Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
Autor: | V. V. Vrublevskaya, V. N. Afanasyev, Oleg S. Morenkov, A. V. Snigireva |
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Rok vydání: | 2015 |
Předmět: |
anchoring and binding to plasma membrane
Fibrosarcoma Cell Biology Cellular and Molecular Neuroscience extracellular Hsp90 Cell Movement Heat shock protein Cell Line Tumor medicine Extracellular Humans HSP90 Heat-Shock Proteins human glioblastoma A-172 and fibrosarcoma HT1080 cells Heparinase Membrane Glycoproteins Heparin Cell Membrane Colocalization Cell Biology cell surface-bound Hsp90α Cell biology Cytosol and Hsp90β medicine.anatomical_structure Immunology HT1080 Heparitin Sulfate cell surface HSPGs medicine.drug Protein Binding Research Paper |
Zdroj: | Cell Adhesion & Migration |
ISSN: | 1933-6926 |
Popis: | Extracellular membrane-bound and secreted heat shock protein 90 (Hsp90) is known to be involved in cell motility and invasion. The mechanism of Hsp90 anchoring to the plasma membrane remains obscure. We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90α and Hsp90β, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells. We revealed that Hsp90α and Hsp90β are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin. The results demonstrate that cell surface HSPGs are involved in the binding/anchoring of Hsp90α and Hsp90β to the plasma membrane. |
Databáze: | OpenAIRE |
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