Interaction of 70-kDa heat shock protein with glycosaminoglycans and acidic glycopolymers

• Published in: Biochemical and biophysical research communications Vol. 453; no. 2; pp. 229 - 234
• Main Authors: Harada, Yoichiro, Garenáux, Estelle, Nagatsuka, Takehiro, Uzawa, Hirotaka, Nishida, Yoshihiro, Sato, Chihiro, Kitajima, Ken
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.10.2014
• Subjects: Animals; Binding Sites; Carbohydrate Sequence; Complex formation; Dermatan sulfate; Dermatan Sulfate - metabolism; Glycolipids - chemistry; Glycolipids - metabolism; Glycosaminoglycan; Glycosaminoglycans - chemistry; Glycosaminoglycans - metabolism; Heat shock protein 70; Heparan sulfate; Heparin; Heparin - metabolism; Heparitin Sulfate - metabolism; HSP70 Heat-Shock Proteins - chemistry; HSP70 Heat-Shock Proteins - metabolism; Mice; Molecular Sequence Data; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Protein Binding; Protein Structure, Tertiary; SBP; Heparan sulfate; CBB; Complex formation; Hsp-N; PAGE; Hsp-FL; GAG; PVDF; Lac; BSA; PAA; Hsp70; pNp; Dermatan sulfate; Hsp-C; LacNAc; Heat shock protein 70; Glycosaminoglycan; Heparin
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2014.05.137

•Heat shock protein 70, Hsp70, is characterized for interaction with acidic glycans.•Hsp70 directly interacts with acidic glycans with sulfated Gal and GlcNAc residues.•Hsp70 forms a large complex with a particular group of GAGs including heparin.•ATPase domain of Hsp70 is responsible for the interaction with acidic glycans.•Peptide-binding domain of Hsp70 stabilizes the complex with the particular GAGs. Interaction of Hsp70 with natural and artificial acidic glycans is demonstrated based on the native PAGE analysis. Hsp70 interacts with acidic glycopolymers that contain clustered sulfated and di-sialylated glycan moieties on a polyacrylamide backbone, but not with neutral or mono-sialylated glycopolymers. Hsp70 also interacts and forms a large complex with heparin, heparan sulfate, and dermatan sulfate that commonly contain 2-O-sulfated iduronic acid residues, but not with other types of glycosaminoglycans (GAGs). Hsp70 consists of the N-terminal ATPase domain and the C-terminal peptide-binding domain. The interaction analyses using the recombinant N- and C-terminal half domains show that the ATPase domain mediates the direct interaction with acidic glycans, while the peptide-binding domain stabilizes the large complexes with particular GAGs. To our knowledge, this is the first demonstration of direct binding of Hsp70 to the particular GAGs. This property may be involved in the physiological functions of Hsp70 at the plasma membrane and extracellular environments.