Calmodulin- and protein phosphorylation-independent release of catecholamines from PC-12 cells

Heinrich J G Matthies, H. Clive Palfrey, Richard J. Miller*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Catecholamine secretion from PC-12 cells can be triggered by agents that increase intracellular Ca2+ and is enhanced by phorbol esters and agents that elevate intracellular cAMP concentrations. In mutant PC-12 cells lacking cAMP-dependent protein kinase (PK-A) in which protein kinase C (PK-C) was down-regulated, Ca2+-dependent secretion occurred normally but was no longer enhanced by cAMP or phorbol esters. In digitonin-permeabilized PC-12 cells that lacked PK-C and PK-A, a range of calmodulin (CaM) inhibitors failed to block Ca2+-triggered catecholamine release. Moreover, Mn2+, a CaM activator, failed to trigger catecholamine release whereas Ba2+, which does not activate CaM, supported secretion. These results indicate that the basic mechanism of stimulus/secretion coupling in PC-12 cells does not absolutely require a regulated protein phosphorylation- or calmodulin-dependent step.

Original languageEnglish (US)
Pages (from-to)238-242
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - Mar 14 1988


  • (PC-12 cell)
  • Calmodulin
  • Exocytosis
  • Protein kinase C
  • cAMP-dependent protein kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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