Phosphatidic Acid Directly Activates Endothelial Cell Protein Kinase C

J. E. Stasek, V. Natarajan, Joe GN Garcia

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

The metabolism of phosphatidic acid (PA) yields diacylglycerol (DAG), a known activator of protein kinase C (PKC). To examine potential direct effects of PA on PKC activation, PKC purified from bovine pulmonary artery endothelial cells (BPAEC) was utilized in an in vitro assay examining γ-[32P]ATP phosphorylation of H1 histone. In the presence of Ca2+ and phosphatidylserine (PS), DAG (80 μM) produced maximal PKC activity (6.4 pmol γ-[32P]ATP incorporated/μg/min). Dioleoyl-PA (80 μM) and l-stearoyl,2-arachidonyl-PA (80 μM) activated PKC in a concentration-dependent manner (maximal activity of 2.01 ± 0.1 pmol/μg/min). Unlike unlabelled phorbol esters or DAG, dioleoyl-PA did not significantly alter the binding of [3H]-phorbol dibutyrate to PKC, suggesting that PA directly activates endothelial cell PKC in a manner distinct from DAG-mediated PKC activation.

Original languageEnglish (US)
Pages (from-to)134-141
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume191
Issue number1
DOIs
StatePublished - Feb 26 1993
Externally publishedYes

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Phosphatidic Acids
Endothelial cells
Protein Kinase C
Endothelial Cells
Diglycerides
Adenosine Triphosphate
Chemical activation
Phosphorylation
Phosphatidylserines
Phorbol Esters
Metabolism
Histones
Pulmonary Artery
Assays

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Phosphatidic Acid Directly Activates Endothelial Cell Protein Kinase C. / Stasek, J. E.; Natarajan, V.; Garcia, Joe GN.

In: Biochemical and Biophysical Research Communications, Vol. 191, No. 1, 26.02.1993, p. 134-141.

Research output: Contribution to journalArticle

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abstract = "The metabolism of phosphatidic acid (PA) yields diacylglycerol (DAG), a known activator of protein kinase C (PKC). To examine potential direct effects of PA on PKC activation, PKC purified from bovine pulmonary artery endothelial cells (BPAEC) was utilized in an in vitro assay examining γ-[32P]ATP phosphorylation of H1 histone. In the presence of Ca2+ and phosphatidylserine (PS), DAG (80 μM) produced maximal PKC activity (6.4 pmol γ-[32P]ATP incorporated/μg/min). Dioleoyl-PA (80 μM) and l-stearoyl,2-arachidonyl-PA (80 μM) activated PKC in a concentration-dependent manner (maximal activity of 2.01 ± 0.1 pmol/μg/min). Unlike unlabelled phorbol esters or DAG, dioleoyl-PA did not significantly alter the binding of [3H]-phorbol dibutyrate to PKC, suggesting that PA directly activates endothelial cell PKC in a manner distinct from DAG-mediated PKC activation.",
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