Premium
Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: specific interaction model
Author(s) -
Kim Seung-Wook,
Ko Jesang,
Kim Jae Hong,
Choi Eung Chil,
Na Doe Sun
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02326-7
Subject(s) - cytosol , phospholipase a2 , immunoprecipitation , chemistry , function (biology) , phospholipase , microbiology and biotechnology , biophysics , biochemistry , biology , enzyme , gene
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‐II 2 P11 2 , ANX‐III, and ANX‐V. Under the conditions for the specific interaction model, ANX‐I, ΔANX‐I, and ANX‐II 2 P11 2 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‐II 2 P11 2 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.