Procoagulant and prothrombotic activation of human erythrocytes by phosphatidic acid

Am J Physiol Heart Circ Physiol. 2010 Aug;299(2):H347-55. doi: 10.1152/ajpheart.01144.2009. Epub 2010 May 21.

Abstract

Increased phosphatidic acid (PA) and phospholipase D (PLD) activity are frequently observed in various disease states including cancers, diabetes, sepsis, and thrombosis. Previously, PA has been regarded as just a precursor for lysophosphatidic acid (LPA) and diacylglycerol (DAG). However, increasing evidence has suggested independent biological activities of PA itself. In the present study, we demonstrated that PA can enhance thrombogenic activities in human erythrocytes through phosphatidylserine (PS) exposure in a Ca(2+)-dependent manner. In freshly isolated human erythrocytes, treatment of PA or PLD induced PS exposure. PA-induced PS exposure was not attenuated by inhibitors of phospholipase A(2) or phosphatidate phosphatase, which converts PA to LPA or DAG. An intracellular Ca(2+) increase and the resultant activation of Ca(2+)-dependent PKC-alpha appeared to underlie the PA-induced PS exposure through the activation of scramblase. A marginal decrease in flippase activity was also noted, contributing further to the maintenance of exposed PS on the outer membrane. PA-treated erythrocytes showed strong thrombogenic activities, as demonstrated by increased thrombin generation, endothelial cell adhesion, and erythrocyte aggregation. Importantly, these procoagulant activations by PA were confirmed in a rat in vivo venous thrombosis model, where PA significantly enhanced thrombus formation. In conclusion, these results suggest that PA can induce thrombogenic activities in erythrocytes through PS exposure, which can increase thrombus formation and ultimately contribute to the development of cardiovascular diseases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blood Coagulation* / drug effects
  • Calcium / blood
  • Cell Adhesion
  • Cells, Cultured
  • Disease Models, Animal
  • Endothelial Cells / metabolism
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Erythrocyte Aggregation
  • Erythrocyte Membrane / drug effects
  • Erythrocyte Membrane / metabolism*
  • Erythrocytes / drug effects
  • Erythrocytes / metabolism*
  • Humans
  • Male
  • Phosphatidate Phosphatase / antagonists & inhibitors
  • Phosphatidate Phosphatase / metabolism
  • Phosphatidic Acids / blood*
  • Phosphatidylserines / blood
  • Phospholipase A2 Inhibitors
  • Phospholipase D / blood
  • Phospholipases A2 / blood
  • Phospholipid Transfer Proteins / metabolism
  • Protein Kinase C-alpha / blood
  • Rats
  • Rats, Sprague-Dawley
  • Thrombin / metabolism
  • Thromboplastin
  • Thrombosis / blood*
  • Thrombosis / chemically induced
  • Time Factors

Substances

  • Enzyme Inhibitors
  • Phosphatidic Acids
  • Phosphatidylserines
  • Phospholipase A2 Inhibitors
  • Phospholipid Transfer Proteins
  • Thromboplastin
  • PRKCA protein, human
  • Protein Kinase C-alpha
  • Phospholipases A2
  • Phosphatidate Phosphatase
  • Phospholipase D
  • Thrombin
  • Calcium