scholarly journals Development of adenylate kinase isoenzymes in rat liver

1971 ◽  
Vol 122 (4) ◽  
pp. 553-555 ◽  
Author(s):  
R. Filler ◽  
W. E. Criss
Keyword(s):  
Rat Liver ◽  
Liver Cell ◽  
Adenylate Kinase ◽  
Energy Flow ◽  
Kinase Activity ◽  
Adult Liver ◽  
Foetal Liver ◽  
Foetal Rat ◽  
Wet Weight ◽  
Developing Rat

Total adenylate kinase activity was determined in developing rat liver. The activity was 18 units/g wet weight of tissue in foetal liver; this increased to 41 units/g immediately after birth and continued increasing until adult activities of 150 units/g were reached after two weeks. The adenylate kinase activity was separated into four isoenzymes. Only isoenzymes II and III were observed in foetal rat liver. Isoenzyme II activity was 2 units/g in the foetal liver and increased to 25 units/g in adult liver. Adenylate kinase III activity was 20 units/g in the foetal liver and increased to 118 units/g in adult liver. The possible role that adenylate kinase might have in regulating the energy flow in the developing liver cell is discussed.

scholarly journals The role of glycogen synthase phosphatase in the glucocorticoid-induced deposition of glycogen in foetal rat liver

1980 ◽  
Vol 192 (2) ◽  
pp. 607-612 ◽  
Author(s):  
F Vanstapel ◽  
F Doperé ◽  
W Stalmans
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Late Gestation ◽  
Adult Liver ◽  
Foetal Liver ◽  
Foetal Rat ◽  
Experimental Approaches ◽  
Protein Components

1. The mechanism that underlies the induction of glycogen synthesis in the foetal rat liver by glucocorticoids was reinvestigated in conditions where the accumulation of glycogen is either precociously induced with dexamethasone or inhibited by steroid deprivation. It appears that glucocorticoids act as the physiological trigger for glycogen synthesis by inducing both glycogen synthase (a known effect) and its activating enzyme, glycogen synthase phosphatase. 2. The activity of glycogen synthase phosphatase in adult liver stems from the interaction of two protein components [Doperé, Vanstapel & Stalmans (1980) Eur. J. Biochem. 104, 137–146]. Two independent experimental approaches indicate that the cytosolic ‘S-component’ is already well developed in the foetal liver before the onset of glycogen synthesis. The manifold glucocorticoid-dependent increase in synthase phosphatase activity during late gestation must be attributed to the specific development of the glycogen-bound ‘G-component’.

scholarly journals The development of gluconeogenesis in rat liver. Effects of glucagon and ether

1970 ◽  
Vol 120 (2) ◽  
pp. 385-392 ◽  
Author(s):  
Helen Philippidis ◽  
F. J. Ballard
Keyword(s):  
Rat Liver ◽  
Redox State ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Fold Increase ◽  
Similar Increase ◽  
Ether Anaesthesia ◽  
Foetal Liver ◽  
Foetal Rat ◽  
Newborn Animals

1. Administration of glucagon to foetal rats produced a 10–15-fold increase in hepatic phosphoenolpyruvate carboxykinase activity together with a similar increase in the overall pathway of pyruvate conversion into glycogen in liver slices. 2. Glucagon was without effect on gluconeogenesis in vivo, which remained at approx. 0.1% of the incorporation as measured in newborn animals. 3. The apparent discrepancy between these results was due to the ether anaesthesia that was required for experimentation in vivo. Under conditions when minimal ether was used, the rates of labelling of glycogen from [3-14C]pyruvate in vivo were increased 10–20-fold and there was an additional stimulus by glucagon. 4. Ether anaesthesia produced a more reduced redox state of the foetal liver cytosol and lowered the ATP/ADP concentration ratio. 5. It is proposed that these effects are significant in the limitation of gluconeogenesis in the foetal rat liver, so that only with high phosphoenolpyruvate carboxykinase activity, high ATP concentration and a relatively oxidized cytosol redox state will a functional gluconeogenic pathway be present.

