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

Year: 1988

Type: article

Abstract: 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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(88)81132-3

Authors: Heinrich J.G. Matthies, H.Clive Palfrey, Richard J. Miller

Institution: University of Chicago

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: National Institutes of Health

OpenAlex ID: W2082394879

FWCI: 1.358

Cites: 20

Cited by: 20

Related to: 10