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BMC Cell Biol. 2004 Jan 21;5:4.

Protein kinase Czeta regulates phospholipase D activity in rat-1 fibroblasts expressing the alpha1A adrenergic receptor.

Author information

1
Department of Pharmacology and Center for Connective Tissue Diseases and Vascular Biology, College of Medicine, The University of Tennessee Health Science Center, 874 Union Avenue, Memphis, TN 38163, USA. jparmentier@utmem.edu

Abstract

BACKGROUND:

Phenylephrine (PHE), an alpha1 adrenergic receptor agonist, increases phospholipase D (PLD) activity, independent of classical and novel protein kinase C (PKC) isoforms, in rat-1 fibroblasts expressing alpha1A adrenergic receptors. The aim of this study was to determine the contribution of atypical PKCzeta to PLD activation in response to PHE in these cells.

RESULTS:

PHE stimulated a PLD activity as demonstrated by phosphatidylethanol production. PHE increased PKCzeta translocation to the particulate cell fraction in parallel with a time-dependent decrease in its activity. PKCzeta activity was reduced at 2 and 5 min and returned to a sub-basal level within 10-15 min. Ectopic expression of kinase-dead PKCzeta, but not constitutively active PKCzeta, potentiated PLD activation elicited by PHE. A cell-permeable pseudosubstrate inhibitor of PKCzeta reduced basal PKCzeta activity and abolished PHE-induced PLD activation.

CONCLUSION:

alpha1A adrenergic receptor stimulation promotes the activation of a PLD activity by a mechanism dependent on PKCzeta; Our data also suggest that catalytic activation of PKCzeta is not required for PLD stimulation.

PMID:
14736339
PMCID:
PMC324395
DOI:
10.1186/1471-2121-5-4
[Indexed for MEDLINE]
Free PMC Article
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