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Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90? and Hsp90? to the cell plasma membrane.

ABSTRACT: 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, Hsp90? and Hsp90?, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells. We revealed that Hsp90? and Hsp90? 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 Hsp90? and Hsp90? to the plasma membrane.

SUBMITTER: Snigireva AV

PROVIDER: S-EPMC4955955 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane.

Snigireva Anastasiya V AV Vrublevskaya Veronika V VV Afanasyev Vladimir N VN Morenkov Oleg S OS

Cell adhesion & migration 20150101 6

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 ...[more]

PMID: 26651243

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