Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface

Abstract 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 r...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Giovanni Perconti, Cristina Maranto, Daniele P. Romancino, Patrizia Rubino, Salvatore Feo, Antonella Bongiovanni, Agata Giallongo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0a6d5641a63d4e43bbe57e984a44c978
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:0a6d5641a63d4e43bbe57e984a44c978
record_format	dspace
spelling	oai:doaj.org-article:0a6d5641a63d4e43bbe57e984a44c9782021-12-02T12:30:36ZPro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface10.1038/s41598-017-04185-82045-2322https://doaj.org/article/0a6d5641a63d4e43bbe57e984a44c9782017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04185-8https://doaj.org/toc/2045-2322Abstract 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.Giovanni PercontiCristina MarantoDaniele P. RomancinoPatrizia RubinoSalvatore FeoAntonella BongiovanniAgata GiallongoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Giovanni Perconti Cristina Maranto Daniele P. Romancino Patrizia Rubino Salvatore Feo Antonella Bongiovanni Agata Giallongo Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
description	Abstract 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.
format	article
author	Giovanni Perconti Cristina Maranto Daniele P. Romancino Patrizia Rubino Salvatore Feo Antonella Bongiovanni Agata Giallongo
author_facet	Giovanni Perconti Cristina Maranto Daniele P. Romancino Patrizia Rubino Salvatore Feo Antonella Bongiovanni Agata Giallongo
author_sort	Giovanni Perconti
title	Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
title_short	Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
title_full	Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
title_fullStr	Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
title_full_unstemmed	Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
title_sort	pro-invasive stimuli and the interacting protein hsp70 favour the route of alpha-enolase to the cell surface
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/0a6d5641a63d4e43bbe57e984a44c978
work_keys_str_mv	AT giovanniperconti proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface AT cristinamaranto proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface AT danielepromancino proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface AT patriziarubino proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface AT salvatorefeo proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface AT antonellabongiovanni proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface AT agatagiallongo proinvasivestimuliandtheinteractingproteinhsp70favourtherouteofalphaenolasetothecellsurface
_version_	1718394317883572224

Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface

Ejemplares similares