Monomeric G-protein, Rhes, is not an imidazoline-regulated protein in pancreatic β-cells. / Sharoyko, Vladimir V.; Zaitseva, Irina I.; Varsanyi, Mark; Portwood, Neil; Leibiger, Barbara; Leibiger, Ingo; Berggren, Per Olof; Efendić, Suad; Zaitsev, Sergei V.
In: Biochemical and Biophysical Research Communications, Vol. 338, No. 3, 23.12.2005, p. 1455-1459.Research output: Contribution to journal › Article › peer-review
}
TY - JOUR
T1 - Monomeric G-protein, Rhes, is not an imidazoline-regulated protein in pancreatic β-cells
AU - Sharoyko, Vladimir V.
AU - Zaitseva, Irina I.
AU - Varsanyi, Mark
AU - Portwood, Neil
AU - Leibiger, Barbara
AU - Leibiger, Ingo
AU - Berggren, Per Olof
AU - Efendić, Suad
AU - Zaitsev, Sergei V.
PY - 2005/12/23
Y1 - 2005/12/23
N2 - 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.
AB - 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.
KW - BL11282
KW - Desensitization
KW - Efaroxan
KW - Imidazolines
KW - Insulin secretion
KW - MIN6 cells
KW - Pancreatic islets
UR - http://www.scopus.com/inward/record.url?scp=27744471356&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2005.10.145
DO - 10.1016/j.bbrc.2005.10.145
M3 - Article
C2 - 16277977
AN - SCOPUS:27744471356
VL - 338
SP - 1455
EP - 1459
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -
ID: 43834363