Effect of Bilateral Nephrectomy on Urea Formation in Rat Liver Slices

1957 ◽  
Vol 191 (2) ◽  
pp. 345-349 ◽  
Author(s):  
Alvin L. Sellers ◽  
Joseph Katz ◽  
Jessie Marmorston
Keyword(s):  
Rat Liver ◽  
Liver Protein ◽  
Urea Synthesis ◽  
Bilateral Nephrectomy ◽  
Liver Slices ◽  
Isolated Liver ◽  
Intact Rats

The rate of urea synthesis by isolated liver slices has been determined. The rate of urea synthesis is approximately 50% greater in liver slices from nephrectomized rats than in those from nonuremic controls. Liver slices from intact rats maintained on a diet of 15% glucose formed only 23–50% as much urea as slices from fasted controls. The results indicate that the increased urea synthesis in liver slices from nephrectomized rats is largely due to an increase in the catabolism of liver protein resulting in an increase in urea precursors.

Insulin stimulus of leucine incorporation into frog liver protein

1962 ◽  
Vol 203 (4) ◽  
pp. 687-689 ◽  
Author(s):  
J. C. Penhos ◽  
M. E. Krahl
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Leucine Incorporation ◽  
Liver Protein ◽  
Amino Acid Incorporation ◽  
Insulin Effect ◽  
Acid Incorporation ◽  
Liver Slices ◽  
Stimulation Of

Slices prepared from livers of bull frogs ( Rana catesbiana), pancreatectomized and/or hypophysectomized 7 days before, were incubated 2 hr in frog Ringer-bicarbonate solution at 25 C. Incorporation of leucine-1-C14 into protein was subnormal in the pancreatectomized series. The addition of insulin in vitro, with glucose also present in the medium, produced a significant ( P < 0.01) stimulation of amino acid incorporation in the following series: livers from normal fed animals; livers from animals pancreatectomized 7 days before; and livers from animals pancreatectomized and hypophysectomized 7 days before. Neither insulin nor glucose alone gave a significant effect. These results therefore confirm and extend those obtained with rat liver slices showing that insulin can stimulate amino acid incorporation into protein when added directly to liver. The effect is relatively greatest with livers from animals pancreatectomized 7 days before; the insulin effect does not depend on the presence of the pituitary, as it is obtainable with livers from animals hypophysectomized and pancreatectomized 7 days previously.

scholarly journals Polyribosomes in isolated liver cells. Preparative procedures, effects of incubation and correlation with protein synthesis

1980 ◽  
Vol 186 (1) ◽  
pp. 35-45 ◽  
Author(s):  
A J Dickson ◽  
C I Pogson
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Isolated Hepatocytes ◽  
Liver Cells ◽  
Liver Protein ◽  
Isolated Cells ◽  
Isolated Liver Cells ◽  
Rat Liver Cells ◽  
Isolated Liver

Methods have been derived which permit the isolation of undergraded polyribosomes from isolated rat liver cells. Under the conditions used the polyribosome profile of hepatocytes immediately after isolation was essentially identical with that from intact liver. However, during incubation of cells in complex physiological media there was a progressive dissociation of polyribosomes. The addition of a variety of factors that produce reaggregation of polyribosomes in rat liver in vivo did not prevent dissociation during cell incubations. Although large polyribosomes were lost most rapidly, the albumin-synthesizing capacity of isolated cells was not selectively lost when compared with total protein synthesis. The significance of these results for the use of isolated hepatocytes in the study of liver protein synthesis is discussed.

scholarly journals Further observations on the activation of lysosomal acid α-glucosidase by cortisone derivatives

1973 ◽  
Vol 132 (3) ◽  
pp. 435-438 ◽  
Author(s):  
E. J. Bourne ◽  
K. Clarke ◽  
J. B. Pridham ◽  
J. J. M. Rowe
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Lysosomal Membrane ◽  
Cortisone Acetate ◽  
Lysosomal Acid ◽  
Liver Slices ◽  
Liver Lysosomes ◽  
Membrane Bound ◽  
Isolated Liver

1. Cortisone acetate activates the acid α-glucosidase in rat liver slices and in isolated liver lysosomes. 2. The reaction is steroid specific and moreover does not occur with lysosomal acid phosphatase or β-galactosidase. 3. After pretreatment of the lysosomes with cortisone, substrate (maltose) binding to the soluble lysosomal acid α-glucosidase is not affected, but the steroid does increase the Vmax. value. Membrane-bound enzyme is not activated by cortisone. 4. 4-[14C]Cortisone is preferentially bound to the lysosomal membrane and the possible involvement of this structure in the activation phenomenon is discussed.

THE INFLUENCE OF ADRENALECTOMY AND INDIVIDUAL STEROID HORMONES UPON THE METABOLISM OF ACETATE-1-C14 BY RAT LIVER SLICES: I. INCORPORATION INTO PROTEINS

1960 ◽  
Vol 38 (1) ◽  
pp. 1387-1392 ◽  
Author(s):  
J. S. Willmer ◽  
T. S. Foster
Keyword(s):  
Adrenal Gland ◽  
Steroid Hormones ◽  
Rat Liver ◽  
Liver Protein ◽  
Liver Slices ◽  
Isotope Incorporation

The influence of the adrenal gland on incorporation of acetate-1-C14 into rat liver protein was studied. Cortisone, corticosterone, and deoxycorticosterone were found to increase isotope incorporation in both sham-operated and adrenalectomized groups, while Reichstefn's substance S increased radioactivity in the protein only from sham-operated animals. The effects of the alcohol and acetate forms of cortisone, hydrocortisone, deoxycorticosterone, and Reichstein's substance S were compared.

