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Epinephrine protects cancer cells from apoptosis via activation of cAMP-dependent protein kinase and BAD phosphorylation.

Authors :
Sastry KS
Karpova Y
Prokopovich S
Smith AJ
Essau B
Gersappe A
Carson JP
Weber MJ
Register TC
Chen YQ
Penn RB
Kulik G
Source :
The Journal of biological chemistry [J Biol Chem] 2007 May 11; Vol. 282 (19), pp. 14094-100. Date of Electronic Publication: 2007 Mar 12.
Publication Year :
2007

Abstract

The stress hormone epinephrine is known to elicit multiple systemic effects that include changes in cardiovascular parameters and immune responses. However, information about its direct action on cancer cells is limited. Here we provide evidence that epinephrine reduces sensitivity of cancer cells to apoptosis through interaction with beta(2)-adrenergic receptors. The antiapoptotic mechanism of epinephrine primarily involves phosphorylation and inactivation of the proapoptotic protein BAD by cAMP-dependent protein kinase. Moreover, BAD phosphorylation was observed at epinephrine concentrations found after acute and chronic psychosocial stress. Antiapoptotic signaling by epinephrine could be one of the mechanisms by which stress promotes tumorigenesis and decreases the efficacy of anti-cancer therapies.

Details

Language :
English
ISSN :
0021-9258
Volume :
282
Issue :
19
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
17353197
Full Text :
https://doi.org/10.1074/jbc.M611370200