Dimer-monomer equilibrium of human HSP27 is influenced by the in-cell macromolecular crowding environment and is controlled by fatty acids and heat.

Sato, Satoshi B; Sugiura, Miwa; Kurihara, Tatsuo

Sato, Satoshi B; Sugiura, Miwa; Kurihara, Tatsuo.

Affiliation

Sato SB; Department of Biophysics, Division of Biological Science, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan. Electronic address: satou.satoshi.3s@kyoto-u.ac.jp.
Sugiura M; Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Kurihara T; Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.

Biochim Biophys Acta Proteins Proteom ; 1866(5-6): 692-701, 2018.

Article in En | MEDLINE | ID: mdl-29635040

Subject(s)

Docosahexaenoic Acids/pharmacology; HSP27 Heat-Shock Proteins/metabolism; Heat-Shock Response/drug effects; Hot Temperature; Human Umbilical Vein Endothelial Cells/drug effects; Acetylcysteine/pharmacology; Arachidonic Acid/pharmacology; Cells, Cultured; Eicosapentaenoic Acid/pharmacology; HSP27 Heat-Shock Proteins/chemistry; HSP27 Heat-Shock Proteins/genetics; Heat-Shock Proteins; Human Umbilical Vein Endothelial Cells/metabolism; Humans; Molecular Chaperones; Molecular Weight; Protein Conformation; Protein Multimerization; Structure-Activity Relationship; Time Factors

Key words

Heat shock protein 27; Macromolecular crowding; Polyunsaturated fatty acid; Protein hydration; Stress response

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Docosahexaenoic Acids / Heat-Shock Response / HSP27 Heat-Shock Proteins / Human Umbilical Vein Endothelial Cells / Hot Temperature Limits: Humans Language: En Journal: Biochim Biophys Acta Proteins Proteom Year: 2018 Type: Article

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