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 language | English |
|---|---|
| Pages (from-to) | 243-248 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 489 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 2001 Feb 2 |
| Externally published | Yes |
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Keywords
- Annexin
- cPLA2 inhibition
- Specific interaction
- Substrate depletion
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity : Specific interaction model. / Kim, Seung Wook; Ko, Je Sang; Kim, Jae-Hong; Choi, Eung Chil; Na, Doe Sun.
In: FEBS Letters, Vol. 489, No. 2-3, 02.02.2001, p. 243-248.Research output: Contribution to journal › Article
}
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, Je Sang
AU - Kim, Jae-Hong
AU - Choi, Eung Chil
AU - Na, Doe Sun
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 - cPLA2 inhibition
KW - Specific interaction
KW - Substrate depletion
UR - http://www.scopus.com/inward/record.url?scp=0035793464&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035793464&partnerID=8YFLogxK
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 -