Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase

J Biol Chem. 1998 Sep 11;273(37):24266-71. doi: 10.1074/jbc.273.37.24266.

Abstract

The mechanism by which 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase inhibitors increase endothelial nitric oxide synthase (eNOS) expression is unknown. To determine whether changes in isoprenoid synthesis affects eNOS expression, human endothelial cells were treated with the HMG-CoA reductase inhibitor, mevastatin (1-10 microM), in the presence of L-mevalonate (200 microM), geranylgeranylpyrophosphate (GGPP, 1-10 microM), farnesylpyrophosphate (FPP, 5-10 microM), or low density lipoprotein (LDL, 1 mg/ml). Mevastatin increased eNOS mRNA and protein levels by 305 +/- 15% and 180 +/- 11%, respectively. Co-treatment with L-mevalonate or GGPP, but not FPP or LDL, reversed mevastatin's effects. Because Rho GTPases undergo geranylgeranyl modification, we investigated whether Rho regulates eNOS expression. Immunoblot analyses and [35S]GTPgammaS-binding assays revealed that mevastatin inhibited Rho membrane translocation and GTP binding activity by 60 +/- 5% and 78 +/- 6%, both of which were reversed by co-treatment with GGPP but not FPP. Furthermore, inhibition of Rho by Clostridium botulinum C3 transferase (50 microg/ml) or by overexpression of a dominant-negative N19RhoA mutant increased eNOS expression. In contrast, activation of Rho by Escherichia coli cytotoxic necrotizing factor-1 (200 ng/ml) decreased eNOS expression. These findings indicate that Rho negatively regulates eNOS expression and that HMG-CoA reductase inhibitors up-regulate eNOS expression by blocking Rho geranylgeranylation, which is necessary for its membrane-associated activity.

Publication types

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

MeSH terms

  • ADP Ribose Transferases / metabolism
  • ADP Ribose Transferases / pharmacology
  • Bacterial Toxins / pharmacology
  • Botulinum Toxins*
  • Cells, Cultured
  • Cytosol / metabolism
  • Cytotoxins / pharmacology
  • Endothelium, Vascular / enzymology*
  • Escherichia coli Proteins*
  • GTP Phosphohydrolases / genetics
  • GTP Phosphohydrolases / metabolism*
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism
  • Gene Expression Regulation, Enzymologic / drug effects
  • Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
  • Guanosine Triphosphate / metabolism
  • Humans
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors / pharmacology
  • Kinetics
  • Lipoproteins, LDL / pharmacology
  • Lipoproteins, LDL / physiology
  • Lovastatin / analogs & derivatives
  • Lovastatin / pharmacology
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Mevalonic Acid / pharmacology
  • Nitric Oxide Synthase / genetics*
  • Nitric Oxide Synthase Type III
  • Polyisoprenyl Phosphates / pharmacology
  • RNA Processing, Post-Transcriptional* / drug effects
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • Sesquiterpenes
  • ras Proteins / metabolism
  • rhoA GTP-Binding Protein
  • rhoB GTP-Binding Protein

Substances

  • Bacterial Toxins
  • Cytotoxins
  • Escherichia coli Proteins
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors
  • Lipoproteins, LDL
  • Membrane Proteins
  • Polyisoprenyl Phosphates
  • RNA, Messenger
  • Sesquiterpenes
  • cytotoxic necrotizing factor type 1
  • mevastatin
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • farnesyl pyrophosphate
  • Guanosine Triphosphate
  • Lovastatin
  • NOS3 protein, human
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type III
  • ADP Ribose Transferases
  • exoenzyme C3, Clostridium botulinum
  • Botulinum Toxins
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • ras Proteins
  • rhoA GTP-Binding Protein
  • rhoB GTP-Binding Protein
  • geranylgeranyl pyrophosphate
  • Mevalonic Acid