Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rotation-mediated aggregate cultures of foetal rat liver cells were prepared and grown in a chemically defined medium. Their capacity for cellular organisation and maturation was studied over a culture period of 3 wk by using both morphologic and biochemical criteria. It was found that within each aggregate, distinct liver cell types were present and attained their normal, differentiated phenotype. Parenchymal cells formed small acini with a central lumen. Within the first 2 wk in culture, albumin and ferritin mRNA levels were maintained, while the alpha-fetoprotein mRNA levels decreased, and tyrosine aminotransferase (TAT) gene expression increased. No significant response to glucocorticoids was observed in early cultures, whereas after 3 wk a marked increase in TAT mRNA levels was elicited by dexamethasone and glucagon (additive stimulatory effects). The results show that foetal rat liver cells cultured in a chemically defined medium are able to rearrange themselves into histotypic structures, and display a developmental pattern of gene expression comparable to that of perinatal rat liver in vivo. This culture system offers therefore a useful model to study the development and function of liver cells.
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PMID:Aggregate cultures of foetal rat liver cells: development and maintenance of liver gene expression. 289 50

1. The administration of glucagon, cAMP [adenosine 3',5'-(cyclic)-monophosphate], BcAMP [6-N-2'-O-dibutyryladenosine 3',5'-(cyclic)-monophosphate] or adrenaline to foetal rats during the last 2 days of gestation evoked the appearance of tyrosine aminotransferase and enhanced the accumulation of glucose 6-phosphatase in the liver. In foetuses 1-2 days younger only BcAMP was effective. After birth liver glucose 6-phosphatase no longer responds to glucagon or BcAMP. Tyrosine aminotransferase is still inducible by these agents in 2-day-old rats, but not in 50-day-old rats. After adrenalectomy of adults glucagon or BcAMP can enhance the induction of the enzyme by hydrocortisone. The results indicate that the ability to synthesize tyrosine aminotransferase and glucose 6-phosphatase when exposed to cAMP develops sooner than the ability to respond to glucagon with an increase in the concentration of cAMP; the responsiveness of enzymes to different hormones changes with age. A scheme illustrating the sequential development of competence in regulating the level of an enzyme is presented. 2. Actinomycin inhibited the effects of glucagon and BcAMP on liver tyrosine aminotransferase and glucose 6-phosphatase in foetal rats. Growth hormone, insulin and hydrocortisone did not enhance the formation of these enzymes. 3. The time-course of accumulation of glucose 6-phosphatase in the kidney is different from that in the liver. Hormones that increase the accumulation in foetal liver do not do so in the kidney of the same foetus or in the livers of postnatal rats.
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PMID:The hormonal regulation of enzymes in penatal and postnatal rat liver. Effects of adenosine 3',5'-(cyclic)-monophosphate. 418 80

1. Premature delivery of foetal rats by uterine section results in the rapid appearance of tyrosine aminotransferase activity in foetal liver, after an initial lag period of 3-6hr. 2. The premature induction of activity is completely repressible by actinomycin D given soon after delivery and partially repressible by puromycin and amino acid analogues. 3. Glucagon injections into foetal rats in utero lead to production of tyrosine aminotransferase in the foetal liver, but adrenalin and nor-adrenalin are without effect. 4. Injections of glucose, galactose, fructose and mannose into prematurely delivered rats repress the development of tyrosine aminotransferase activity about 50% when they are given 2hr. after delivery, but glucose has no significant effect when injected at delivery. 5. The results are discussed in relation to current hypotheses on the role of hormones in enzyme induction in foetal development.
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PMID:Factors affecting the premature induction of tyrosine aminotransferase in foetal rat liver. 438 41

Alpha-aminoisobutyric acid transport in hepatoma cells in culture was increased by insulin but not by hydrocortisone. Both of these agents induce tyrosine aminotransferase activity in this system. The apparent increase in alpha-aminoisobutyric acid transport and tyrosine aminotransferase activity produced by glucagon is probably caused by insulin contamination. Insulin did not increase transport in this system until after tyrosine aminotransferase activity had reached maximum levels. The mechanisms underlying increased alpha-aminoisobutyric acid transport appear to differ from those for tyrosine aminotransferase induction with hydrocortisone despite their close association in previous whole animal experiments.
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PMID:Amino acid transport in hepatoma cell cultures during tyrosine aminotransferase induction. 439 27

Intragastric administration of glucose inhibits the induction of serine dehydratase and tyrosine aminotransferase by glucagon in rat liver, but has no effect on the increase in hepatic adenosine 3',5'-monophosphate resulting from administration of glucagon. Thus, glucose repression in mammalian liver, unlike catabolite repression in microorganisms, appears to operate independently of the amounts of cyclic nucleotide in the cells.
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PMID:Cyclic adenosine 3',5'-monophosphate during glucose repression in the rat liver. 439 64

Administration of pyridoxine stabilizes rat liver tyrosine aminotransferase in vivo, whereas administration of cortisol, cyclic AMP, glucagon, insulin, tryptophan or tyrosine does not. The results of these and other experiments with pyridoxine are discussed in relation to the mechanisms of action of this vitamin on the activity of the enzyme.
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PMID:Stabilization of rat liver tyrosine aminotransferase in vivo by pyridoxine administration. 610 2

Freshly isolated liver parenchymal cells were maintained in either short-term monolayer, suspension of long-term monolayer culture. Rapidly occurring processes through hepatocellular membrane, e.g., the enhanced amino acid transport and the concomitantly increased potassium influx following progressive starvation, were kinetically evaluated best in short-term monolayer culture. The inducibility of tyrosine aminotransferase by glucagon, dexamethasone, and a combination of both was compared in suspension and in monolayer culture. The induction of slowly inducible foreign compound-metabolizing enzymes, (e.g., ethoxycoumarin-O-dealkylase, p-nitroanisole-O-demethylase, and UDP-glucuronyltransferase) by phenobarbital, 3-methylcholanthrene, and dexamethasone were studied in long-term monolayer culture. The latter system was also used to maintain isolated kidney cortical tubules for the investigation of renal enzyme adaptation during progressive time in culture.
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PMID:Primary monolayer culture of liver parenchymal cells and kidney cortical tubules as a useful new model for biochemical pharmacology and experimental toxicology. Studies in vitro on hepatic membrane transport, induction of liver enzymes, and adaptive changes in renal cortical enzymes. 610 78

1. The response of tyrosine aminotransferase activity in isolated liver cells has been studied under several conditions. 2. Activity is increased over a 5 h period by both glucagon and glucocorticoids in cells from adrenalectomized rats. The results do not support the view that glucagon action is dependent on preexposure of cells to steroid. 3. In cells from fed animals, significant stimulation is seen only when both glucagon and steroid are present together. 4. In cells from 48 h fasted rats steroid is effective, but glucagon is not significant so. 5. These anomalies are attributed to the differences in hormonal and nutritional status between the animals from which the cells are isolated.
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PMID:Factors affecting induction of tyrosine aminotransferase in isolated rat liver cells. 611 64

Tyrosine aminotransferase induction has been studied in hepatocytes from untreated, partially and fully glucocorticoid-induced rats: enzyme activities were initially 12.9 +/- 1.7 (n = 16), 41.4 +/- 3.2 (n = 6) and 117.9 +/- 10.5 (n = 7) munits/mg protein, respectively. Untreated or fully induced hepatocytes maintain initial levels, whereas partially induced hepatocytes increase their tyrosine aminotransferase activity even in the presence of actinomycin D. Fully induced hepatocytes possess a normal protein synthetizing machinery and the mechanisms to degrade selectively tyrosine aminotransferase. The effect of progesterone treatment is consistent with these cells retaining a high dexamethasone level. Glucagon induces tyrosine aminotransferase via its second messenger, cyclic AMP. This induction decreases dramatically with in vivo glucocorticoid treatment. Time courses and effects of inhibitors are consistent with these in vivo and in vitro treatments being alternative methods of inducing tyrosine aminotransferase by the same basic pretranslational step.
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PMID:The regulation of hepatic tyrosine aminotransferase. 611 30

The effects of acute and chronic glucagon treatment on phenylalanine metabolism in vivo in the rat have been investigated. A single, large dose of glucagon (2 mg/kg, i.p.) increased metabolism of a large load of phenylalanine (1.27 g/kg) via hydroxylation and transamination. The increased metabolism was associated with increased activities of hepatic phenylalanine:pyruvate aminotransferase, tyrosine aminotransferase and phenylalanine hydroxylase. In rats administered this amount of phenylalanine, the p-hydroxyphenylpyruvate dioxygenase reaction was apparently rate limiting, as indicated by increased urinary excretion of p-hydroxyphenylpyruvate and p-hydroxyphenyllactate, in addition to urinary excretion of phenylpyruvate and phenyllactate. Chronic glucagon treatment (1.25 mg/kg every 12 hr for 8 days) increased oxidation of the large phenylalanine load and urinary excretion of phenylpyruvate and phenyllactate but not p-hydroxyphenylpyruvate or p-hydroxyphenyllactate. The increased excretion of phenylpyruvate and phenyllactate was associated with an increase in hepatic phenylalanine: pyruvate aminotransferase activity. The absence of p-hydroxyphenylpyruvate in the urine and the increased oxidation of phenylalanine imply that, in rats administered glucagon chronically, flux of p-hydroxyphenylpyruvate through the p-hydroxyphenylpyruvate dioxygenase reaction was increased. A kinetic assay for phenylalanine hydroxylase based on measurement of oxygen consumption in described.
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PMID:Glucagon stimulation of phenylalanine metabolism. The effects of acute and chronic glucagon treatment. 612 64


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