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Activation of phospholipase A2 by Hsp70 in vitro

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  • Ajay K Mahalka
  • Christian Code
  • Behnam Rezaijahromi
  • Thomas Kirkegaard
  • Jaattela, Marja
  • Paavo Kinnunen
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+).
OriginalsprogEngelsk
TidsskriftBBA General Subjects
Vol/bind1808
Udgave nummer10
Sider (fra-til)2569-72
Antal sider4
ISSN0304-4165
DOI
StatusUdgivet - 2011

ID: 38488637