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Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20).
Cell Stress Chaperones. 2016 07; 21(4):617-29.CS

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+Show Affiliations

Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russian Federation.Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russian Federation.A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119991, Russian Federation.Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russian Federation. NBGusev@mail.ru.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

27061807

Citation

Muranova, Lydia K., et al. "Effect of Methylglyoxal Modification On the Structure and Properties of Human Small Heat Shock Protein HspB6 (Hsp20)." Cell Stress & Chaperones, vol. 21, no. 4, 2016, pp. 617-29.
Muranova LK, Perfilov MM, Serebryakova MV, et al. Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20). Cell Stress Chaperones. 2016;21(4):617-29.
Muranova, L. K., Perfilov, M. M., Serebryakova, M. V., & Gusev, N. B. (2016). Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20). Cell Stress & Chaperones, 21(4), 617-29. https://doi.org/10.1007/s12192-016-0686-4
Muranova LK, et al. Effect of Methylglyoxal Modification On the Structure and Properties of Human Small Heat Shock Protein HspB6 (Hsp20). Cell Stress Chaperones. 2016;21(4):617-29. PubMed PMID: 27061807.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20). AU - Muranova,Lydia K, AU - Perfilov,Maxim M, AU - Serebryakova,Marina V, AU - Gusev,Nikolai B, Y1 - 2016/04/09/ PY - 2016/01/19/received PY - 2016/03/26/accepted PY - 2016/03/06/revised PY - 2016/4/11/entrez PY - 2016/4/12/pubmed PY - 2017/3/14/medline KW - Diabetes KW - Methylglyoxal KW - Oligomeric structure KW - Phosphorylation KW - Small heat shock proteins SP - 617 EP - 29 JF - Cell stress & chaperones JO - Cell Stress Chaperones VL - 21 IS - 4 N2 - 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. SN - 1466-1268 UR - https://www.unboundmedicine.com/medline/citation/27061807/Effect_of_methylglyoxal_modification_on_the_structure_and_properties_of_human_small_heat_shock_protein_HspB6__Hsp20__ L2 - https://dx.doi.org/10.1007/s12192-016-0686-4 DB - PRIME DP - Unbound Medicine ER -