THE INFLUENCE OF ADRENALECTOMY AND INDIVIDUAL STEROID HORMONES UPON THE METABOLISM OF ACETATE-1-C14 BY RAT LIVER SLICES: I. INCORPORATION INTO PROTEINS

1960 ◽  
Vol 38 (12) ◽  
pp. 1387-1392 ◽  
Author(s):  
J. S. Willmer ◽  
T. S. Foster
Keyword(s):  
Adrenal Gland ◽  
Steroid Hormones ◽  
Rat Liver ◽  
Liver Protein ◽  
Liver Slices ◽  
Isotope Incorporation

The influence of the adrenal gland on incorporation of acetate-1-C14 into rat liver protein was studied. Cortisone, corticosterone, and deoxycorticosterone were found to increase isotope incorporation in both sham-operated and adrenalectomized groups, while Reichstefn's substance S increased radioactivity in the protein only from sham-operated animals. The effects of the alcohol and acetate forms of cortisone, hydrocortisone, deoxycorticosterone, and Reichstein's substance S were compared.

Control of Urea Synthesis in Fetal Rat Liver Slices

Neonatology ◽  
1981 ◽  
Vol 40 (5-6) ◽  
pp. 224-231 ◽  
Author(s):  
A. Husson ◽  
A. Fairand ◽  
R. Vaillant
Keyword(s):  
Rat Liver ◽  
Urea Synthesis ◽  
Liver Slices ◽  
Fetal Rat ◽  
Fetal Rat Liver

Insulin stimulus of leucine incorporation in rat liver protein

1962 ◽  
Vol 202 (2) ◽  
pp. 349-352 ◽  
Author(s):  
J. C. Penhos ◽  
M. E. Krahl
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Leucine Incorporation ◽  
Liver Protein ◽  
Amino Acid Incorporation ◽  
Experimental Conditions ◽  
Maximum Percentage ◽  
Acid Incorporation ◽  
Liver Slices

Slices were prepared from livers of partially pancreatectomized rats and incubated 2 hr in Krebs bicarbonate solution at 37 C. Incorporation of leucine-1-C14 into protein decreased progressively as severity of diabetes increased during 1–6 months after operation; at 2–4 months insulin (0.01 U/ml of medium) plus glucose (200 mg/100 ml) added in vitro stimulated incorporation 62–78%; stimulation was not significant at 6 months. Neither insulin nor glucose was effective separately. Alkali-inactivated insulin was ineffective, even with glucose. Liver slices from sham-operated rats responded similarly to insulin under the present experimental conditions, although the maximum percentage stimulation was smaller than in the partially pancreatectomized series. It is concluded that insulin can act directly on the liver to stimulate amino acid incorporation in protein by a mechanism dependent on the presence of glucose.

Effect of pyruvate and other substrates on urea synthesis in rat liver slices

Metabolism ◽  
1968 ◽  
Vol 17 (2) ◽  
pp. 158-167 ◽  
Author(s):  
Robert Metz ◽  
James M. Salter ◽  
Gunther Brunet
Keyword(s):  
Rat Liver ◽  
Urea Synthesis ◽  
Liver Slices

OXYDATION DES ANABOLIKUMS 1-METHYL-ANDROST-1-EN-17β-OL-3-ON MIT WASSERSTOFFTRANSFER AUF ÖSTRON

1971 ◽  
Vol 67 (3) ◽  
pp. 517-530 ◽  
Author(s):  
Martin Wenzel
Keyword(s):  
Rat Liver ◽  
Anabolic Steroid ◽  
Female Rats ◽  
Male Rats ◽  
Female Rat ◽  
Liver Slices ◽  
Androgen Effects ◽  
Biochemical Difference

ABSTRACT With the aid of metenolon-17α-T a tritium-transfer to oestrone in rat liver slices was demonstrated. This tritium-transfer from metenolon17α-T to oestrone yielding tritium-labelled oestradiol had a higher efficiency in male than in female rat liver. Correspondingly in the presence of metenolon the relation of oestrone to oestradiol is changed more in male than in female rat liver. Looking for biochemical differences between the anabolic steroid metenolon and testosterone the oxydation at C17 was measured in different organs of the rat using 17α-T-labelled steroids. The highest oxydation rate was found for both steroids in the liver. In the sexual organs of male rats the oxydation rate of testosterone was 50–10 times higher than that of the anabolic steroid. This difference was less in sexual organs of female rats. This result of a greater biochemical difference between both steroids in males than in females leads to the question, whether the dissociation between the anabolic and the androgen effects is higher in males than in females.

scholarly journals THE ESTIMATION OF FATTY ACID SYNTHESIS IN RAT LIVER SLICES

1953 ◽  
Vol 205 (1) ◽  
pp. 401-408
Author(s):  
Grace Medes ◽  
Morris A. Spirtes ◽  
Sidney Weinhouse
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Synthesis ◽  
Acid Synthesis ◽  
Liver Slices
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