Insulin-like growth factor-I (IGF-I) stimulates tyrosine kinase activity in purified receptors from a rat liver cell line

1984 ◽  
Vol 119 (1) ◽  
pp. 6-13 ◽  
Author(s):  
Yehiel Zick ◽  
Norio Sasaki ◽  
Robert W. Rees-Jones ◽  
George Grunberger ◽  
S.Peter Nissley ◽  
...  
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Cell Line ◽  
Rat Liver ◽  
Liver Cell ◽  
Kinase Activity ◽  
Tyrosine Kinase Activity ◽  
Factor I ◽  
Liver Cell Line ◽  
Igf I

Adenylate kinase activity in rat liver

1968 ◽  
Vol 6 ◽  
pp. 425-436 ◽  
Author(s):  
Richard C. Adelman ◽  
Chai Ho Lo ◽  
Sidney Weinhouse
Keyword(s):  
Rat Liver ◽  
Adenylate Kinase ◽  
Kinase Activity

scholarly journals Precocious development of cytochrome P-450 in neonatal rat liver after glucocorticoid treatment

1979 ◽  
Vol 182 (1) ◽  
pp. 233-235 ◽  
Author(s):  
J E A Leakey ◽  
J R Fouts
Keyword(s):  
Rat Liver ◽  
Neonatal Rat ◽  
Adult Liver ◽  
Glucocorticoid Treatment ◽  
Early Postnatal Development ◽  
Liver Cytochrome ◽  
Foetal Rat ◽  
Cytochrome P 450 ◽  
Precocious Development ◽  
Hepatic Cytochrome

Intraperitoneal injection of neonatal rats with glucocorticoid hormones causes precocious development of hepatic cytochrome P-450. Glucagon injection fails to stimulate this cytochrome P-450 development. Adult liver cytochrome P-450 is less responsive to glucocorticoid stimulation than is that of neonatal rat liver. Adrenalectomy of prematurely delivered neonatal animals prevents the early postnatal development of cytochrome P-450. Glucocorticoids failed to increase cytochrome P-450 concentrations in foetal rat liver. These findings imply that, although glucocorticoids are mandatory regulatory factors controlling cytochrome P-450 development, they are not themselves the ‘trigger’ initiating onset of that development.

scholarly journals The effect of cytosine arabinoside and bromodeoxyuridine on the appearance of tyrosine aminotransferase in cultured foetal hepatocytes of the rat

1980 ◽  
Vol 188 (3) ◽  
pp. 929-932 ◽  
Author(s):  
G C Yeoh ◽  
I T Oliver
Keyword(s):  
Cell Differentiation ◽  
Rat Liver ◽  
Cytosine Arabinoside ◽  
Culture Medium ◽  
Tyrosine Aminotransferase ◽  
Aminotransferase Activity ◽  
Inhibitory Effects ◽  
Foetal Liver ◽  
Foetal Rat

1. The acquisition of dexamethasone-inducibility of tyrosine aminotransferase activity by hepatocytes cultured from 15-day-foetal rat liver is blocked in the presence of cytosine arabinoside. 2. Similar results are obtained in the presence of bormodeoxyuridine. 3. No effects on steroid-inducibility of tyrosine aminotransferase are obtained with either of the above compounds in hepatocytes cultured from 19-day-foetal liver. 4. the inhibitory effects of the agents are substantially reversed after their removal from the culture medium. 5. The effects of bromodeoxyuridine suggest that cell differentiation, with respect to tyrosine aminotransferase-inducibility, occurs in cultures of 15-day-doetal hepatocytes. 6. The effects of cytosine arabinoside suggest that such an event is dependent on mitosis.

scholarly journals Comparison of the properties of two forms of pyruvate kinase in rat liver and determination of their separate activities during development

1972 ◽  
Vol 127 (4) ◽  
pp. 721-731 ◽  
Author(s):  
Marshall C. Middleton ◽  
Deryck G. Walker
Keyword(s):  
Skeletal Muscle ◽  
Pyruvate Kinase ◽  
Rat Liver ◽  
Developmental Period ◽  
Late Gestation ◽  
Kinetic Properties ◽  
Foetal Rat ◽  
Neonatal Liver ◽  
Developing Rat

