Involvement of calcium/calmodulin kinase II (CaMKII), mitogen-activated protein kinase (MAPK), and protein kinase C (PKC) in the release of arachidonic acid (AA) elicited by phenylephrine (PE) via selective activation of phospholipase D in rat-1 fibroblasts transfected with alpha 1a/c adrenergic receptor (AR)

Y. Ruan, J. H. Parmentier, A. Ahmed, L. F. Allen, Kafait Malik

Research output: Contribution to journalArticle

Abstract

PE, an α1 AR agonist, stimulates AA release in rat-1 fibroblasts transfected with α1a/c AR (FASEB J., 10: A146, 1996). The present study was conducted to determine the type of phospholipase (PL) involved in AA release and the underlying mechanism of its activation by PE in these cells. PE (2 μM) increased AA release and PLD activity hut not PLA2 activity. Inhibitors of PLD (C2-ceramide, 10 μM), phosphatidate phosphohydrolase (propanolol, 50 μM) and diacylglycerol lipase (RHC80867, 10 μM) attenuated PE-induced AA release. Removal of calcium from the medium abolished the PE-induced AA release and PLD activity. The inhibitors of calmodulin (E6-brebamine, 10 μM), CaMKII (KN-93, 10 MM), and MAPK kinase (MEK) (PD-98059, 50 μM), attenuated both AA release and PLD activity. A PKC activator, phorbol-12-myristate-13-acetate (PMA), also increased AA release and PLD activity. The effect of PMA (5 μM) as well as of PE on AA release and PLD activity was attenuated by PKC the inhibitor hisindolylmaleimide I (0.5 μM), These data suggest that PE stimulates the release of AA in rat-1 fibroblasts transfected with α1a/c AR by selective activation of PLD via stimulation of PKC. CaMKII, and MEK.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number3
StatePublished - Dec 1 1997

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Adrenergic alpha-1 Receptors
MAP Kinase Kinase Kinases
Phospholipase D
Calcium-Calmodulin-Dependent Protein Kinases
Mitogen-Activated Protein Kinase Kinases
Phenylephrine
Fibroblasts
Mitogen-Activated Protein Kinases
Arachidonic Acid
Adrenergic Receptors
Protein Kinase C
Rats
Chemical activation
Calcium
Acetates
Phosphatidate Phosphatase
Adrenergic Agonists
Lipoprotein Lipase
Phospholipases
Protein C Inhibitor

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

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title = "Involvement of calcium/calmodulin kinase II (CaMKII), mitogen-activated protein kinase (MAPK), and protein kinase C (PKC) in the release of arachidonic acid (AA) elicited by phenylephrine (PE) via selective activation of phospholipase D in rat-1 fibroblasts transfected with alpha 1a/c adrenergic receptor (AR)",
abstract = "PE, an α1 AR agonist, stimulates AA release in rat-1 fibroblasts transfected with α1a/c AR (FASEB J., 10: A146, 1996). The present study was conducted to determine the type of phospholipase (PL) involved in AA release and the underlying mechanism of its activation by PE in these cells. PE (2 μM) increased AA release and PLD activity hut not PLA2 activity. Inhibitors of PLD (C2-ceramide, 10 μM), phosphatidate phosphohydrolase (propanolol, 50 μM) and diacylglycerol lipase (RHC80867, 10 μM) attenuated PE-induced AA release. Removal of calcium from the medium abolished the PE-induced AA release and PLD activity. The inhibitors of calmodulin (E6-brebamine, 10 μM), CaMKII (KN-93, 10 MM), and MAPK kinase (MEK) (PD-98059, 50 μM), attenuated both AA release and PLD activity. A PKC activator, phorbol-12-myristate-13-acetate (PMA), also increased AA release and PLD activity. The effect of PMA (5 μM) as well as of PE on AA release and PLD activity was attenuated by PKC the inhibitor hisindolylmaleimide I (0.5 μM), These data suggest that PE stimulates the release of AA in rat-1 fibroblasts transfected with α1a/c AR by selective activation of PLD via stimulation of PKC. CaMKII, and MEK.",
author = "Y. Ruan and Parmentier, {J. H.} and A. Ahmed and Allen, {L. F.} and Kafait Malik",
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AU - Ruan, Y.

AU - Parmentier, J. H.

AU - Ahmed, A.

AU - Allen, L. F.

AU - Malik, Kafait

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N2 - PE, an α1 AR agonist, stimulates AA release in rat-1 fibroblasts transfected with α1a/c AR (FASEB J., 10: A146, 1996). The present study was conducted to determine the type of phospholipase (PL) involved in AA release and the underlying mechanism of its activation by PE in these cells. PE (2 μM) increased AA release and PLD activity hut not PLA2 activity. Inhibitors of PLD (C2-ceramide, 10 μM), phosphatidate phosphohydrolase (propanolol, 50 μM) and diacylglycerol lipase (RHC80867, 10 μM) attenuated PE-induced AA release. Removal of calcium from the medium abolished the PE-induced AA release and PLD activity. The inhibitors of calmodulin (E6-brebamine, 10 μM), CaMKII (KN-93, 10 MM), and MAPK kinase (MEK) (PD-98059, 50 μM), attenuated both AA release and PLD activity. A PKC activator, phorbol-12-myristate-13-acetate (PMA), also increased AA release and PLD activity. The effect of PMA (5 μM) as well as of PE on AA release and PLD activity was attenuated by PKC the inhibitor hisindolylmaleimide I (0.5 μM), These data suggest that PE stimulates the release of AA in rat-1 fibroblasts transfected with α1a/c AR by selective activation of PLD via stimulation of PKC. CaMKII, and MEK.

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