Selective non-lipid modulator of LPA5 activity in human platelets

Bioorg Med Chem Lett. 2012 Aug 15;22(16):5239-43. doi: 10.1016/j.bmcl.2012.06.057. Epub 2012 Jun 27.

Abstract

Lysophosphatidic acid (LPA) is a potent activator of human platelets in vitro. Recently, the G protein-coupled receptor LPA5/GPR92 has been identified to be the relevant LPA receptor responsible for the activation of human platelets by LPA. In a high-throughput screening campaign we identified a diphenyl pyrazole carboxylic acid as a small-molecule inhibitor for LPA5. Confirmation for the specificity of this small molecule was achieved in human platelets as the relevant cellular in vitro model. We could confirm using antagonists for alternative LPA receptors that we identified in our work the first non-lipid, small-molecule inhibitor for LPA5/GPR92 specifically inhibiting LPA-mediated platelet activation in vitro.

MeSH terms

  • Binding Sites
  • Blood Platelets / metabolism*
  • Computer Simulation
  • Humans
  • Lysophospholipids / chemistry*
  • Lysophospholipids / pharmacology
  • Platelet Activation / drug effects
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism
  • Protein Structure, Tertiary
  • Receptors, Lysophosphatidic Acid / chemistry*
  • Receptors, Lysophosphatidic Acid / metabolism

Substances

  • LPAR5 protein, human
  • Lysophospholipids
  • Protein Isoforms
  • Receptors, Lysophosphatidic Acid
  • lysophosphatidic acid