Activation of phospholipase A2 by Hsp70 in vitro

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Standard

Activation of phospholipase A2 by Hsp70 in vitro. / Mahalka, Ajay K; Code, Christian; Rezaijahromi, Behnam; Kirkegaard, Thomas; Jaattela, Marja; Kinnunen, Paavo.

I: BBA General Subjects, Bind 1808, Nr. 10, 2011, s. 2569-72.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Mahalka, AK, Code, C, Rezaijahromi, B, Kirkegaard, T, Jaattela, M & Kinnunen, P 2011, 'Activation of phospholipase A2 by Hsp70 in vitro', BBA General Subjects, bind 1808, nr. 10, s. 2569-72. https://doi.org/10.1016/j.bbamem.2011.06.002

APA

Mahalka, A. K., Code, C., Rezaijahromi, B., Kirkegaard, T., Jaattela, M., & Kinnunen, P. (2011). Activation of phospholipase A2 by Hsp70 in vitro. BBA General Subjects, 1808(10), 2569-72. https://doi.org/10.1016/j.bbamem.2011.06.002

Vancouver

Mahalka AK, Code C, Rezaijahromi B, Kirkegaard T, Jaattela M, Kinnunen P. Activation of phospholipase A2 by Hsp70 in vitro. BBA General Subjects. 2011;1808(10):2569-72. https://doi.org/10.1016/j.bbamem.2011.06.002

Author

Mahalka, Ajay K ; Code, Christian ; Rezaijahromi, Behnam ; Kirkegaard, Thomas ; Jaattela, Marja ; Kinnunen, Paavo. / Activation of phospholipase A2 by Hsp70 in vitro. I: BBA General Subjects. 2011 ; Bind 1808, Nr. 10. s. 2569-72.

Bibtex

@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 a-synuclein and Alzheimer {\ss}-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 Mg(2+).",

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",

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

language = "English",

volume = "1808",

pages = "2569--72",

journal = "B B A - General Subjects",

issn = "0304-4165",

publisher = "Elsevier",

number = "10",

}

RIS

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

Y1 - 2011

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 a-synuclein and Alzheimer ß-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 Mg(2+).

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 a-synuclein and Alzheimer ß-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 Mg(2+).

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

VL - 1808

SP - 2569

EP - 2572

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 10

ER -

ID: 38488637