Inability of thiamine phosphates transport in isolated rat hepatocyte

1983 ◽  
Vol 39 (5) ◽  
pp. 505-507 ◽  
Author(s):  
K. Yoshioka ◽  
H. Nishimura ◽  
K. Sempuku ◽  
A. Iwashima
Keyword(s):  
Rat Hepatocyte ◽  
Thiamine Phosphates ◽  
Isolated Rat

scholarly journals Characteristics of system ASC for transport of neutral amino acids in the isolated rat hepatocyte.

1981 ◽  
Vol 256 (7) ◽  
pp. 3304-3312
Author(s):  
M.S. Kilberg ◽  
M.E. Handlogten ◽  
H.N. Christensen
Keyword(s):  
Amino Acids ◽  
Rat Hepatocyte ◽  
Neutral Amino Acids ◽  
Isolated Rat

A characterization of heam uptake and intracellular distribution by isolated hepatocytes

1985 ◽  
Vol 5 (7) ◽  
pp. 609-614 ◽  
Author(s):  
A. Lodola
Keyword(s):  
Endoplasmic Reticulum ◽  
Specific Binding ◽  
Isolated Hepatocytes ◽  
Intracellular Distribution ◽  
Distribution Data ◽  
Temperature Dependent ◽  
Rat Hepatocyte ◽  
Isolated Rat ◽  
Endoplasmic Reticulum Fraction

The uptake and intracellular distribution of haem by isolated rat hepatocyte suspensions was studied. An increase in cell haem content occurred after a challenge with 5, 10 or 20 μM haem, supplied as methaemalbumin. The rate of haem uptake was temperature dependent; no non-specific binding occurred. Intracellular haem distribution data are consistent with a rapid association of haem with the endoplasmic reticulum fraction prior to its accumulation in the cytosol and at the mitochondrion.

Presence of functional cytochrome P-450 on isolated rat hepatocyte plasma membrane

Hepatology ◽  
1990 ◽  
Vol 11 (5) ◽  
pp. 850-858 ◽  
Author(s):  
Jacqueline Loeper ◽  
Veronique Descatoire ◽  
Michelle Maurice ◽  
Philippe Beaune ◽  
Gerard Feldmann ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Rat Hepatocyte ◽  
Cytochrome P 450 ◽  
Isolated Rat

Conformational change in plasma albumin due to interaction with isolated rat hepatocyte

1988 ◽  
Vol 254 (4) ◽  
pp. G465-G470 ◽  
Author(s):  
T. Horie ◽  
T. Mizuma ◽  
S. Kasai ◽  
S. Awazu
Keyword(s):  
Conformational Change ◽  
Organic Anion ◽  
Resonance Spectroscopy ◽  
Hepatic Transport ◽  
Rat Hepatocyte ◽  
Plasma Albumin ◽  
Spin Resonance ◽  
Albumin Molecule ◽  
Hepatocyte Suspension ◽  
Isolated Rat

The electron spin resonance spectroscopy of 4-isothiocyanato-tempo labeled to bovine serum albumin (BSA) and the absorption spectroscopy of eosin maleimide labeled to BSA in the isolated rat hepatocyte suspension indicate conformational change occurring in the albumin molecule during interaction with the hepatocellular membrane. The conformational change in the albumin molecule may possibly accelerate the dissociation of albumin-organic anion complexes at the surface of the liver cell. The conformational change in the albumin molecule may explain in part the mechanism of albumin-mediated hepatic transport.

Insulin induces Ca2+ influx into isolated rat hepatocyte couplets

1997 ◽  
Vol 272 (6) ◽  
pp. G1425-G1432 ◽  
Author(s):  
K. Benzeroual ◽  
G. van de Werve ◽  
S. Meloche ◽  
L. Mathe ◽  
A. Romanelli ◽  
...  
Keyword(s):  
Peptide Hormone ◽  
Insulin Binding ◽  
Mitogen Activated Protein Kinase ◽  
Rat Hepatocyte ◽  
Mapk Activity ◽  
Mitogen Activated Protein ◽  
Insulin Dependent ◽  
Dose Dependent Increase ◽  
Isolated Rat ◽  
Stimulation Of

Isolated rat hepatocyte couplets were used to study the direct effect of insulin on intracellular Ca2+ homeostasis. Insulin induced a dose-dependent increase in hepatocellular Ca2+ that was gradual, generally monophasic, and reversible. Chelation of extracellular Ca2+ abolished the insulin-induced Ca2+ response, and this suppression was not related to an effect on insulin binding, as indicated by displacement studies. We thus tested the effect of several Ca2+ channel inhibitors on insulin-induced Ca2+ influx. Verapamil at 20 or 200 microM was without effect, whereas 500 microM nickel and 50 microM gadolinium strongly inhibited insulin-induced Ca2+ entry. Finally, we tested whether insulin-induced Ca2+ movements were implicated in the stimulation of mitogen-activated protein kinase (MAPK) activity, which we measured with the use of an immune-complex assay. Verapamil was without effect on the insulin-dependent stimulation of p44mapk activity, whereas addition of ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid, nickel, or gadolinium strongly inhibited the effect of the peptide hormone. Our results indicate that insulin triggers Ca2+ influx into hepatocytes, possibly through the opening of channels on the plasma membrane, and that this effect is important for insulin activation of MAPK.

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