Domain-induced activation of human phospholipase A2 type IIA: Local versus global lipid composition

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Domain-induced activation of human phospholipase A2 type IIA : Local versus global lipid composition. / Leidy, Chad; Linderoth, Lars; Andresen, Thomas L.; Mouritsen, Ole G.; Jørgensen, Kent; Peters, Günther H.

In: Biophysical Journal, Vol. 90, No. 9, 05.2006, p. 3165-3175.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Leidy, C, Linderoth, L, Andresen, TL, Mouritsen, OG, Jørgensen, K & Peters, GH 2006, 'Domain-induced activation of human phospholipase A2 type IIA: Local versus global lipid composition', Biophysical Journal, vol. 90, no. 9, pp. 3165-3175. https://doi.org/10.1529/biophysj.105.070987

APA

Leidy, C., Linderoth, L., Andresen, T. L., Mouritsen, O. G., Jørgensen, K., & Peters, G. H. (2006). Domain-induced activation of human phospholipase A2 type IIA: Local versus global lipid composition. Biophysical Journal, 90(9), 3165-3175. https://doi.org/10.1529/biophysj.105.070987

Vancouver

Leidy C, Linderoth L, Andresen TL, Mouritsen OG, Jørgensen K, Peters GH. Domain-induced activation of human phospholipase A2 type IIA: Local versus global lipid composition. Biophysical Journal. 2006 May;90(9):3165-3175. https://doi.org/10.1529/biophysj.105.070987

Author

Leidy, Chad ; Linderoth, Lars ; Andresen, Thomas L. ; Mouritsen, Ole G. ; Jørgensen, Kent ; Peters, Günther H. / Domain-induced activation of human phospholipase A2 type IIA : Local versus global lipid composition. In: Biophysical Journal. 2006 ; Vol. 90, No. 9. pp. 3165-3175.

Bibtex

@article{7776545ef7f247dbb6be76a46dc5329e,
title = "Domain-induced activation of human phospholipase A2 type IIA: Local versus global lipid composition",
abstract = "Secretory human phospholipase A2 type IIA (PLA2-IIA) catalyzes the hydrolysis of the sn-2 ester bond in glycerolipids to produce fatty acids and lysolipids. The enzyme is coupled to the inflammatory response, and its specificity toward anionic membrane interfaces suggests a role as a bactericidal agent. PLA2-IIA may also target perturbed native cell membranes that expose anionic lipids to the extracellular face. However, anionic lipid contents in native cells appear lower than the threshold levels necessary for activation. By using phosphatidylcholine/phosphatidylglycerol model systems, we show that local enrichment of anionic lipids into fluid domains triggers PLA2-IIA activity. In addition, the compositional range of enzyme activity is shown to be related to the underlying lipid phase diagram. A comparison is done between PLA2-IIA and snake venom PLA2, which in contrast to PLA2-IIA hydrolyzes both anionic and zwitterionic membranes. In general, this work shows that PLA2-IIA activation can be accomplished through local enrichment of anionic lipids into domains, indicating a mechanism for PLA2-IIA to target perturbed native membranes with low global anionic lipid contents. The results also show that the underlying lipid phase diagram, which determines the lipid composition at a local level, can be used to predict PLA2-IIA activity.",
author = "Chad Leidy and Lars Linderoth and Andresen, {Thomas L.} and Mouritsen, {Ole G.} and Kent J{\o}rgensen and Peters, {G{\"u}nther H.}",
year = "2006",
month = "5",
doi = "10.1529/biophysj.105.070987",
language = "English",
volume = "90",
pages = "3165--3175",
journal = "Biophysical Society. Annual Meeting. Abstracts",
issn = "0523-6800",
publisher = "Biophysical Society",
number = "9",

}

RIS

TY - JOUR

T1 - Domain-induced activation of human phospholipase A2 type IIA

T2 - Local versus global lipid composition

AU - Leidy, Chad

AU - Linderoth, Lars

AU - Andresen, Thomas L.

AU - Mouritsen, Ole G.

AU - Jørgensen, Kent

AU - Peters, Günther H.

PY - 2006/5

Y1 - 2006/5

N2 - Secretory human phospholipase A2 type IIA (PLA2-IIA) catalyzes the hydrolysis of the sn-2 ester bond in glycerolipids to produce fatty acids and lysolipids. The enzyme is coupled to the inflammatory response, and its specificity toward anionic membrane interfaces suggests a role as a bactericidal agent. PLA2-IIA may also target perturbed native cell membranes that expose anionic lipids to the extracellular face. However, anionic lipid contents in native cells appear lower than the threshold levels necessary for activation. By using phosphatidylcholine/phosphatidylglycerol model systems, we show that local enrichment of anionic lipids into fluid domains triggers PLA2-IIA activity. In addition, the compositional range of enzyme activity is shown to be related to the underlying lipid phase diagram. A comparison is done between PLA2-IIA and snake venom PLA2, which in contrast to PLA2-IIA hydrolyzes both anionic and zwitterionic membranes. In general, this work shows that PLA2-IIA activation can be accomplished through local enrichment of anionic lipids into domains, indicating a mechanism for PLA2-IIA to target perturbed native membranes with low global anionic lipid contents. The results also show that the underlying lipid phase diagram, which determines the lipid composition at a local level, can be used to predict PLA2-IIA activity.

AB - Secretory human phospholipase A2 type IIA (PLA2-IIA) catalyzes the hydrolysis of the sn-2 ester bond in glycerolipids to produce fatty acids and lysolipids. The enzyme is coupled to the inflammatory response, and its specificity toward anionic membrane interfaces suggests a role as a bactericidal agent. PLA2-IIA may also target perturbed native cell membranes that expose anionic lipids to the extracellular face. However, anionic lipid contents in native cells appear lower than the threshold levels necessary for activation. By using phosphatidylcholine/phosphatidylglycerol model systems, we show that local enrichment of anionic lipids into fluid domains triggers PLA2-IIA activity. In addition, the compositional range of enzyme activity is shown to be related to the underlying lipid phase diagram. A comparison is done between PLA2-IIA and snake venom PLA2, which in contrast to PLA2-IIA hydrolyzes both anionic and zwitterionic membranes. In general, this work shows that PLA2-IIA activation can be accomplished through local enrichment of anionic lipids into domains, indicating a mechanism for PLA2-IIA to target perturbed native membranes with low global anionic lipid contents. The results also show that the underlying lipid phase diagram, which determines the lipid composition at a local level, can be used to predict PLA2-IIA activity.

UR - http://www.scopus.com/inward/record.url?scp=33646154889&partnerID=8YFLogxK

U2 - 10.1529/biophysj.105.070987

DO - 10.1529/biophysj.105.070987

M3 - Journal article

C2 - 16461407

AN - SCOPUS:33646154889

VL - 90

SP - 3165

EP - 3175

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 9

ER -

ID: 230978253