Hsp90 Binds Directly to Fibronectin (FN) and Inhibition Reduces the Extracellular Fibronectin Matrix in Breast Cancer Cells

Heat shock protein 90 (Hsp90) has been identified in the extracellular space and has been shown to chaperone a finite number of extracellular proteins involved in cell migration and invasion. We used chemical cross-linking and immunoprecipitation followed by tandem mass spectrometry (MS/MS) to isola...

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Bibliographic Details
Published in:	PloS one Vol. 9; no. 1; p. e86842
Main Authors:	Hunter, Morgan C., O’Hagan, Kyle L., Kenyon, Amy, Dhanani, Karim C. H., Prinsloo, Earl, Edkins, Adrienne L.
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 22.01.2014 Public Library of Science (PLoS)
Subjects:	Bacterial Proteins Binding Binding sites Biochemistry Biology Biotechnology Breast cancer Breast Neoplasms - metabolism Cancer Cancer cells Cancer metastasis Cell adhesion & migration Cell Line, Tumor Cell migration Chromatography, Affinity Collagen Confocal microscopy Crosslinking Electrophoresis, Polyacrylamide Gel Embryogenesis Embryonic growth stage Endoplasmic reticulum Enzyme-Linked Immunosorbent Assay Epidermal growth factor Extracellular Matrix - metabolism Female Fibronectin Fibronectins Fibronectins - metabolism Fluorescence Heat shock proteins HSP90 Heat-Shock Proteins - metabolism Hsp90 protein Humans Immunoprecipitation Inhibition Internalization Kinases LAMP-1 protein Low density lipoprotein receptors Mass spectrometry Mass spectroscopy Matrix protein MCF-7 Cells Medicine Metastases Metastasis Microscopy Microscopy, Confocal Novobiocin Penicillin Proteins RNA Interference Sepharose - analogs & derivatives Spectroscopy Stability Surface Plasmon Resonance Tandem Mass Spectrometry Tumor cell lines Wound healing South Africa
ISSN:	1932-6203, 1932-6203
Online Access:	Get full text
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