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Related Experiment Videos

Elevated cytosolic Ca2+ activates phospholipase D in human platelets.

R Huang1, G L Kucera, S E Rittenhouse

  • 1Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405.

The Journal of Biological Chemistry
|January 25, 1991
PubMed
Summary

Alpha-thrombin activates phospholipase D in human platelets. Increased intracellular calcium, not protein kinase C, regulates this enzyme, with phospholipase D contributing 13% to phosphatidic acid accumulation.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Hematology

Background:

  • Platelet activation is crucial for hemostasis and thrombosis.
  • Phospholipase D (PLD) plays a role in cellular signaling pathways.
  • Understanding PLD regulation in platelets is important for cardiovascular research.

Purpose of the Study:

  • To investigate the activation mechanism of phospholipase D in human platelets stimulated by alpha-thrombin.
  • To determine the roles of intracellular calcium and protein kinase C in PLD activation.
  • To quantify the relative contributions of PLD and other pathways to phosphatidic acid formation.

Main Methods:

  • Human platelets were labeled with radioactive precursors to track lipid metabolism.
  • Platelets were stimulated with alpha-thrombin, calcium ionophore A23187, or phorbol ester.

Related Experiment Videos

  • Formation of labeled phosphatidic acid (PtdOH) and diglyceride was measured.
  • Inhibition studies using staurosporine assessed the role of protein kinase C.
  • Radioisotope analysis quantified the contribution of different enzymatic pathways to PtdOH accumulation.

    • Main Results:

    • Alpha-thrombin and A23187 stimulated time- and concentration-dependent formation of labeled phosphatidic acid (PtdOH).
    • Increased intracellular calcium, induced by A23187, mimicked alpha-thrombin's effect on PtdOH production.
    • Protein kinase C activation had minimal effect on PtdOH accumulation, and its inhibition only slightly affected alpha-thrombin-induced PtdOH.
    • Phospholipase D accounted for 13% of the incremental PtdOH, while phospholipase C followed by diglyceride kinase contributed 87%.

    Conclusions:

    • Intracellular calcium increase is a primary regulator of phospholipase D activity in alpha-thrombin-stimulated human platelets.
    • Protein kinase C activity is not the major determinant of PLD-mediated PtdOH production in this context.
    • The phospholipase C/diglyceride kinase pathway is the dominant source of phosphatidic acid accumulation in activated platelets.