title: Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20).
abstract: Human small heat shock protein HspB6 (Hsp20) was modified by metabolic α-dicarbonyl compound methylglyoxal (MGO). At low MGO/HspB6 molar ratio, Arg13, Arg14, Arg27, and Arg102 were the primary sites of MGO modification. At high MGO/HspB6 ratio, practically, all Arg and Lys residues of HspB6 were modified. Both mild and extensive MGO modification decreased susceptibility of HspB6 to trypsinolysis and prevented its heat-induced aggregation. Modification by MGO was accompanied by formation of small quantities of chemically crosslinked dimers and did not dramatically affect quaternary structure of HspB6. Mild modification by MGO did not affect whereas extensive modification decreased interaction of HspB6 with HspB1. Phosphorylation of HspB6 by cyclic adenosine monophosphate (cAMP)-dependent protein kinase was inhibited after mild modification and completely prevented after extensive modification by MGO. Chaperone-like activity of HspB6 measured with subfragment 1 of skeletal myosin was enhanced after MGO modifications. It is concluded that Arg residues located in the N-terminal domain of HspB6 are easily accessible to MGO modification and that even mild modification by MGO affects susceptibility to trypsinolysis, phosphorylation by cAMP-dependent protein kinase, and chaperone-like activity of HspB6.
authors.affiliation: Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russian Federation.
authors.forename: Lydia K
authors.initials: LK
authors.lastname: Muranova
authors.affiliation: Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russian Federation.
authors.forename: Maxim M
authors.initials: MM
authors.lastname: Perfilov
authors.affiliation: A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119991, Russian Federation.
authors.forename: Marina V
authors.initials: MV
authors.lastname: Serebryakova
authors.affiliation: Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russian Federation. NBGusev@mail.ru.
authors.forename: Nikolai B
authors.initials: NB
authors.lastname: Gusev
mesh_terms: D000242:Cyclic AMP / Q000378:metabolism; D050886:HSP20 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D055551:HSP27 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins; D006801:Humans; D018832:Molecular Chaperones; D010766:Phosphorylation; D020836:Protein Structure, Quaternary; D011765:Pyruvaldehyde / Q000737:chemistry*
chemical_list: D050886:HSP20 Heat-Shock Proteins; D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; C494382:HSPB6 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011765:Pyruvaldehyde; D000242:Cyclic AMP
keywords: Diabetes; Methylglyoxal; Oligomeric structure; Phosphorylation; Small heat shock proteins