Monomeric G-protein, Rhes, is not an imidazoline-regulated protein in pancreatic β-cells

Vladimir V. Sharoyko, Irina I. Zaitseva, Mark Varsanyi, Neil Portwood, Barbara Leibiger, Ingo Leibiger, Per Olof Berggren, Suad Efendić, Sergei V. Zaitsev

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


The monomeric G-protein, Rhes, is a candidate imidazoline-regulated molecule involved in mediating the insulin secretory response to efaroxan [S.L. Chan, L.K. Monks, H. Gao, P. Deaville, N.G. Morgan, Identification of the monomeric G-protein, Rhes, as an efaroxan-regulated protein in the pancreatic beta-cell, Br. J. Pharmacol. 136 (1) (2002) 31-36]. This suggestion was based on observations regarding changes in Rhes mRNA expression in rat islets and pancreatic β-cells after prolonged culture with efaroxan, leading to desensitization of the insulin response to the compound. To verify this report, we have evaluated the effects of the imidazoline compounds efaroxan and BL11282 on Rhes mRNA expression in isolated rat pancreatic islets maintained in conditions identical to those used by Chan et al. The results demonstrate that desensitization of the insulin response to efaroxan, or to another imidazoline, BL11282, does not change Rhes mRNA expression levels. Transfection of MIN6 cells with plasmids containing Rhes or Rhes-antisense also does not alter efaroxan- or BL11282-induced insulin secretion. Together, these data do not support the hypothesis that Rhes is an imidazoline-regulated protein.

Original languageEnglish (US)
Pages (from-to)1455-1459
Number of pages5
JournalBiochemical and biophysical research communications
Issue number3
StatePublished - Dec 23 2005


  • BL11282
  • Desensitization
  • Efaroxan
  • Imidazolines
  • Insulin secretion
  • MIN6 cells
  • Pancreatic islets

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


Dive into the research topics of 'Monomeric G-protein, Rhes, is not an imidazoline-regulated protein in pancreatic β-cells'. Together they form a unique fingerprint.

Cite this