Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

dc.contributor.author	El Hamidieh, Avraam	en
dc.contributor.author	Γραμματικάκης, Νικόλας	el
dc.contributor.author	Πατσαβούδη, Ευαγγελία	el
dc.date.accessioned	2015-06-05T17:54:23Z
dc.date.available	2015-06-05T17:54:23Z
dc.date.issued	2015-06-05
dc.identifier.uri	http://hdl.handle.net/11400/15176
dc.rights	Αναφορά Δημιουργού-Μη Εμπορική Χρήση-Όχι Παράγωγα Έργα 3.0 Ηνωμένες Πολιτείες	*
dc.rights.uri	http://creativecommons.org/licenses/by-nc-nd/3.0/us/	*
dc.source	http://www.plosone.org/	en
dc.subject	Immunoprecipitation
dc.subject	Immunostaining
dc.subject	Breast cancer
dc.subject	Cell disruption
dc.subject	Chaperone proteins
dc.subject	Cell mobility
dc.subject	Small interfering RNA
dc.subject	Protein kinases
dc.subject	Ανοσοκατακρήμνιση
dc.subject	Ανοσοβαφή
dc.subject	Καρκίνος μαστού
dc.subject	Διάσπαση των κυττάρων
dc.subject	Πρωτεϊνες συνοδοί
dc.subject	Κινητικότητα κυττάρου
dc.subject	Μικρά παρεμβαλλόμενα RNA
dc.subject	Πρωτεϊνικές κινάσες
dc.title	Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion	en
heal.type	journalArticle
heal.classification	Medicine
heal.classification	Oncology
heal.classification	Ιατρική
heal.classification	Ογκολογία
heal.classificationURI	http://id.loc.gov/authorities/subjects/sh00006614
heal.classificationURI	http://id.loc.gov/authorities/subjects/sh85094724
heal.classificationURI	N/A-Ιατρική
heal.classificationURI	N/A-Ογκολογία
heal.keywordURI	http://id.loc.gov/authorities/subjects/sh2003008503
heal.identifier.secondary	DOI: 10.1371/journal.pone.0042722
heal.language	en
heal.access	campus
heal.recordProvider	Σχολή Τεχνολογικών Εφαρμογών. Τμήμα Μηχανικών Βιοϊατρικής Τεχνολογίας Τ.Ε.	el
heal.publicationDate	2012-08-17
heal.bibliographicCitation	Hamidieh, A., Grammatikakis, N. and Patsavoudi, E. (2012) Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion. "PLOS One", 7 (8). Available from: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0042722 [Accessed: 05/06/2015].	en
heal.abstract	Cdc37 is a 50 kDa molecular chaperone which targets intrinsically unstable protein kinases to the molecular chaperone HSP90. It is also an over-expressed oncoprotein that mediates carcinogenesis and maintenance of the malignant phenotype by stabilizing the compromised structures of mutant and/or over-expressed oncogenic kinases. Here we report that Cdc37 is not restricted intracellularly but instead it is also present on the surface of MDA-MB-453 and MDA-MB-231 human breast cancer cells, where it is shown to participate in cancer cell motility processes. Furthermore, we demonstrate using an anti-Cdc37 cell impermeable antibody, that similarly to its intracellular counterpart, this surface pool of Cdc37 specifically interacts with HSP90 as well as the kinase receptors HER2 and EGFR on the cell surface, probably acting as a co-factor in HSP90's extracellular chaperoning activities. Finally, we show that functional inhibition of surface HSP90 using mAb 4C5, a cell impermeable monoclonal antibody against this protein, leads not only to disruption of the Cdc37/HSP90 complex but also to inhibition of the Cdc37/ErbB receptors complexes. These results support an essential role for surface Cdc37 in concert with HSP90 on the cell surface during cancer cell invasion processes and strengthen the therapeutic potential of mAb 4C5 for the treatment of cancer.	en
heal.journalName	PLOS One	en
heal.journalType	peer-reviewed
heal.fullTextAvailability	true