Goniothalamin induces coronary artery smooth muscle cells apoptosis: the p53-dependent caspase-2 activation pathway

Toxicol Sci. 2010 Aug;116(2):533-48. doi: 10.1093/toxsci/kfq151. Epub 2010 May 24.

Abstract

Goniothalamin (GN), a styryl-lactone isolated from Goniothalamus andersonii, has been demonstrated to possess antirestenostic properties by inducing apoptosis on coronary artery smooth muscle cells (CASMCs). In this study, the molecular mechanisms of GN-induced CASMCs apoptosis were further elucidated. Apoptosis assessment based on the externalization of phosphatidylserine demonstrated that GN induces CASMCs apoptosis in a concentration-dependent manner. The GN-induced DNA damage occurred with concomitant elevation of p53 as early as 2 h, demonstrating an upstream signal for apoptosis. However, the p53 elevation in GN-treated CASMCs was independent of NAD(P)H: quinone oxidoreductase 1 and Mdm-2 expression. An increase in hydrogen peroxide and reduction in free thiols confirmed the role for oxidative stress in GN treatment. Pretreatment with the pan-caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone (z-VAD-FMK) that significantly abrogated GN-induced CASMCs apoptosis suggested the involvement of caspase(s). The role of apical caspase-2, -8, and -9 was then investigated, and sequential activation of caspase-2 and -9 but not caspase-8 leading to downstream caspase-3 cleavage was observed in GN-treated CASMCs. Reduction of ATP level and decrease in oxygen consumption further confirmed the role of mitochondria in GN-induced apoptosis in CASMCs. The mitochondrial release of cytochrome c was seen without mitochondrial membrane potential loss and was independent of cardiolipin. These data provide insight into the mechanisms of GN-induced apoptosis, which may have important implications in the development of drug-eluting stents.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / analysis
  • Amino Acid Chloromethyl Ketones / pharmacology
  • Apoptosis / drug effects*
  • Caspase 2 / metabolism*
  • Cells, Cultured
  • Cytochromes c / metabolism
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Humans
  • Hydrogen Peroxide / metabolism
  • Membrane Potential, Mitochondrial / drug effects
  • Muscle, Smooth, Vascular / drug effects*
  • Myocytes, Smooth Muscle / drug effects*
  • NAD(P)H Dehydrogenase (Quinone) / metabolism
  • Oxygen Consumption / drug effects
  • Pyrones / toxicity*
  • Superoxides / metabolism
  • Tumor Suppressor Protein p53 / physiology*

Substances

  • Amino Acid Chloromethyl Ketones
  • Pyrones
  • Tumor Suppressor Protein p53
  • benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
  • Superoxides
  • goniothalamin
  • Adenosine Triphosphate
  • Cytochromes c
  • Hydrogen Peroxide
  • NAD(P)H Dehydrogenase (Quinone)
  • NQO1 protein, human
  • Caspase 2