title: Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin.
abstract: Effect of recombinant chicken small heat shock protein with molecular mass 24 kDa (Hsp24) and recombinant human small heat shock protein with molecular mass 27 kDa (Hsp27) on the heat-induced denaturation and aggregation of skeletal F-actin was analyzed by means of differential scanning calorimetry and light scattering. All small heat shock proteins did not affect thermal unfolding of F-actin measured by differential scanning calorimetry, but effectively prevented aggregation of thermally denatured actin. Small heat shock protein formed stable complexes with denatured (but not with intact) F-actin. The size of these highly soluble complexes was smaller than the size of intact F-actin filaments. It is supposed that protective effect of small heat shock proteins on the cytoskeleton is at least partly due to prevention of aggregation of denatured actin.
authors.affiliation: A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow 119071, Russia.
authors.forename: Anastasiya V
authors.initials: AV
authors.lastname: Pivovarova
authors.forename: Valeria V
authors.initials: VV
authors.lastname: Mikhailova
authors.forename: Ivan S
authors.initials: IS
authors.lastname: Chernik
authors.forename: Natalia A
authors.initials: NA
authors.lastname: Chebotareva
authors.forename: Dmitrii I
authors.initials: DI
authors.lastname: Levitsky
authors.forename: Nikolai B
authors.initials: NB
authors.lastname: Gusev
mesh_terms: D000199:Actins / Q000737:chemistry*; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D011489:Protein Denaturation
chemical_list: D000199:Actins; D006360:Heat-Shock Proteins