Behavioral sensitization to binge-pattern cocaine administration is not associated with changes in protein levels of four major G-proteins

2005 ◽  
Vol 133 (2) ◽  
pp. 224-232 ◽  
Author(s):  
Shane A. Perrine ◽  
Joseph A. Schroeder ◽  
Ellen M. Unterwald
1999 ◽  
Vol 5 (S2) ◽  
pp. 1232-1233
Author(s):  
L. B. Kozell ◽  
C. K. Meshul

Repeated intermittent administration of cocaine to rodents has been shown to result in behavioral sensitization, or enhanced locomotor activity. Because there are similarities between effects of intermittent cocaine use in humans and sensitization in rats, understanding the neural mechanism underlying sensitization may provide insights into mechanisms of psychopathologies in humans.There is abundant evidence that the mesolimbic dopaminergic pathways, originating in the ventral tegmental area (VTA) and terminating in both nucleus accumbens (NAc) and prefrontal cortex (PFC), are critically important for development of sensitization to the motor-stimulating effects of cocaine. Evidence also suggests that changes in glutamate (Glu) transmission in the mesolimbic DA pathways are associated with sensitization to cocaine. In recent collaborative studies, we have shown that cocaine administration transiently decreases the density of nerve terminal glutamate immunolabeling within the NAc shell following withdrawal from continuous or intermittent cocaine administration. Locomotor activity was not assessed in either of these studies.


1999 ◽  
Vol 64 (3) ◽  
pp. 605-610 ◽  
Author(s):  
Rosemarie M Booze ◽  
Marcie L Wood ◽  
Marian A Welch ◽  
Stepheny Berry ◽  
Charles F Mactutus

1994 ◽  
Vol 167 (1-2) ◽  
pp. 121-124 ◽  
Author(s):  
Richard A. Orona ◽  
R.Dayne Mayfield ◽  
Elizabeth J. Cline ◽  
Nancy R. Zahniser

1992 ◽  
Vol 282 (1) ◽  
pp. 15-23 ◽  
Author(s):  
N McFarlane-Anderson ◽  
J Bailly ◽  
N Bégin-Heick

G-protein levels were assessed in liver and brain membranes of lean and obese mice. ADP-ribosylation and immunodetection studies revealed a decrease in the abundance of Gs and Gi alpha-subunits in the liver membranes of obese mice compared with lean mice. In contrast, in brain membranes, the abundance of these proteins was not significantly different between lean and obese mice. Studies at the mRNA level in both liver and brain revealed no difference in gene expression between lean and obese mice. Protein and mRNA studies both showed that Gs, Gi alpha 1, Gi alpha 2, Go alpha and G beta subunits are present in brain membranes, and Gi alpha 3 is barely detectable. In liver, Ga alpha, Gi alpha 2 and G beta subunits are the major constituents, whereas Gi alpha 1, Gi alpha 3 and Go alpha are barely detectable. It is possible that the differences observed at the protein level are due to different rates of translation of the mRNA. Different rates of release of the alpha-subunits from the membrane and/or different rates of degradation would also explain these results.


1991 ◽  
Vol 545 (1-2) ◽  
pp. 287-291 ◽  
Author(s):  
Jeffery D. Steketee ◽  
Caryn D. Striplin ◽  
Thomas F. Murray ◽  
Peter W. Kalivas

2009 ◽  
Vol 296 (4) ◽  
pp. G948-G954 ◽  
Author(s):  
Ping Cong ◽  
Victor Pricolo ◽  
Piero Biancani ◽  
Jose Behar

Gallbladder disease is prevalent during pregnancy. It has been suggested that this complication of pregnancy is attributable to increased bile cholesterol (Ch) induced by estrogens and to gallbladder hypomotility caused by increasing levels of progesterone (P4). Studies on nonpregnant gallbladders have shown that increased levels of bile Ch contribute to both gallstone formation and bile stasis. These studies investigated the effects of high levels of plasma membrane Ch on P4 on gallbladder muscle cells from human and guinea pigs. Contraction was studied in intact and permeabilized muscle cells. G proteins were determined by Western blot, and 3H-P4 incorporation by muscle cells was measured in the β-scintillation counter. High levels of caveolar Ch blocked the effects induced by P4 treatment for 6 h. They suppressed the expected P4 inhibition of GTP-γS (a G protein activator)-induced contraction and changes in G proteins by downregulating Gi3 and upregulating Gs protein levels. Ch inhibited these P4 actions at the caveolar 3 (CAV-3) level, since the P4 effects were antagonized by treatment with CAV-3 antibody, by reducing CAV-3 expression through CAV-3 siRNA. CAV-3 antibody and siRNA reduced caveolar Ch levels. High caveolar levels of Ch and CAV-3 antibody blocked the incorporation of 3H-P4 into caveolae. Treatment with GDP-βS (a G protein antagonist) had no effect on P4 actions. High caveolar Ch levels blocked the P4 effects on muscle contraction and G protein changes probably because both Ch and P4 require CAV-3 proteins for their transport across the plasma membrane.


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