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

Authors

• Konduru S R Sastry
• Yelena Karpova
• Sergey Prokopovich
• Adrienne J Smith
• Brian Essau
• Avynash Gersappe
• Jonathan P Carson
• Michael J Weber
• Thomas C Register
• Yong Q Chen
• Raymond B Penn
• George Kulik

Publication/Presentation Date

5-11-2007

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.

Volume

282

Issue

19

First Page

14094

Last Page

14100

ISSN

0021-9258

Published In/Presented At

Sastry, K. S., Karpova, Y., Prokopovich, S., Smith, A. J., Essau, B., Gersappe, A., Carson, J. P., Weber, M. J., Register, T. C., Chen, Y. Q., Penn, R. B., & Kulik, G. (2007). Epinephrine protects cancer cells from apoptosis via activation of cAMP-dependent protein kinase and BAD phosphorylation. The Journal of biological chemistry, 282(19), 14094–14100. https://doi.org/10.1074/jbc.M611370200

Disciplines

Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods

PubMedID

17353197

Department(s)

Administration and Leadership

Document Type

Article