Interaction of 70-kDa heat shock protein with glycosaminoglycans and acidic glycopolymers |
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Authors: | Yoichiro Harada,Estelle Garená ux,Takehiro Nagatsuka,Hirotaka Uzawa,Yoshihiro Nishida,Chihiro Sato,Ken Kitajima |
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Affiliation: | 1. Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan;2. Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8565, Japan;3. Division of Molecular Bio-Engineering, Department of Horticulture, Chiba University, Matsudo 271-0092, Japan |
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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. |
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Keywords: | BSA, bovine serum albumin CBB, Coomassie Brilliant Blue GAG, glycosaminoglycan Hsp70, 70-kDa heat-shock protein 70 Hsp-C, the peptide-binding domain of Hsp70 Hsp-FL, full-length of Hsp70 Hsp-N, the ATPase domain of Hsp70 Lac, lactose LacNAc, N-acetyllactosamine PAGE, polyacrylamide gel electrophoresis PAA, polyacrylamide pNp, para-nitrophenyl PVDF, polyvinylidene difluoride SBP, sperm-binding protein |
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