Activation of phospholipase A2 by Hsp70 in vitro

Ajay K Mahalka; Christian Code; Behnam Rezaijahromi; Thomas Kirkegaard; Marja Jaattela; Paavo Kinnunen

doi:10.1016/j.bbamem.2011.06.002

Activation of phospholipase A2 by Hsp70 in vitro

Ajay K Mahalka, Christian Code, Behnam Rezaijahromi, Thomas Kirkegaard, Marja Jaattela, Paavo Kinnunen

Morphogenesis and Differentiation Program

9 Citationer (Scopus)

Abstract

We recently suggested a novel mechanism for the activation of phospholipase A2 (PLA2), with a (catalytically) highly active oligomeric state, which subsequently becomes inactivated by conversion into amyloid. This process can be activated by lysophosphatidylcholine which promotes both oligomerization and amyloid activation/inactivation. The heat shock protein 70 (Hsp70), has been demonstrated to be able to revert the conversion of α-synuclein and Alzheimer β-peptide to amyloid fibrils in vitro. Accordingly, we would expect Hsp70 to sustain the lifetime of the active state of the enzyme oligomer by attenuating the conversion of the enzyme oligomers into inactive amyloid. Here we show that Hsp70 activates PLA2 in vitro, in a manner requiring ATP and Mg²⁺.

Originalsprog	Engelsk
Tidsskrift	BBA General Subjects
Vol/bind	1808
Udgave nummer	10
Sider (fra-til)	2569-72
Antal sider	4
ISSN	0304-4165
DOI	https://doi.org/10.1016/j.bbamem.2011.06.002
Status	Udgivet - okt. 2011

Adgang til dokumentet

10.1016/j.bbamem.2011.06.002

Citationsformater

@article{e8507669364e4de097d7eb666856eb9d,

title = "Activation of phospholipase A2 by Hsp70 in vitro",

abstract = "We recently suggested a novel mechanism for the activation of phospholipase A2 (PLA2), with a (catalytically) highly active oligomeric state, which subsequently becomes inactivated by conversion into amyloid. This process can be activated by lysophosphatidylcholine which promotes both oligomerization and amyloid activation/inactivation. The heat shock protein 70 (Hsp70), has been demonstrated to be able to revert the conversion of α-synuclein and Alzheimer β-peptide to amyloid fibrils in vitro. Accordingly, we would expect Hsp70 to sustain the lifetime of the active state of the enzyme oligomer by attenuating the conversion of the enzyme oligomers into inactive amyloid. Here we show that Hsp70 activates PLA2 in vitro, in a manner requiring ATP and Mg2+.",

keywords = "Biocatalysis, Enzyme Activation, HSP70 Heat-Shock Proteins, Phospholipases A2, Spectroscopy, Fourier Transform Infrared",

author = "Mahalka, {Ajay K} and Christian Code and Behnam Rezaijahromi and Thomas Kirkegaard and Marja Jaattela and Paavo Kinnunen",

year = "2011",

month = oct,

doi = "10.1016/j.bbamem.2011.06.002",

language = "English",

volume = "1808",

pages = "2569--72",

journal = "BBA General Subjects",

issn = "0304-4165",

publisher = "Elsevier",

number = "10",

}

TY - JOUR

T1 - Activation of phospholipase A2 by Hsp70 in vitro

AU - Mahalka, Ajay K

AU - Code, Christian

AU - Rezaijahromi, Behnam

AU - Kirkegaard, Thomas

AU - Jaattela, Marja

AU - Kinnunen, Paavo

PY - 2011/10

Y1 - 2011/10

N2 - We recently suggested a novel mechanism for the activation of phospholipase A2 (PLA2), with a (catalytically) highly active oligomeric state, which subsequently becomes inactivated by conversion into amyloid. This process can be activated by lysophosphatidylcholine which promotes both oligomerization and amyloid activation/inactivation. The heat shock protein 70 (Hsp70), has been demonstrated to be able to revert the conversion of α-synuclein and Alzheimer β-peptide to amyloid fibrils in vitro. Accordingly, we would expect Hsp70 to sustain the lifetime of the active state of the enzyme oligomer by attenuating the conversion of the enzyme oligomers into inactive amyloid. Here we show that Hsp70 activates PLA2 in vitro, in a manner requiring ATP and Mg2+.

AB - We recently suggested a novel mechanism for the activation of phospholipase A2 (PLA2), with a (catalytically) highly active oligomeric state, which subsequently becomes inactivated by conversion into amyloid. This process can be activated by lysophosphatidylcholine which promotes both oligomerization and amyloid activation/inactivation. The heat shock protein 70 (Hsp70), has been demonstrated to be able to revert the conversion of α-synuclein and Alzheimer β-peptide to amyloid fibrils in vitro. Accordingly, we would expect Hsp70 to sustain the lifetime of the active state of the enzyme oligomer by attenuating the conversion of the enzyme oligomers into inactive amyloid. Here we show that Hsp70 activates PLA2 in vitro, in a manner requiring ATP and Mg2+.

KW - Biocatalysis

KW - Enzyme Activation

KW - HSP70 Heat-Shock Proteins

KW - Phospholipases A2

KW - Spectroscopy, Fourier Transform Infrared

U2 - 10.1016/j.bbamem.2011.06.002

DO - 10.1016/j.bbamem.2011.06.002

M3 - Journal article

C2 - 21683684

SN - 0304-4165

VL - 1808

SP - 2569

EP - 2572

JO - BBA General Subjects

JF - BBA General Subjects

IS - 10

ER -

Activation of phospholipase A2 by Hsp70 in vitro

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater