LPA protects intestinal epithelial cells from apoptosis by inhibiting the mitochondrial pathway

Am J Physiol Gastrointest Liver Physiol. 2003 May;284(5):G821-9. doi: 10.1152/ajpgi.00406.2002.

Abstract

We previously showed (Gastroenterology 123: 206-216, 2002) that lysophosphatidic acid (LPA) protects and rescues rat intestinal epithelial cells (IEC-6) from apoptosis. Here, we provide evidence for the LPA-elicited inhibition of the mitochondrial apoptotic pathway leading to attenuation of caspase-3 activation. Pretreatment of IEC-6 cells with LPA inhibited campothecin-induced caspase-9 and caspase-3 activation and DNA fragmentation. A caspase-9 inhibitor peptide mimicked the LPA-elicited antiapoptotic activity. LPA elicited ERK1/ERK2 and PKB/Akt phosphorylation. The LPA-elicited antiapoptotic activity and inhibition of caspase-9 activity were abrogated by pertussis toxin, PD 98059, wortmannin, and LY 294002. LPA reduced cytochrome c release from mitochondria and prevented activation of caspase-9. LPA prevented translocation of Bax from cytosol to mitochondria and increased the expression of the antiapoptotic Bcl-2 mRNA and protein. LPA had no effect on Bcl-xl, Bad, and Bak mRNA or protein expression. These data indicate that LPA protects IEC-6 cells from camptothecin-induced apoptosis through G(i)-coupled inhibition of caspase-3 activation mediated by the attenuation of caspase-9 activation due to diminished cytochrome c release, involving upregulation of Bcl-2 protein expression and prevention of Bax translocation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoptosis / drug effects*
  • Camptothecin / pharmacology
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Caspase Inhibitors
  • Caspases / metabolism
  • Cell Line
  • Cytochrome c Group / metabolism
  • Epithelial Cells / cytology*
  • Epithelial Cells / drug effects*
  • Epithelial Cells / metabolism
  • Gene Expression Regulation / drug effects
  • Heterotrimeric GTP-Binding Proteins / metabolism
  • Intestines / cytology*
  • Lysophospholipids / pharmacology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Mitochondria / drug effects*
  • Mitochondria / metabolism
  • Protein Transport / drug effects
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Signal Transduction / drug effects
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein
  • bcl-Associated Death Protein
  • bcl-X Protein

Substances

  • Carrier Proteins
  • Caspase Inhibitors
  • Cytochrome c Group
  • Lysophospholipids
  • Membrane Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Messenger
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein
  • bcl-Associated Death Protein
  • bcl-X Protein
  • Caspases
  • Heterotrimeric GTP-Binding Proteins
  • Camptothecin