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

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 chlor...

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Main Authors:	Snigireva, Anastasiya V, Vrublevskaya, Veronika V, Afanasyev, Vladimir N, Morenkov, Oleg S
Format:	Online
Language:	English
Published:	Taylor & Francis 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4955955/

id	pubmed-4955955
recordtype	oai_dc
spelling	pubmed-49559552016-08-05 Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane Snigireva, Anastasiya V Vrublevskaya, Veronika V Afanasyev, Vladimir N Morenkov, Oleg S Research Paper 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. Taylor & Francis 2015-12-10 /pmc/articles/PMC4955955/ /pubmed/26651243 http://dx.doi.org/10.1080/19336918.2015.1103421 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Snigireva, Anastasiya V Vrublevskaya, Veronika V Afanasyev, Vladimir N Morenkov, Oleg S
spellingShingle	Snigireva, Anastasiya V Vrublevskaya, Veronika V Afanasyev, Vladimir N Morenkov, Oleg S Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
author_facet	Snigireva, Anastasiya V Vrublevskaya, Veronika V Afanasyev, Vladimir N Morenkov, Oleg S
author_sort	Snigireva, Anastasiya V
title	Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
title_short	Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
title_full	Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
title_fullStr	Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
title_full_unstemmed	Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane
title_sort	cell surface heparan sulfate proteoglycans are involved in the binding of hsp90α and hsp90β to the cell plasma membrane
description	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.
publisher	Taylor & Francis
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4955955/
_version_	1613612918008446976

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

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