title: Interaction of 70-kDa heat shock protein with glycosaminoglycans and acidic glycopolymers.
abstract: 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.
authors.affiliation: Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
authors.forename: Yoichiro
authors.initials: Y
authors.lastname: Harada
authors.affiliation: Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
authors.forename: Estelle
authors.initials: E
authors.lastname: Garenáux
authors.affiliation: Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8565, Japan.
authors.forename: Takehiro
authors.initials: T
authors.lastname: Nagatsuka
authors.affiliation: Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8565, Japan.
authors.forename: Hirotaka
authors.initials: H
authors.lastname: Uzawa
authors.affiliation: Division of Molecular Bio-Engineering, Department of Horticulture, Chiba University, Matsudo 271-0092, Japan.
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Nishida
authors.affiliation: Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
authors.forename: Chihiro
authors.initials: C
authors.lastname: Sato
authors.affiliation: Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan. Electronic address: kitajima@agr.nagoya-u.ac.jp.
authors.forename: Ken
authors.initials: K
authors.lastname: Kitajima
mesh_terms: D000818:Animals; D001665:Binding Sites; D002240:Carbohydrate Sequence; D003871:Dermatan Sulfate / Q000378:metabolism; D006017:Glycolipids / Q000737:chemistry / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000737:chemistry / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism; D006497:Heparan Sulfate / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D003871:Dermatan Sulfate; D006017:Glycolipids; D006025:Glycosaminoglycans; D018840:HSP70 Heat-Shock Proteins; D006493:Heparin; D006497:Heparan Sulfate; D010446:Peptide Fragments; C081884:heat-shock protein 70.1
keywords: Complex formation; Dermatan sulfate; Glycosaminoglycan; Heat shock protein 70; Heparan sulfate; Heparin