Distribution of NADH pyrophosphatase between plasma membrane and intracellular membranes in rat hepatoma cells

1983 ◽  
Vol 11 (6) ◽  
pp. 784-785
Author(s):  
RICHARD J. PEASE ◽  
NEIL D. COOK ◽  
GEOFFERY D. SMITH ◽  
TIMOTHY J. PETERS
Keyword(s):  
Plasma Membrane ◽  
Hepatoma Cells ◽  
Intracellular Membranes ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

scholarly journals Isolation of plasma-membrane-associated tumour-specific antigen from rat hepatoma cells

1972 ◽  
Vol 128 (4) ◽  
pp. 130P-131P ◽  
Author(s):  
R W Baldwin ◽  
J R Harris ◽  
M R Price
Keyword(s):  
Plasma Membrane ◽  
Specific Antigen ◽  
Hepatoma Cells ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

scholarly journals Preferential degradation of the terminal carbohydrate moiety of membrane glycoproteins in rat hepatoma cells and after transfer to the membranes of mouse fibroblasts.

1983 ◽  
Vol 96 (1) ◽  
pp. 139-150 ◽  
Author(s):  
H Baumann ◽  
E Hou ◽  
G P Jahreis
Keyword(s):  
Plasma Membrane ◽  
Protein Fraction ◽  
Hepatoma Cells ◽  
Total Cell ◽  
Cell Protein ◽  
Two Dimensional ◽  
Membrane Glycoproteins ◽  
Membrane Components ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

Glycoproteins in the plasma membrane of rat hepatoma cells were labeled at their externally exposed tyrosine residues with 131I and at their galactose and sialic acid residues with 3H. The degradation of both isotopes in the total cell protein fraction, in glycoproteins purified by concanavalin A, and in glycoproteins separated on two-dimensional gels was determined. Similarly, the total cellular membrane glycoproteins were metabolically labeled with [35S]methionine and [3H]fucose. The fate of both incorporated labels was followed by lectin chromatography or by precipitation of the proteins with specific antibodies followed by electrophoretic gel separation. In both labeling experiments, the carbohydrate markers were lost from the ligand-recognized fraction with similar kinetics as from the total cell protein fraction. In some glycoprotein species which were separated by two-dimensional gel electrophoresis, the polypeptide portion exhibited up to a twofold slower rate of degradation relative to that of the carbohydrate moiety. This difference is most pronounced in carbohydrate-rich glycoproteins. To corroborate this finding, double-labeled membrane glycoproteins were incorporated into reconstituted phospholipid vesicles which were then transferred via fusion into the plasma membrane of mouse fibroblasts. Both the polypeptide and carbohydrate moieties of the transferred membrane glycoproteins were degraded with the same relative kinetics as in the original hepatoma cells. The rate of degradation is mostly a function of the structural properties of the membrane components as shown by the preservation of metabolically stable fucogangliosides of Reuber H-35 hepatoma cells transferred onto the fibroblasts. The technique of insertion of membrane components into the plasma membrane of another cell should assist in the elucidation of the exact route and mechanism of membrane protein destruction.

scholarly journals Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells.

1988 ◽  
Vol 263 (1) ◽  
pp. 350-359 ◽  
Author(s):  
H E Tornqvist ◽  
J R Gunsalus ◽  
R A Nemenoff ◽  
A R Frackelton ◽  
M W Pierce ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Hepatoma Cells ◽  
Tyrosine Residues ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells
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