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

doi:10.1016/S0014-5793(00)02326-7

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 journal › Article › peer-review

46 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 language	English
Pages (from-to)	243-248
Number of pages	6
Journal	FEBS Letters
Volume	489
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(00)02326-7
Publication status	Published - 2001 Feb 2
Externally published	Yes

Bibliographical note

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.

Keywords

Annexin
Specific interaction
Substrate depletion
cPLA2 inhibition

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/S0014-5793(00)02326-7

Cite this

@article{1565e1a995134e528523e1f553928894,

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

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.",

keywords = "Annexin, Specific interaction, Substrate depletion, cPLA2 inhibition",

author = "Kim, {Seung Wook} and Jesang Ko and Kim, {Jae Hong} and Choi, {Eung Chil} and Na, {Doe Sun}",

note = "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.",

year = "2001",

month = feb,

day = "2",

doi = "10.1016/S0014-5793(00)02326-7",

language = "English",

volume = "489",

pages = "243--248",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "2-3",

}

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

UR - http://www.scopus.com/inward/record.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

SN - 0014-5793

VL - 489

SP - 243

EP - 248

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this