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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


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Αναφορά Δημιουργού-Μη Εμπορική Χρήση-Όχι Παράγωγα Έργα 3.0 Ηνωμένες Πολιτείες Except where otherwise noted, this item's license is described as Αναφορά Δημιουργού-Μη Εμπορική Χρήση-Όχι Παράγωγα Έργα 3.0 Ηνωμένες Πολιτείες