Modulation of octopamine-mediated production of cyclic AMP by phorbol-ester-sensitive protein kinase C in an insect cell line

Gregory L. Orr, John W.D. Gole, Jyothi Gupta, Roger G.H. Downer

Research output: Contribution to journalArticlepeer-review

Abstract

The presence of protein kinase C (EC 2.7.1.37) in an insect cell line has been demonstrated. Phorbol 12-myristate 13-acetate (PMA), in micromolar concentrations, activated protein kinase C with a translocation of the enzyme from the cytosol to the particulate fraction. Cyclin AMP production in the presence of PMA, octopamine and a combination of both increased in a dose-dependent and time-dependent fashio. The biologically inactive 4α-phorbol 12,13-didecanoate had no effect on protein kinase C activity or on octopamine-mediated cyclic AMP production. Pretreatment of the cells with pertussis toxin had no effect on the responce of cells to octopamine or PMA. However, pretreatment with cholera toxin resulted in increased cyclic AMP production which was further enhanced when both cholera toxin and PMA were used in combination. Our data indicate that the octopamine-mediated cyclic AMP production is modulated by protein kinase C.

Original languageEnglish (US)
Pages (from-to)324-332
Number of pages9
JournalBBA - Molecular Cell Research
Volume970
Issue number3
DOIs
StatePublished - Jul 29 1988
Externally publishedYes

Keywords

  • (Insect cell)
  • Adenylate cyclase
  • Octopamine
  • Phorbol Ester
  • Protein kinase C
  • cyclic AMP

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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