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

Cristina Maranto, Salvatore Feo, Giovanni Perconti, Cristina Maranto, Patrizia Rubino, Daniele P. Romancino, Agata Giallongo, Salvatore Feo, Antonella Bongiovanni

Risultato della ricerca: Articlepeer review

8 Citazioni (Scopus)


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.
Lingua originaleEnglish
pagine (da-a)1-12
Numero di pagine12
RivistaScientific Reports
Stato di pubblicazionePublished - 2017

All Science Journal Classification (ASJC) codes

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