TY - JOUR
T1 - Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity
T2 - Specific interaction model
AU - Kim, Seung Wook
AU - Ko, Jesang
AU - Kim, Jae Hong
AU - Choi, Eung Chil
AU - Na, Doe Sun
N1 - Funding Information:
This study was supported in part by Grants to D.S.N. from the Ministry of Health and Welfare (HMP-98-B-2-0007) and from the Ministry of Science and Technology (00-G-08-02-A-100). We thank Dr. Waisman for providing us with ANX-II and ANX-II 2 P11. We also thank Dr. Russo-Marie for sending us ANX-III cDNA.
PY - 2001/2/2
Y1 - 2001/2/2
N2 - 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.
AB - 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.
KW - Annexin
KW - Specific interaction
KW - Substrate depletion
KW - cPLA2 inhibition
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U2 - 10.1016/S0014-5793(00)02326-7
DO - 10.1016/S0014-5793(00)02326-7
M3 - Article
C2 - 11165258
AN - SCOPUS:0035793464
VL - 489
SP - 243
EP - 248
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2-3
ER -