Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
| Autor: | Daniele P. Romancino, Antonella Bongiovanni, Patrizia Rubino, Cristina Maranto, Giovanni Perconti, Agata Giallongo, Salvatore Feo |
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| Přispěvatelé: | Perconti, G., Maranto, C., Romancino, D., Rubino, P., Feo, S., Bongiovanni, A., Giallongo, A. |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Lipopolysaccharides
0301 basic medicine Alpha-enolase Science Cell Plasma protein binding Article 03 medical and health sciences Cell Movement Epidermal growth factor Cell Line Tumor medicine Humans HSP70 Heat-Shock Proteins Regulation of gene expression Multidisciplinary biology Cell Membrane 3. Good health Cell biology Gene Expression Regulation Neoplastic Settore BIO/18 - Genetica 030104 developmental biology medicine.anatomical_structure Phosphopyruvate Hydratase Chaperone (protein) Cancer cell biology.protein Medicine Enolase Hsp70 protein cell surface cancer biology Intracellular Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017) |
| Popis: | Cell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to the motility and invasiveness of cancer cells through the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation. Although a few recent records indicate the involvement of protein partners in the localization of alpha-enolase to the plasma membrane, the cellular mechanisms underlying surface exposure remain largely elusive. Searching for novel interactors and signalling pathways, we used low-metastatic breast cancer cells, a doxorubicin-resistant counterpart and a non-tumourigenic mammary epithelial cell line. Here, we demonstrate by a combination of experimental approaches that epidermal growth factor (EGF) exposure, like lipopolysaccharide (LPS) exposure, promotes the surface expression of alpha-enolase. We also establish Heat shock protein 70 (Hsp70), a multifunctional chaperone distributed in intracellular, plasma membrane and extracellular compartments, as a novel alpha-enolase interactor and demonstrate a functional involvement of Hsp70 in the surface localization of alpha-enolase. Our results contribute to shedding light on the control of surface expression of alpha-enolase in non-tumourigenic and cancer cells and suggest novel targets to counteract the metastatic potential of tumours. |
| Databáze: | OpenAIRE |
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