Stimulation of microsomal cholesterol ester hydrolase by glucagon, cyclic AMP analogues, and vasopressin in isolated rat hepatocytes

Lipids ◽  
1996 ◽  
Vol 31 (3) ◽  
pp. 269-276
Author(s):  
María L. Hernández ◽  
María J. Martínez ◽  
José I. Ruiz ◽  
Begoño Ochoa
Keyword(s):  
Cyclic Amp ◽  
Cholesterol Ester ◽  
Rat Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Cholesterol Ester Hydrolase ◽  
Ester Hydrolase ◽  
Isolated Rat ◽  
Microsomal Cholesterol ◽  
Stimulation Of

Hormonal regulation of acid cholesterol ester hydrolase activity: effects of triiodothyronine and 17α-ethynylestradiol

1984 ◽  
Vol 62 (2) ◽  
pp. 244-247
Author(s):  
David L. Severson ◽  
L. Joseph Hayden ◽  
Thea Fletcher
Keyword(s):  
Hormonal Regulation ◽  
Cholesterol Ester ◽  
Rat Hepatocytes ◽  
Hydrolase Activity ◽  
Isolated Rat Hepatocytes ◽  
Cholesterol Ester Hydrolase ◽  
Ester Hydrolase ◽  
Parenchymal Cells ◽  
Selective Increase ◽  
Stimulation Of

Cholesterol ester hydrolase activity was measured in isolated rat hepatocytes and adipocytes. Administration of triiodothyronine to rats resulted in a specific and selective increase in lysosomal acid (pH 4.5) cholesterol ester hydrolase activity in hepatocytes. Since the majority of lipoprotein degradation occurs in liver parenchymal cells (hepatocytes), the stimulation of liver (hepatocyte) acid cholesterol ester hydrolase activity by triiodothyronine could contribute to the hypocholesterolemie action of thyroid hormones. Treatment of rats with 17α-ethynylestradiol to increase the hepatic degradation of lipoproteins did not change acid cholesterol ester hydrolase activity in liver, indicating that the thyroid hormone induced stimulation of acid cholesterol ester hydrolase activity in hepatocytes is not a secondary effect owing to the increased hepatic catabolism of low density lipoproteins (LDL). In contrast to the results with hepatocytes, hyperthyroidism did not increase acid cholesterol ester hydrolase activity in rat adipocytes.

scholarly journals Stimulatory effect of the intestinal peptide PHI on glycogenolysis and gluconeogenesis in isolated rat hepatocytes

1983 ◽  
Vol 214 (3) ◽  
pp. 999-1002 ◽  
Author(s):  
J E Felíu ◽  
J Marco
Keyword(s):  
Cyclic Amp ◽  
Pyruvate Kinase ◽  
Glycogen Phosphorylase ◽  
Rat Hepatocytes ◽  
Fold Increase ◽  
Isolated Rat Hepatocytes ◽  
Mediated Effects ◽  
Dose Dependent ◽  
Isolated Rat ◽  
Stimulation Of

The newly isolated peptide PHI provoked a dose-dependent stimulation of glycogenolysis and gluconeogenesis in isolated rat hepatocytes; at 1 microM-PHI, both processes were increased 1.6-fold as compared with basal values. These PHI-mediated effects were accompanied by the activation of glycogen phosphorylase and the inactivation of pyruvate kinase. PHI (1 microM) also caused a 2-fold increase in hepatocyte cyclic AMP.

scholarly journals Effects of phorbol esters on α1-adrenergic-mediated and glucagon-mediated actions in isolated rat hepatocytes

1985 ◽  
Vol 228 (1) ◽  
pp. 277-280 ◽  
Author(s):  
J A García-Sáinz ◽  
F Mendlovic ◽  
M A Martínez-Olmedo
Keyword(s):  
Cyclic Amp ◽  
Dose Response ◽  
Response Curve ◽  
Phorbol Esters ◽  
Rat Hepatocytes ◽  
Metabolic Effects ◽  
Isolated Rat Hepatocytes ◽  
The Right ◽  
Isolated Rat ◽  
Stimulation Of

Phorbol 12-myristate 13-acetate (PMA) inhibited the stimulation of ureogenesis produced by adrenaline, but produced a minimal displacement to the right of the dose-response curve for glucagon. However, PMA diminished the accumulation of cyclic AMP induced by glucagon. Dissociation between the cyclic AMP concentrations and the metabolic effects induced by glucagon is evidenced in the presence of phorbol esters.

Stimulation of bile acid synthesis by dibutyryl cyclic AMP in isolated rat hepatocytes

Lipids ◽  
1983 ◽  
Vol 18 (7) ◽  
pp. 443-447 ◽  
Author(s):  
G. S. Sundaram ◽  
Vicki Rothman ◽  
Simeon Margolis
Keyword(s):  
Bile Acid ◽  
Cyclic Amp ◽  
Rat Hepatocytes ◽  
Acid Synthesis ◽  
Bile Acid Synthesis ◽  
Dibutyryl Cyclic Amp ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat ◽  
Stimulation Of

Effects of polyamines on cyclic AMP-mediated stimulation of amino acid transport in isolated rat hepatocytes

1983 ◽  
Vol 117 (2) ◽  
pp. 204-210 ◽  
Author(s):  
Patrick Auberger ◽  
Michel Samson ◽  
Ginette Le Cam ◽  
Alphonse Le Cam
Keyword(s):  
Amino Acid ◽  
Cyclic Amp ◽  
Amino Acid Transport ◽  
Rat Hepatocytes ◽  
Acid Transport ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat ◽  
Stimulation Of

scholarly journals The mechanism by which adenosine decreases gluconeogenesis from lactate in isolated rat hepatocytes

1987 ◽  
Vol 246 (2) ◽  
pp. 449-454 ◽  
Author(s):  
A Lavoinne ◽  
H A Buc ◽  
S Claeyssens ◽  
M Pinosa ◽  
F Matray
Keyword(s):  
Ketone Body ◽  
Adenine Nucleotides ◽  
Rat Hepatocytes ◽  
Adenosine Kinase ◽  
Isolated Rat Hepatocytes ◽  
Adenosine Deaminase 2 ◽  
Body Production ◽  
Gluconeogenic Substrates ◽  
Isolated Rat ◽  
Stimulation Of

Incubation of hepatocytes from 24 h-starved rats in the presence of 0.5 mM-adenosine decreased gluconeogenesis from lactate, but not from alanine. The inhibition of gluconeogenesis was associated with a stimulation of ketone-body production and an inhibition of pyruvate oxidation. These metabolic changes were suppressed in the presence of iodotubercidin (an inhibitor of adenosine kinase), but were reinforced in the presence of deoxycoformycin (an inhibitor of adenosine deaminase); 2-chloroadenosine induced no change in gluconeogenesis from lactate. These data indicate that the inhibition of gluconeogenesis by adenosine probably results from its conversion into adenine nucleotides. In the presence of lactate or pyruvate, but not with alanine or asparagine, this conversion resulted in a decrease in the [ATP]/[ADP] ratio in both mitochondrial and cytosolic compartments. Adenosine decreased the Pi concentration with all gluconeogenic substrates.

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