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Cyclic AMP-dependent protein kinase promotes glucocorticoid receptor function.
Open accessAbstract
Murine lymphoma cell lines such as WEHI-7 exhibit a cytolytic response to both cAMP and glucocorticoids. We have exploited this behavior to ask if cyclic AMP-dependent protein kinase plays a role in regulating glucocorticoid receptor function. We have found that cAMP-resistant cell lines containing a defective cAMP-dependent protein kinase activity give rise to spontaneous steroid-resistant variants at a high frequency (approximately 10(-7)) relative to wild type cells (less than 10(-10)). Unlike previous results with wild type cells, nearly complete loss of glucocorticoid receptor function was observed in a single selection using unmutagenized cAMPr derivatives of WEHI-7. Thus, the initial selection of the cAMPr phenotype serves as a permissive step toward the acquisition of glucocorticoid resistance in WEHI-7. In addition, cAMP was found to increase the levels of steroid binding in these cell lines, and the dose response was dependent upon the phenotype of the cyclic AMP-dependent protein kinase. The results demonstrate an important role for cAMP in regulating glucocorticoid receptor activity and strongly suggest that this novel two-step selection scheme leads to the isolation of new forms of glucocorticoid resistance.
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Cortisol and noradrenaline support each other in release of energy-rich fuels or calcium/phosphorus from stores.
“Since cortisol and noradrenaline are often cooperative in their individual functions by increasing the respective signaling pathway of the β-adrenoceptor and glucocorticoid receptor type α (for example, [55,56]), these two hormones support each other in release of energy-rich fuels or calcium/phosphorus from stores.”
From Interaction of the endocrine system with inflammation: a function of energy and volume regulation (2014) · cites this paper as [55]
Release of cortisol is typically coupled to release of norepinephrine, which leads to stronger signalling through the beta adrenoceptor.
“Release of cortisol is typically coupled to release of norepinephrine, which leads to stronger signalling through the b adrenoceptor; several studies have shown cooperation of cortisol and norepinephrine at a molecular level.”
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Metadata
- Authors
- Gruol, D. J., Campbell, N. F., & Bourgeois, S.
- Affiliations
- Salk Institute for Biological Studies (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-04
- Volume
- 261
- Issue
- 11
- Pages
- 4909-4914
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1534019559
- Cited by
- 94
- References
- 40
- Citations by year
- 2023: 1 · 2022: 1 · 2019: 2 · 2015: 2 · 2014: 3
- FWCI
- 4.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 36146)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Keywords
- protein kinase A, glucocorticoid receptor, glucocorticoid resistance, steroid resistance, lymphoma cell lines, steroid binding
- MeSH terms
- Cyclic AMP, Animals, Cell Line, Dexamethasone, Bucladesine, Drug Resistance, Female, Colforsin, Kinetics, Lymphoma, Mice, Inbred BALB C, Mutation, Phenotype, Protein Kinases, Receptors, Glucocorticoid, Mice
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