1. Two forms of hepatic pyruvate kinase, designated type L and type M, were distinguished on the basis of kinetic, chromatographic, electrophoretic and immunological criteria. They were partially purified and their properties compared with each other and with the purified enzyme from skeletal muscle. 2. In contrast with type L, the type M enzyme showed no marked evidence of co-operative interactions with phosphoenolpyruvate and was not stimulated by fructose diphosphate. 3. The activity profiles of type L and type M enzymes were determined in developing rat liver by utilizing differences in the kinetic properties of the two forms. The high activity of type M enzyme in the early foetal rat decreased in late gestation and immediately after birth to reach a low value, which remained essentially constant for the remainder of the developmental period. The activity of type L enzyme, in contrast, was low in the early foetal and neonatal liver but increased markedly at the onset of weaning. 4. Possible roles of the two forms of hepatic pyruvate kinase in the control of glycolysis and gluconeogenesis are discussed.

scholarly journals Pathways of fructose conversion into glucose in foetal rat liver

1965 ◽  
Vol 97 (2) ◽  
pp. 365-370 ◽  
Author(s):  
FJ Ballard
Keyword(s):  
Rat Liver ◽  
Specific Activity ◽  
High Specific Activity ◽  
Direct Conversion ◽  
Seminal Vesicles ◽  
Adult Liver ◽  
Adult Rats ◽  
Liver Slices ◽  
Foetal Rat ◽  
Glucose Formation

1. Glucose, formed from [1-(14)C]fructose or [6-(14)C]fructose in rat-liver slices, has been isolated as gluconate and degraded to give the radioactivity in C-1, C-2-5 and C-6. 2. By using this method it has been shown that, in liver from foetal rats younger than 20 days, glucose is formed from fructose without splitting of the molecule by the aldolase reaction. The rate of glucose formation from fructose in liver from these foetuses is approximately half of the rate in adult liver. 3. The direct conversion of fructose into glucose in foetal rat liver is not via sorbitol as in seminal vesicles, as this pathway cannot be detected. 4. When liver slices are incubated with [U-(14)C]fructose of high specific activity, the labelled intermediates are similar whether from liver from 18-day foetal, newborn or adult rats. 5. These findings are discussed with reference to the changing pathways of fructose metabolism during perinatal development of the liver in the rat.

scholarly journals Influence of Aging on the Carcinogen-Induced Protein Kinase Activity in Rat Liver Cell Nuclei.

2002 ◽  
Vol 196 (3) ◽  
pp. 131-138
Author(s):  
TETSUO SAKAI ◽  
RITSUKO SATO ◽  
HITOSHI MIZUNO ◽  
HIDEO MATSUO ◽  
AKIRA NOMURA ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Liver Cell ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Cell Nuclei

scholarly journals Demonstration of two functionally heterogenous groups within the activities of UDP-glucuronosyltransferase towards a series of 4-alkyl-substituted phenols

1979 ◽  
Vol 178 (2) ◽  
pp. 443-447 ◽  
Author(s):  
G J Wishart ◽  
M T Campbell
Keyword(s):  
Rat Liver ◽  
Colorimetric Assay ◽  
In Utero ◽  
Substituted Phenols ◽  
Adult Liver ◽  
Molecular Weights ◽  
Foetal Liver ◽  
Neonatal Group ◽  
Udp Glucuronosyltransferase ◽  
Phenol Reagent

1. A simple colorimetric assay for UDP-glucuronosyltransferase activities towards phenolic substrates, using Folin & Ciocalteu's phenol reagent, is described. The assay is used to measure rat liver transferase activities towards substrates from a series of 4-alkyl-substituted phenols. 2. Activities towards phenol, 4-methylphenol and 4-ethylphenol develop near-adult values before birth, are precociously stimulated by dexa methasone in utero and are stimulated 3–4-fold by 3-methylcholanthrene in adult liver. These are assigned to a “late-foetal”! group of transferase activities. 3. Activities towards 4-n-propylphenol, 4-s-butylphenol and 4-t-butylphenol are negligible in late-foetal liver, developing to near-adult values in the first 4 postnatal days, and are not affected by dexamethasone or 3-methylcholanthrene. They are assigned to a “neonatal” group of transferase activities. 4. Although 4-ethylphenol and 4-n-propylphenol differ only by a single –CH2– moiety, this is sufficient to change the acceptability of these substrates respectively from the late-foetal to the neonatal group of transferase activities. The change is distinct, with no overlapping of substrate acceptability between the two groups of transferase activities. 5. From consideration of the above and other substrates, the two groups of transferase activities do not distinguish substrates on the basis of their molecular weights or lipophilicity. The distinguishing feature appears to be the specific molecular configurations of the substrates.

Sign in / Sign up

Export Citation Format

Share Document