Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90ß to the cell plasma membrane.
Cell Adh Migr
; 9(6): 460-8, 2015.
Article
en En
| MEDLINE
| ID: mdl-26651243
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 Hsp90ß, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells. We revealed that Hsp90α and Hsp90ß 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 Hsp90ß to the plasma membrane.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas HSP90 de Choque Térmico
/
Fibrosarcoma
/
Heparitina Sulfato
Límite:
Humans
Idioma:
En
Revista:
Cell Adh Migr
Año:
2015
Tipo del documento:
Article
País de afiliación:
Rusia