Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: Specific interaction model

Seung Wook Kim, Jesang Ko, Jae Hong Kim, Eung Chil Choi, Doe Sun Na

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Annexins (ANXs) are a family of proteins with calcium-dependent phospholipid binding properties. Although inhibition of phospholipase A2 (PLA2) by ANX-I has been reported, the mechanism is still controversial. Previously we proposed a 'specific interaction' model for the mechanism of cytosolic PLA2 (cPLA2) inhibition by ANX-I [Kim et al., FEBS Lett. 343 (1994) 251-255]. Here we have studied the cPLA2 inhibition mechanism using ANX-I, N-terminally deleted ANX-I (ΔANX-I), ANX-II, ANX-II2P112, ANX-III, and ANX-V. Under the conditions for the specific interaction model, ANX-I, ΔANX-I, and ANX-II2P112 inhibited cPLA2, whereas inhibition by ANX-II and ANX-III was negligible. Inhibition by ANX-V was much smaller than that by ANX-I. The protein-protein interactions between cPLA2 and ANX-I, ΔANX-I, and ANX-II2P112 were verified by immunoprecipitation. We can therefore conclude that inhibition of cPLA2 by specific interaction is not a general function of all ANXs, and is rather a specific function of ANX-I. The results are consistent with the specific interaction model.

Original languageEnglish
Pages (from-to)243-248
Number of pages6
JournalFEBS Letters
Volume489
Issue number2-3
DOIs
Publication statusPublished - 2001 Feb 2

Keywords

  • Annexin
  • Specific interaction
  • Substrate depletion
  • cPLA2 inhibition

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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