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 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 lipopoly

SUBMITTER: Perconti G 

PROVIDER: S-EPMC5476664 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature