scholarly journals Ontogeny of the glucocorticoid receptor and its relationship to tyrosine aminotransferase induction in cultured foetal hepatocytes

1981 ◽  
Vol 198 (2) ◽  
pp. 301-307 ◽  
Author(s):  
M H Cake ◽  
G C T Yeoh ◽  
I T Oliver
Keyword(s):  
Glucocorticoid Receptor ◽  
Cytosine Arabinoside ◽  
Tyrosine Aminotransferase ◽  
Receptor Activity ◽  
Cultured Hepatocytes ◽  
Foetal Liver ◽  
Receptor Concentration ◽  
Steroid Responsiveness ◽  
Haemopoietic Cells ◽  
Rate Of Accumulation

The glucocorticoid receptor activity that can be detected in the liver from 15-day foetal rats would appear to be associated with the haemopoietic cells. In hepatocytes, purified by culture for 1-2 days from 15-day foetal rats, the glucocorticoid receptor activity is low and dexamethasone does not induce the enzyme tyrosine aminotransferase. If culture is continued both receptor activity and steroid responsiveness are acquired. Cultured hepatocytes from 19-day foetal liver contain receptor from the first day of culture and, furthermore, the subsequent level of response to glucocorticoids is directly correlated with the actual receptor concentration. It would appear that the glucocorticoid receptor is not acquired by hepatocytes until after 18 days of gestation. Nevertheless, the fact that bromodeoxyuridine has no effect on the rate of accumulation of receptor in hepatocytes suggests that the differentiative event leading to the subsequent appearance of the receptor has already occurred before day 15 of gestation. However, the acquisition of the receptor would appear to be dependent on mitosis as cytosine arabinoside can inhibit the process.

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 The hormonal regulation of enzymes in prenatal and postnatal rat liver. Effects of adenosine 3′,5′-(cyclic)-monophosphate

1969 ◽  
Vol 115 (1) ◽  
pp. 19-24 ◽  
Author(s):  
Olga Greengard
Keyword(s):  
Growth Hormone ◽  
Hormonal Regulation ◽  
Time Course ◽  
Tyrosine Aminotransferase ◽  
Cyclic Monophosphate ◽  
Sequential Development ◽  
Foetal Liver ◽  
Old Rats ◽  
Postnatal Rats ◽  
Do So

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.

scholarly journals Regulation of Glucocorticoid Receptor Activity by 14–3-3-Dependent Intracellular Relocalization of the Corepressor RIP140

2001 ◽  
Vol 15 (4) ◽  
pp. 501-511 ◽  
Author(s):  
Johanna Zilliacus ◽  
Elin Holter ◽  
Hideki Wakui ◽  
Hiroshi Tazawa ◽  
Eckardt Treuter ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Receptor Activity

scholarly journals DNA binding-dependent glucocorticoid receptor activity promotes adipogenesis via Krüppel-like factor 15 gene expression

2010 ◽  
Vol 91 (2) ◽  
pp. 203-215 ◽  
Author(s):  
Maki Asada ◽  
Alexander Rauch ◽  
Hirohito Shimizu ◽  
Hiromi Maruyama ◽  
Shigeru Miyaki ◽  
...  
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Receptor Activity

Effects of a single inhaled budesonide/formoterol dose on glucocorticoid receptor activity in sputum of COPD patients

2016 ◽  
Author(s):  
Amir Hakim ◽  
Younis Khan ◽  
Ignacio Esteban ◽  
Anna Miller-Larsson ◽  
Peter Barnes ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Receptor Activity ◽  
Copd Patients ◽  
Inhaled Budesonide
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