Protein kinase C-β and -δ Isoenzymes promote arachidonic acid production and proliferation of MonoMac-6 cells

Zoltán Griger, Edit Páyer, Ildikó Kovács, Balázs I. Tóth, László Kovács, S. Sipka, T. Bíró

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

In this study, we investigated the putative roles of certain protein kinase C (PKC) isoenzymes in the regulation of proliferation and arachidonic acid (AA) release in the human monocytoid MonoMac-6 cell line. Experiments employing specific PKC inhibitors and molecular biological methods (RNA-interference, recombinant overexpression) revealed that the two dominantly expressed isozymes, i.e., the "conventional" cPKCβ and the "novel" nPKCδ, promote AA production and cellular proliferation. In addition, using different phospholipase A2 (PLA2) inhibitors, we were able to show that the calcium-independent iPLA2 as well as diacylglycerol lipase (but not the cytosolic PLA2) function as "downstream" targets of cPKCβ and nPKCδ. In addition, we have also found that, among the other existing PKC isoforms, cPKCα plays a minor inhibitory role, whereas nPKCε and aPKCζ apparently do not regulate these cellular processes. In conclusion, in this paper we provide the first evidence that certain PKC isoforms play pivotal, specific, and (at least partly) antagonistic roles in the regulation of AA production and cellular proliferation of human monocytoid MonoMac-6 cells.

Original languageEnglish
Pages (from-to)1031-1042
Number of pages12
JournalJournal of Molecular Medicine
Volume85
Issue number9
DOIs
Publication statusPublished - Sep 2007

Fingerprint

Arachidonic Acid
Protein Kinase C
Isoenzymes
Protein Isoforms
Phospholipase A2 Inhibitors
Cell Proliferation
Cytosolic Phospholipases A2
Lipoprotein Lipase
Protein C Inhibitor
Protein Kinase Inhibitors
RNA Interference
Calcium
Cell Line

Keywords

  • Arachidonic acid release
  • Isoenzymes
  • MonoMac6 cells
  • Proliferation
  • Protein kinase C

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Protein kinase C-β and -δ Isoenzymes promote arachidonic acid production and proliferation of MonoMac-6 cells. / Griger, Zoltán; Páyer, Edit; Kovács, Ildikó; Tóth, Balázs I.; Kovács, László; Sipka, S.; Bíró, T.

In: Journal of Molecular Medicine, Vol. 85, No. 9, 09.2007, p. 1031-1042.

Research output: Contribution to journalArticle

Griger, Zoltán ; Páyer, Edit ; Kovács, Ildikó ; Tóth, Balázs I. ; Kovács, László ; Sipka, S. ; Bíró, T. / Protein kinase C-β and -δ Isoenzymes promote arachidonic acid production and proliferation of MonoMac-6 cells. In: Journal of Molecular Medicine. 2007 ; Vol. 85, No. 9. pp. 1031-1042.
@article{e3dea7cc17514507be2b1a0cfd8c651b,
title = "Protein kinase C-β and -δ Isoenzymes promote arachidonic acid production and proliferation of MonoMac-6 cells",
abstract = "In this study, we investigated the putative roles of certain protein kinase C (PKC) isoenzymes in the regulation of proliferation and arachidonic acid (AA) release in the human monocytoid MonoMac-6 cell line. Experiments employing specific PKC inhibitors and molecular biological methods (RNA-interference, recombinant overexpression) revealed that the two dominantly expressed isozymes, i.e., the {"}conventional{"} cPKCβ and the {"}novel{"} nPKCδ, promote AA production and cellular proliferation. In addition, using different phospholipase A2 (PLA2) inhibitors, we were able to show that the calcium-independent iPLA2 as well as diacylglycerol lipase (but not the cytosolic PLA2) function as {"}downstream{"} targets of cPKCβ and nPKCδ. In addition, we have also found that, among the other existing PKC isoforms, cPKCα plays a minor inhibitory role, whereas nPKCε and aPKCζ apparently do not regulate these cellular processes. In conclusion, in this paper we provide the first evidence that certain PKC isoforms play pivotal, specific, and (at least partly) antagonistic roles in the regulation of AA production and cellular proliferation of human monocytoid MonoMac-6 cells.",
keywords = "Arachidonic acid release, Isoenzymes, MonoMac6 cells, Proliferation, Protein kinase C",
author = "Zolt{\'a}n Griger and Edit P{\'a}yer and Ildik{\'o} Kov{\'a}cs and T{\'o}th, {Bal{\'a}zs I.} and L{\'a}szl{\'o} Kov{\'a}cs and S. Sipka and T. B{\'i}r{\'o}",
year = "2007",
month = "9",
doi = "10.1007/s00109-007-0209-y",
language = "English",
volume = "85",
pages = "1031--1042",
journal = "Journal of Molecular Medicine",
issn = "0946-2716",
publisher = "Springer Verlag",
number = "9",

