ signaling.