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Cytosolic phospholipase A(2) activity associated with nuclei is not inhibited by arachidonyl trifluoromethyl ketone in macrophages stimulated with receptor-recognized forms of alpha(2)-macroglobulin.

Publication ,  Journal Article
Misra, UK; Pizzo, SV
Published in: Arch Biochem Biophys
July 1, 2000

We have studied the translocation of cytosolic phospholipase A(2) (cPLA(2)) to nuclei in macrophages stimulated with receptor-recognized forms of alpha(2)-macroglobulin (alpha(2)M*). Translocation of phosphorylated cPLA(2) to nuclei was determined by immunoprecipitation of cPLA(2) in (32)P(i)-labeled cells. The identity of cPLA(2) was established by comparing its mobility on gels with an authentic cPLA(2) standard. cPLA(2) activity was quantified by measuring the release of [(14)C]arachidonic acid from the substrate 1-palmitoyl-2-[1-(14)C]arachidonyl-sn-glycerophosphatidylcholine. alpha(2)M* caused a two- to threefold increase in cPLA(2) phosphorylation and its translocation to nuclei. The p38 MAPK inhibitor SB203580, PKC inhibitor chelerythrin, or depletion of intracellular Ca(2+) profoundly decreased cPLA(2) activity in nuclei isolated from agonist-stimulated cells. The requirement for Ca(2+), PKC, and p38 MAPK activation appears to be of major importance for nuclear cPLA(2) activity. In contrast to cellular cPLA(2) activity, nuclear cPLA(2) activity was not inhibited by arachidonyl trifluoromethyl ketone (AACOCF(3)) in agonist-stimulated cells. It is concluded that the association of cPLA(2) with nuclear membranes in agonist-stimulated cells modifies the activity and the sensitivity of the enzyme to inhibition by AACOCF(3) in this phospholipid environment.

Duke Scholars

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

July 1, 2000

Volume

379

Issue

1

Start / End Page

153 / 160

Location

United States

Related Subject Headings

  • p38 Mitogen-Activated Protein Kinases
  • alpha-Macroglobulins
  • Signal Transduction
  • Pyridines
  • Protein Kinase C
  • Phosphorylation
  • Phospholipases A
  • Phosphatidylcholines
  • Mitogen-Activated Protein Kinases
  • Mice, Inbred C57BL
 

Citation

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Misra, U. K., and S. V. Pizzo. “Cytosolic phospholipase A(2) activity associated with nuclei is not inhibited by arachidonyl trifluoromethyl ketone in macrophages stimulated with receptor-recognized forms of alpha(2)-macroglobulin.Arch Biochem Biophys 379, no. 1 (July 1, 2000): 153–60. https://doi.org/10.1006/abbi.2000.1878.
Misra, U. K., and S. V. Pizzo. “Cytosolic phospholipase A(2) activity associated with nuclei is not inhibited by arachidonyl trifluoromethyl ketone in macrophages stimulated with receptor-recognized forms of alpha(2)-macroglobulin.Arch Biochem Biophys, vol. 379, no. 1, July 2000, pp. 153–60. Pubmed, doi:10.1006/abbi.2000.1878.
Journal cover image

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

July 1, 2000

Volume

379

Issue

1

Start / End Page

153 / 160

Location

United States

Related Subject Headings

  • p38 Mitogen-Activated Protein Kinases
  • alpha-Macroglobulins
  • Signal Transduction
  • Pyridines
  • Protein Kinase C
  • Phosphorylation
  • Phospholipases A
  • Phosphatidylcholines
  • Mitogen-Activated Protein Kinases
  • Mice, Inbred C57BL