scholarly journals Adhesion-Related Kinase Induction of Migration Requires Phosphatidylinositol-3-Kinase and Ras Stimulation of Rac Activity in Immortalized Gonadotropin-Releasing Hormone Neuronal Cells

Endocrinology ◽  
2007 ◽  
Vol 148 (6) ◽  
pp. 2806-2814 ◽  
Author(s):  
Sheila M. Nielsen-Preiss ◽  
Melissa P. Allen ◽  
Mei Xu ◽  
Daniel A. Linseman ◽  
John E. Pawlowski ◽  
...  
Keyword(s):  
Neuronal Cells ◽  
Gonadotropin Releasing Hormone ◽  
Phosphatidylinositol 3 Kinase ◽  
Releasing Hormone ◽  
Stimulation Of ◽  
Phosphatidylinositol 3

scholarly journals Insulin and Leptin Induce Glut4 Plasma Membrane Translocation and Glucose Uptake in a Human Neuronal Cell Line by a Phosphatidylinositol 3-Kinase- Dependent Mechanism

Endocrinology ◽  
2006 ◽  
Vol 147 (5) ◽  
pp. 2550-2556 ◽  
Author(s):  
Yacir Benomar ◽  
Nadia Naour ◽  
Alain Aubourg ◽  
Virginie Bailleux ◽  
Arieh Gertler ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Neuronal Cells ◽  
Neuronal Cell ◽  
Glut4 Translocation ◽  
Phosphatidylinositol 3 Kinase ◽  
Human Neuronal Cell ◽  
The Impact ◽  
Dependent Mechanism ◽  
Stimulation Of ◽  
Phosphatidylinositol 3

The insulin-sensitive glucose transporter Glut4 is expressed in brain areas that regulate energy homeostasis and body adiposity. In contrast with peripheral tissues, however, the impact of insulin on Glut4 plasma membrane (PM) translocation in neurons is not known. In this study, we examined the role of two anorexic hormones (leptin and insulin) on Glut4 translocation in a human neuronal cell line that express endogenous insulin and leptin receptors. We show that insulin and leptin both induce Glut4 translocation to the PM of neuronal cells and activate glucose uptake. Wortmannin, a specific inhibitor of phosphatidylinositol 3-kinase, totally abolished insulin- and leptin-dependent Glut4 translocation and stimulation of glucose uptake. Thus, Glut4 translocation is a phosphatidylinositol 3-kinase-dependent mechanism in neuronal cells. Next, we investigated the impact of chronic insulin and leptin treatments on Glut4 expression and translocation. Chronic exposure of neuronal cells to insulin or leptin down-regulates Glut4 proteins and mRNA levels and abolishes the acute stimulation of glucose uptake in response to acute insulin or leptin. In addition, chronic treatment with either insulin or leptin impaired Glut4 translocation. A cross-desensitization between insulin and leptin was apparent, where exposure to insulin affects leptin-dependent Glut4 translocation and vice versa. This cross-desensitization could be attributed to the increase in suppressor of cytokine signaling-3 expression, which was demonstrated in response to each hormone. These results provide evidence to suggest that Glut4 translocation to neuronal PM is regulated by both insulin and leptin signaling pathways. These pathways might contribute to an in vivo glucoregulatory reflex involving a neuronal network and to the anorectic effect of insulin and leptin.

Stimulation of tetrahydrobiopterin synthesis induced by insulin: possible involvement of phosphatidylinositol 3-kinase

2001 ◽  
Vol 33 (1) ◽  
pp. 65-73 ◽  
Author(s):  
Masakazu Ishii ◽  
Shunichi Shimizu ◽  
Tsutomu Nagai ◽  
Kazuhiro Shiota ◽  
Yuji Kiuchi ◽  
...  
Keyword(s):  
Phosphatidylinositol 3 Kinase ◽  
Stimulation Of ◽  
Phosphatidylinositol 3

Autocrine induction of c-fos expression in GT1 neuronal cells by gonadotropin-releasing hormone.

Endocrinology ◽  
1993 ◽  
Vol 133 (6) ◽  
pp. 3042-3045 ◽  
Author(s):  
M Cesnjaj ◽  
L Z Krsmanovic ◽  
K J Catt ◽  
S S Stojilkovic
Keyword(s):  
Neuronal Cells ◽  
Gonadotropin Releasing Hormone ◽  
Releasing Hormone ◽  
Fos Expression
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