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 Mg(2+).
authors.affiliation: Department of Biomedical Engineering and Computational Science, Aalto University, Espoo, Finland.
authors.forename: Ajay K
authors.initials: AK
authors.lastname: Mahalka
authors.forename: Christian
authors.initials: C
authors.lastname: Code
authors.forename: Behnam Rezai
authors.initials: BR
authors.lastname: Jahromi
authors.forename: Behnam
authors.initials: B
authors.lastname: Rezaijahromi
authors.forename: Thomas
authors.initials: T
authors.lastname: Kirkegaard
authors.forename: Marja
authors.initials: M
authors.lastname: Jäättelä
authors.forename: Paavo K J
authors.initials: PK
authors.lastname: Kinnunen
mesh_terms: D055162:Biocatalysis; D004789:Enzyme Activation; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D054467:Phospholipases A2 / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D018840:HSP70 Heat-Shock Proteins; D054467:Phospholipases A2