ArticleBMC cell biology2004
Protein kinase Czeta regulates phospholipase D activity in rat-1 fibroblasts expressing the alpha1A adrenergic receptor.
Article in BMC cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 6 citations in OpenAlex.
- Protein kinase C zeta suppresses low- or high-grade colorectal cancer (CRC) phenotypes by interphase centrosome anchoring.The Journal of pathology · 2018Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
backgroundPhenylephrine (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.
resultsPHE 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.
conclusionalpha1A 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.
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Registered trials
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