Concanavalin A receptors in the plasma membrane of rat liver cells: comparative electron microscopic studies on normal cells and on cells in vivo transformed by diethylnitrosamine

1975 ◽  
Vol 10 (3-4) ◽  
pp. 143-155
Author(s):  
J. Roth ◽  
G. Neupert ◽  
F. Bolck
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Concanavalin A ◽  
Electron Microscopic ◽  
Normal Cells ◽  
Rat Liver Cells ◽  
Microscopic Studies ◽  
Concanavalin A Receptors ◽  
Comparative Electron

scholarly journals Glucagon and p21 ras enhance the phosphorylation of the same 38-kilodalton membrane protein from rat liver cells.

1990 ◽  
Vol 10 (6) ◽  
pp. 2468-2474 ◽  
Author(s):  
A N Hegde ◽  
M R Das
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
G Proteins ◽  
Rat Liver ◽  
Guanine Nucleotide ◽  
Ras Proteins ◽  
P21 Ras ◽  
Rat Liver Cells ◽  
Stimulation Of

We had reported earlier the enhanced phosphorylation of a 38-kilodalton protein (p38) in rat liver plasma membrane by ras proteins. Now we show that glucagon increased the phosphorylation of the same protein. The nature and site(s) of phosphorylation were the same as those for the ras proteins. Both ATP and GTP could donate phosphate for the phosphorylation of p38. The stimulation of p38 phosphorylation by glucagon was guanine nucleotide dependent. This observation, together with our data on the stimulation of p38 phosphorylation by AIF4-, suggest the involvement of G proteins in the reaction. We also showed that glucagon stimulates the phosphorylation of p38 in vivo.

In vivo and electron microscopic studies of rat liver after intravenous injection of polyamino acid microspheres

1994 ◽  
Vol 28 (8) ◽  
pp. 881-890 ◽  
Author(s):  
C. Li ◽  
P. McCuskey ◽  
Z. Kan ◽  
D. J. Yang ◽  
K. C. Wright ◽  
...  
Keyword(s):  
Intravenous Injection ◽  
Rat Liver ◽  
Electron Microscopic ◽  
Polyamino Acid ◽  
Microscopic Studies

Glucagon and p21 ras enhance the phosphorylation of the same 38-kilodalton membrane protein from rat liver cells

1990 ◽  
Vol 10 (6) ◽  
pp. 2468-2474
Author(s):  
A N Hegde ◽  
M R Das
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
G Proteins ◽  
Rat Liver ◽  
Guanine Nucleotide ◽  
Ras Proteins ◽  
P21 Ras ◽  
Rat Liver Cells ◽  
Stimulation Of

We had reported earlier the enhanced phosphorylation of a 38-kilodalton protein (p38) in rat liver plasma membrane by ras proteins. Now we show that glucagon increased the phosphorylation of the same protein. The nature and site(s) of phosphorylation were the same as those for the ras proteins. Both ATP and GTP could donate phosphate for the phosphorylation of p38. The stimulation of p38 phosphorylation by glucagon was guanine nucleotide dependent. This observation, together with our data on the stimulation of p38 phosphorylation by AIF4-, suggest the involvement of G proteins in the reaction. We also showed that glucagon stimulates the phosphorylation of p38 in vivo.

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