}

TY - JOUR

T1 - Protein kinase C-β and -δ Isoenzymes promote arachidonic acid production and proliferation of MonoMac-6 cells

AU - Griger, Zoltán

AU - Páyer, Edit

AU - Kovács, Ildikó

AU - Tóth, Balázs I.

AU - Kovács, László

AU - Sipka, S.

AU - Bíró, T.

PY - 2007/9

Y1 - 2007/9

N2 - In this study, we investigated the putative roles of certain protein kinase C (PKC) isoenzymes in the regulation of proliferation and arachidonic acid (AA) release in the human monocytoid MonoMac-6 cell line. Experiments employing specific PKC inhibitors and molecular biological methods (RNA-interference, recombinant overexpression) revealed that the two dominantly expressed isozymes, i.e., the "conventional" cPKCβ and the "novel" nPKCδ, promote AA production and cellular proliferation. In addition, using different phospholipase A2 (PLA2) inhibitors, we were able to show that the calcium-independent iPLA2 as well as diacylglycerol lipase (but not the cytosolic PLA2) function as "downstream" targets of cPKCβ and nPKCδ. In addition, we have also found that, among the other existing PKC isoforms, cPKCα plays a minor inhibitory role, whereas nPKCε and aPKCζ apparently do not regulate these cellular processes. In conclusion, in this paper we provide the first evidence that certain PKC isoforms play pivotal, specific, and (at least partly) antagonistic roles in the regulation of AA production and cellular proliferation of human monocytoid MonoMac-6 cells.

AB - In this study, we investigated the putative roles of certain protein kinase C (PKC) isoenzymes in the regulation of proliferation and arachidonic acid (AA) release in the human monocytoid MonoMac-6 cell line. Experiments employing specific PKC inhibitors and molecular biological methods (RNA-interference, recombinant overexpression) revealed that the two dominantly expressed isozymes, i.e., the "conventional" cPKCβ and the "novel" nPKCδ, promote AA production and cellular proliferation. In addition, using different phospholipase A2 (PLA2) inhibitors, we were able to show that the calcium-independent iPLA2 as well as diacylglycerol lipase (but not the cytosolic PLA2) function as "downstream" targets of cPKCβ and nPKCδ. In addition, we have also found that, among the other existing PKC isoforms, cPKCα plays a minor inhibitory role, whereas nPKCε and aPKCζ apparently do not regulate these cellular processes. In conclusion, in this paper we provide the first evidence that certain PKC isoforms play pivotal, specific, and (at least partly) antagonistic roles in the regulation of AA production and cellular proliferation of human monocytoid MonoMac-6 cells.

KW - Arachidonic acid release

KW - Isoenzymes

KW - MonoMac6 cells

KW - Proliferation

KW - Protein kinase C

UR - http://www.scopus.com/inward/record.url?scp=34548037900&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34548037900&partnerID=8YFLogxK

U2 - 10.1007/s00109-007-0209-y

DO - 10.1007/s00109-007-0209-y

M3 - Article

C2 - 17549442

AN - SCOPUS:34548037900

VL - 85

SP - 1031

EP - 1042

JO - Journal of Molecular Medicine

JF - Journal of Molecular Medicine

SN - 0946-2716

IS - 9

ER -