Transformation with SV40 virus prevents retinoic acid inhibition of plasma membrane NADH diferric transferrin reductase in rat liver cells

1988 ◽  
Vol 20 (3) ◽  
pp. 383-391 ◽  
Author(s):  
I. L. Sun ◽  
W. Toole-Simms ◽  
F. L. Crane ◽  
D. J. Morr� ◽  
H. L�w ◽  
...  
1981 ◽  
Vol 198 (3) ◽  
pp. 457-466 ◽  
Author(s):  
Govind S. Rao ◽  
Marie Luise Rao ◽  
Astrid Thilmann ◽  
Hans D. Quednau

1. Influx and efflux of l-tri-[125I]iodothyronine with isolated rat liver parenchymal cells and their plasma-membrane vesicles were studied by a rapid centrifugation technique. 2. At 23°C and in the concentration range that included the concentration of free l-tri-iodothyronine in rat plasma (3–5pm) influx into cells was saturable; an apparent Kt value of 8.6±1.6pm was obtained. 3. At 5pm-l-tri-[125I]iodothyronine in the external medium the ratios of the concentrations inside to outside in cells and plasma-membrane vesicles were 38:1 and 366:1 respectively after 7s of incubation. At equilibrium (60s at 23°C) uptake of l-tri-[125I]iodothyronine by cells was linear with the hormone concentration, whereas that by plasma-membrane vesicles exhibited an apparent saturation with a Kd value of 6.1±1.3pm. 4. Efflux of l-tri-[125I]iodothyronine from cells equilibrated with the hormone (5–123pm) was constant up to 21 s; the amount that flowed out was 17.7±3.8% when cells were equilibrated with 5pm-hormone. When plasma-membrane vesicles were equilibrated with l-tri-[125I]iodothyronine (556–1226pm) 66.8±5.8% flowed out after 21 s. 5. From a consideration of the data on efflux from cells and binding of l-tri-[125I]iodothyronine to the liver homogenate, as studied by the charcoal-adsorption and equilibrium-dialysis methods, it appears that 18–22% of the hormone exists in the free form in the cell. 6. Vinblastine and colchicine diminished the uptake of l-tri-[125I]iodothyronine by cells but not by plasma-membrane vesicles; binding to the cytosol fraction was not affected. Phenylbutazone, 6-n-propyl-2-thiouracil, methimazole and corticosterone diminished the uptake by cells, plasma-membrane vesicles and binding to the cytosol fraction to different extents. 7. These results suggest that at low concentrations of l-tri-[125I]iodothyronine rat liver cells and their plasma-membrane vesicles accumulated the hormone against an apparent gradient by a membrane-mediated process. Contribution of cytoplasmic proteins to uptake by plasma-membrane vesicles was negligible. The amount of l-tri-[125I]iodothyronine required to achieve half-maximal uptake agrees with that occurring in the free form in the blood, conferring physiological importance to the transporting system in the plasma membrane of the liver cell.


1984 ◽  
Vol 22 (1) ◽  
pp. 31-39 ◽  
Author(s):  
C. Lafarge-Frayssinet ◽  
S. Estrade ◽  
B. Rosa-Loridon ◽  
C. Frayssinet ◽  
R. Cassingena

1982 ◽  
Vol 92 (3) ◽  
pp. 865-870 ◽  
Author(s):  
H J Geuze ◽  
J W Slot ◽  
G J Strous ◽  
H F Lodish ◽  
A L Schwartz

We used high-resolution immunocytochemistry on ultrathin frozen sections labeled with colloidal gold to study the subcellular distribution of the asialoglycoprotein receptor in rat liver. The receptor was localized along the entire hepatocyte plasma membrane, including the bile capillary membrane, but was scarce intracellularly. Sinusoidal lining (Kupffer) cells and blood cells showed no immunoreactivity. In liver cells of rats injected with 1 to 100 micrograms of asialoorosomucoid (ASOR) 2-15 min before tissue fixation, endocytotic internalization of receptors at the blood front was conspicuous. At all times in this interval, receptor was present in approximately 100-nm vesicles and larger vacuoles adjacent to the sinusoidal plasma membrane. No other significant intracellular receptor was noted during the 15-min exposure to ASOR; in particular, lysosomes and Golgi complex were not labeled. Our observations, in combination with data from the literature which demonstrate that, under these conditions, the ligand is transferred further to the Golgi complex-lysosome region, suggest that the receptor and ligand are dissociated in the vicinity of the plasma membrane, after which the receptor rapidly returns to the cell surface.


Science ◽  
1972 ◽  
Vol 176 (4031) ◽  
pp. 175-177 ◽  
Author(s):  
L. Shlatz ◽  
G. V. Marinetti

1990 ◽  
Vol 173 (3) ◽  
pp. 1287-1291 ◽  
Author(s):  
Cristina Pujades ◽  
Ricardo Bastos ◽  
Carlos Enrich ◽  
Oriol Bachs

1972 ◽  
Vol 247 (9) ◽  
pp. 2742-2746
Author(s):  
Cara-Lynne Schengrund ◽  
Doris S. Jensen ◽  
Abraham Rosenberg

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