Annexin-I inhibits PMA-induced c-fos SRE activation by suppressing cytosolic phospholipase A2 signal

Jiyoung Oh, Hae Jin Rhee, Seung Wook Kim, Soon Bae Kim, Hye Jin You, Jae-Hong Kim, Doe Sun Na

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25 Citations (Scopus)


Annexin-I (ANX-I) is a 37-kDa protein with a calcium-dependent phospholipid-binding property. Previously we have observed the inhibition of cytosolic phospholipase A2 (cPLA2) by ANX-I in the studies using purified recombinant ANX-I, and proposed a specific interaction model for the mechanism of cPLA2 inhibition by ANX-I [Kim et al. (1994) FEBS Lett. 343, 251-255]. Here we have studied the role of ANX-I in the cPLA2 signaling pathway by transient transfection assay. The stimulation of Rat2 fibroblast cells with phorbol 12-myristate 13-acetate (PMA) induced the c-fos serum response element (SRE). The SRE stimulation by PMA was dramatically reduced by (1) pretreatment with a cPLA2-specific inhibitor, arachidonyltrifluoromethyl ketone, or (2) co-transfection with antisense cPLA2 oligonucleotide, indicating that the SRE activation was through cPLA2 activation. Co-transfection with an ANX-I expression vector also reduced the SRE stimulation by PMA, suggesting the inhibition of cPLA2 by ANX-I. The active domain of ANX-I was mapped using various deletion mutants. ANX-I(1-113) and ANX-I(34-346) were fully active, whereas ANX-I(114-346) abolished the activity. Therefore the activity was in the amino acid 34 to 113 region, which corresponds to the conserved domain I of ANX-I. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)244-248
Number of pages5
JournalFEBS Letters
Issue number3
Publication statusPublished - 2000 Jul 21
Externally publishedYes



  • Annexin-I
  • c-fos serum response element
  • Cytosolic phospholipase A2
  • Phorbol 12-myristate 13-acetate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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