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Related Experiment Videos

Receptor- and phorbol ester-mediated phospholipase D activation in rat parotid involves two different pathways

I Guillemain1, B Rossignol

  • 1Laboratoire de Biochimie des Transports Cellulaires, Centre National de la Recherche Scientifique, Unité de Recherche Associée 1116, Université Paris-Sud, Orsay, France.

The American Journal of Physiology
|March 1, 1994
PubMed
Summary

Phospholipase D (PLD) activation in rat parotid acini occurs via distinct pathways. Receptor-mediated agonists trigger a calcium-dependent PLD activation, while phorbol esters activate it independently of calcium.

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Area of Science:

  • Biochemistry
  • Cellular Signaling
  • Enzymology

Background:

  • Phospholipase D (PLD) is an enzyme involved in membrane phospholipid metabolism.
  • Understanding PLD regulation is crucial for comprehending cellular signaling pathways.
  • Rat parotid acini are a model system for studying exocrine gland secretion and signaling.

Purpose of the Study:

  • To investigate the mechanisms regulating phospholipase D (PLD) activation in rat parotid acini.
  • To determine the role of protein kinase C (PKC) and calcium in PLD activation.
  • To elucidate the distinct pathways involved in PLD activation by different stimuli.

Main Methods:

  • Rat parotid acini were prelabeled with [14C]stearic acid.
  • PLD activity was assessed by measuring the formation of [14C]phosphatidylethanol in the presence of ethanol.

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  • Stimulation was achieved using muscarinic and alpha-adrenergic agonists, calcium ionophore (ionomycin), and phorbol esters (PMA, PDBu).
  • Inhibition studies were performed using protein kinase C inhibitors (chelerythrine, staurosporine).

    • Main Results:

    • Muscarinic and alpha-adrenergic agonists stimulated PLD activity, leading to phosphatidylethanol formation.
    • Ionomycin and phorbol esters (PMA, PDBu) also stimulated phosphatidylethanol accumulation.
    • 1-oleyl-2-acetyl-sn-glycerol (OAG) did not affect PLD activity.
    • Protein kinase C inhibitors did not alter the observed responses, suggesting PKC is not involved.
    • A differential requirement for extracellular calcium was observed between receptor-mediated agonists and phorbol esters.
    • PLD activation did not alter phosphatidic acid levels.

    Conclusions:

    • PLD activation in rat parotid acini involves distinct pathways: a calcium-dependent route activated by receptor agonists and a calcium-independent route activated by phorbol esters.
    • Protein kinase C is not implicated in the regulation of PLD activity in this model.
    • The phosphatidyl transferase activity of PLD may represent a metabolic pathway, potentially facilitating a base-exchange reaction in the parotid gland.