A farnesyltransferase inhibitor attenuates cardiac myocyte hypertrophy and gene expression

J Mol Cell Cardiol. 2000 Jun;32(6):1127-40. doi: 10.1006/jmcc.2000.1150.

Abstract

The overexpression of either oncogenic ras or calmodulin in cardiac myocytes can elicit a hypertrophic response, albeit their recruitment by physiologically relevant stimuli remains unresolved. The present study utilized a pharmacological approach to examine the role of ras and calmodulin in norepinephrine- and endothelin-1-stimulated hypertrophy of neonatal rat cardiac myocytes. The pretreatment of cardiac myocytes with the farnesyltransferase inhibitor BMS-191563 (25 microM) increased the level of unfarnesylated ras in the cytosolic fraction, and caused a concomitant 42 +/- 2% decrease in immunodetectable farnesylated ras in the particulate fraction. In parallel, BMS-191563 pretreatment inhibited norepinephrine-mediated 3H-leucine uptake (80 +/- 10% decrease: n = 6; P<0.01), whereas a significant but less pronounced effect on the endothelin-1 response (46 +/- 6% decrease: n = 6; P<0.05) was observed. The calmodulin inhibitor W7 caused a 50 +/- 10% decrease (n = 8; P<0.05) of norepinephrine stimulated protein synthesis, whereas the endothelin-1 response was unaffected. Consistent with the recruitment of ras, BMS-191563 pretreatment attenuated norepinephrine and endothelin-1-stimulated extracellular signal-regulated kinase (ERK) activity. However, PD098059-mediated inhibition of MEK-dependent stimulation of ERK did not alter the hypertrophic response of either agonist. At the molecular level, the pretreatment with either BMS-191563 or W7 attenuated the norepinephrine-mediated increase of prepro-ANP and -BNP mRNA. Likewise, BMS-191563 caused a significant decrease of endothelin-1-mediated expression of the natriuretic peptide mRNAs, but to a lesser extent, as compared to norepinephrine. Thus, the present study has shown the treatment of neonatal rat cardiac myocytes with a farnesyltransferase inhibitor can attenuate the hypertrophic phenotype in response to physiologically relevant stimuli, thereby supporting a role of the small GTP-binding protein ras. Moreover, these data further suggest alternative ras-independent signaling pathways are also implicated in the hypertrophic response, albeit, there appears to exist a stimulus-specific heterogeneity in their recruitment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkyl and Aryl Transferases / antagonists & inhibitors*
  • Alkyl and Aryl Transferases / metabolism
  • Animals
  • Atrial Natriuretic Factor / genetics*
  • Calmodulin / pharmacology
  • Cardiomegaly / drug therapy
  • Cardiomegaly / enzymology*
  • Cells, Cultured
  • Endothelin-1 / pharmacology
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology*
  • Farnesyltranstransferase
  • Gene Expression / drug effects
  • Heart / drug effects*
  • Mitogen-Activated Protein Kinases / metabolism
  • Myocardium / cytology
  • Myocardium / enzymology*
  • Natriuretic Peptide, Brain
  • Nerve Tissue Proteins / genetics*
  • Norepinephrine / pharmacology
  • Protein Precursors / genetics*
  • RNA, Messenger
  • Rats
  • Rats, Sprague-Dawley
  • Sulfonamides / pharmacology
  • ras Proteins / physiology

Substances

  • Calmodulin
  • Endothelin-1
  • Enzyme Inhibitors
  • Nerve Tissue Proteins
  • Protein Precursors
  • RNA, Messenger
  • Sulfonamides
  • prepro-brain natriuretic peptide
  • Natriuretic Peptide, Brain
  • W 7
  • Atrial Natriuretic Factor
  • Alkyl and Aryl Transferases
  • Farnesyltranstransferase
  • Mitogen-Activated Protein Kinases
  • ras Proteins
  • Norepinephrine