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Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma

We have established a continous cell line (G1) in which the tyrosine hydroxylase specific activity is increased as much as 50-100-fold in response to dexamethasone. This response is specific for the glucocorticoid class of steroid hormones; it is elicited by dexamethasone, corticosterone, and triamc...

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Detalles Bibliográficos
Autores principales: Goodman, R., Edgar, D., Thoenen, H., Wechsler, W., Herschman, H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1978
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110175/
https://www.ncbi.nlm.nih.gov/pubmed/27525
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author Goodman, R.
Edgar, D.
Thoenen, H.
Wechsler, W.
Herschman, H.
author_facet Goodman, R.
Edgar, D.
Thoenen, H.
Wechsler, W.
Herschman, H.
author_sort Goodman, R.
collection PubMed
description We have established a continous cell line (G1) in which the tyrosine hydroxylase specific activity is increased as much as 50-100-fold in response to dexamethasone. This response is specific for the glucocorticoid class of steroid hormones; it is elicited by dexamethasone, corticosterone, and triamcinolone, but not by estradiol, testosterone, progesterone, or deoxycorticosterone acetate. The increase in tyrosine hydroxylase specific activity is likely to be due to the increased synthesis of new enzyme protein rather than an activation of existing protein molecules, inasmuch as this increase is completely blocked by cycloheximide.
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spelling pubmed-21101752008-05-01 Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma Goodman, R. Edgar, D. Thoenen, H. Wechsler, W. Herschman, H. J Cell Biol Rapid Communication We have established a continous cell line (G1) in which the tyrosine hydroxylase specific activity is increased as much as 50-100-fold in response to dexamethasone. This response is specific for the glucocorticoid class of steroid hormones; it is elicited by dexamethasone, corticosterone, and triamcinolone, but not by estradiol, testosterone, progesterone, or deoxycorticosterone acetate. The increase in tyrosine hydroxylase specific activity is likely to be due to the increased synthesis of new enzyme protein rather than an activation of existing protein molecules, inasmuch as this increase is completely blocked by cycloheximide. The Rockefeller University Press 1978-07-01 /pmc/articles/PMC2110175/ /pubmed/27525 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Rapid Communication
Goodman, R.
Edgar, D.
Thoenen, H.
Wechsler, W.
Herschman, H.
Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
title Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
title_full Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
title_fullStr Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
title_full_unstemmed Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
title_short Glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
title_sort glucocorticoid induction of tyrosine hydroxylase in a continous cell line of rat pheochromocytoma
topic Rapid Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110175/
https://www.ncbi.nlm.nih.gov/pubmed/27525
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