Involvement of mitogen activated protein kinase (mapk) and cytosolic phospholipase A2 (cPLA2) translocation to nuclear envelope in acetylcholine (ACh) induced prostacyclin synthesis in coronary endothelial cells of rabbit heart

H. Kan, Y. Rtian, Kafait Malik

Research output: Contribution to journalArticle

Abstract

ACh-induced proslacyclin (PGI2) synthesis, in rabbit coronary cndothelial cells (CEC) is mediated by activation of cPLA2 but not phospholipase C or protein kinase C (THE FASEB J. VOL. 9, No. 3, 111, 1995). The purpose of this study was to determine if ACh-induced PGI2 synthesis involves cPLA2 translocation to plasma or nuclear membrane and MAPK activation in the CEC of the rahhit heart. ACh (3 μM) increased synthesis of PGI2, measured as immunoreaclive 6-keto-PGF1α, in CEC. The increase in PGI2 production by ACh was associated with translocation ol cPLA2 hut not MAPK to the nuclear envelope and increased cPLA2 and MAPK activity in CEC. AG 126, a tyrosine kinase inhibitor known to decrease MAPK activity, attenuated PGI2 synthesis and ePLA2 and MAPK activation elicited by ACh ; cPLA2 translocation to nuclear membrane was nut altered by this agent. Extracellular Ca2+ depletion inhibited AChinduced cPLA2 translocalicm to nuclear envelope hut not MAPK activation in CEC. These data suggest that ACh-induced increase in Ca2+ influx promotes cPLA2 translocatiim to the nuclear membrane and that MAPK stimulates cPLA2 to release araehidonic acid for PGI2 synthesis in the CEC of the rabbit heart.

Original languageEnglish (US)
JournalFASEB Journal
Volume10
Issue number3
StatePublished - Dec 1 1996

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Cytosolic Phospholipases A2
Nuclear Envelope
Endothelial cells
Epoprostenol
Mitogen-Activated Protein Kinases
Acetylcholine
Endothelial Cells
Rabbits
Chemical activation
Membranes
Nuts
Type C Phospholipases
Protein-Tyrosine Kinases
Protein Kinase C
Cell Membrane
Plasmas
Acids

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

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title = "Involvement of mitogen activated protein kinase (mapk) and cytosolic phospholipase A2 (cPLA2) translocation to nuclear envelope in acetylcholine (ACh) induced prostacyclin synthesis in coronary endothelial cells of rabbit heart",
abstract = "ACh-induced proslacyclin (PGI2) synthesis, in rabbit coronary cndothelial cells (CEC) is mediated by activation of cPLA2 but not phospholipase C or protein kinase C (THE FASEB J. VOL. 9, No. 3, 111, 1995). The purpose of this study was to determine if ACh-induced PGI2 synthesis involves cPLA2 translocation to plasma or nuclear membrane and MAPK activation in the CEC of the rahhit heart. ACh (3 μM) increased synthesis of PGI2, measured as immunoreaclive 6-keto-PGF1α, in CEC. The increase in PGI2 production by ACh was associated with translocation ol cPLA2 hut not MAPK to the nuclear envelope and increased cPLA2 and MAPK activity in CEC. AG 126, a tyrosine kinase inhibitor known to decrease MAPK activity, attenuated PGI2 synthesis and ePLA2 and MAPK activation elicited by ACh ; cPLA2 translocation to nuclear membrane was nut altered by this agent. Extracellular Ca2+ depletion inhibited AChinduced cPLA2 translocalicm to nuclear envelope hut not MAPK activation in CEC. These data suggest that ACh-induced increase in Ca2+ influx promotes cPLA2 translocatiim to the nuclear membrane and that MAPK stimulates cPLA2 to release araehidonic acid for PGI2 synthesis in the CEC of the rabbit heart.",
author = "H. Kan and Y. Rtian and Kafait Malik",
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language = "English (US)",
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T1 - Involvement of mitogen activated protein kinase (mapk) and cytosolic phospholipase A2 (cPLA2) translocation to nuclear envelope in acetylcholine (ACh) induced prostacyclin synthesis in coronary endothelial cells of rabbit heart

AU - Kan, H.

AU - Rtian, Y.

AU - Malik, Kafait

PY - 1996/12/1

Y1 - 1996/12/1

N2 - ACh-induced proslacyclin (PGI2) synthesis, in rabbit coronary cndothelial cells (CEC) is mediated by activation of cPLA2 but not phospholipase C or protein kinase C (THE FASEB J. VOL. 9, No. 3, 111, 1995). The purpose of this study was to determine if ACh-induced PGI2 synthesis involves cPLA2 translocation to plasma or nuclear membrane and MAPK activation in the CEC of the rahhit heart. ACh (3 μM) increased synthesis of PGI2, measured as immunoreaclive 6-keto-PGF1α, in CEC. The increase in PGI2 production by ACh was associated with translocation ol cPLA2 hut not MAPK to the nuclear envelope and increased cPLA2 and MAPK activity in CEC. AG 126, a tyrosine kinase inhibitor known to decrease MAPK activity, attenuated PGI2 synthesis and ePLA2 and MAPK activation elicited by ACh ; cPLA2 translocation to nuclear membrane was nut altered by this agent. Extracellular Ca2+ depletion inhibited AChinduced cPLA2 translocalicm to nuclear envelope hut not MAPK activation in CEC. These data suggest that ACh-induced increase in Ca2+ influx promotes cPLA2 translocatiim to the nuclear membrane and that MAPK stimulates cPLA2 to release araehidonic acid for PGI2 synthesis in the CEC of the rabbit heart.

AB - ACh-induced proslacyclin (PGI2) synthesis, in rabbit coronary cndothelial cells (CEC) is mediated by activation of cPLA2 but not phospholipase C or protein kinase C (THE FASEB J. VOL. 9, No. 3, 111, 1995). The purpose of this study was to determine if ACh-induced PGI2 synthesis involves cPLA2 translocation to plasma or nuclear membrane and MAPK activation in the CEC of the rahhit heart. ACh (3 μM) increased synthesis of PGI2, measured as immunoreaclive 6-keto-PGF1α, in CEC. The increase in PGI2 production by ACh was associated with translocation ol cPLA2 hut not MAPK to the nuclear envelope and increased cPLA2 and MAPK activity in CEC. AG 126, a tyrosine kinase inhibitor known to decrease MAPK activity, attenuated PGI2 synthesis and ePLA2 and MAPK activation elicited by ACh ; cPLA2 translocation to nuclear membrane was nut altered by this agent. Extracellular Ca2+ depletion inhibited AChinduced cPLA2 translocalicm to nuclear envelope hut not MAPK activation in CEC. These data suggest that ACh-induced increase in Ca2+ influx promotes cPLA2 translocatiim to the nuclear membrane and that MAPK stimulates cPLA2 to release araehidonic acid for PGI2 synthesis in the CEC of the rabbit heart.

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