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

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

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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 β2-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.

Original languageEnglish
Pages (from-to)14094-14100
Number of pages7
JournalJournal of Biological Chemistry
Volume282
Issue number19
DOIs
Publication statusPublished - 11 May 2007

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Sastry, K. S. R., 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. Journal of Biological Chemistry, 282(19), 14094-14100. https://doi.org/10.1074/jbc.M611370200