<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(1)</volume><submitter>Perconti G</submitter><pubmed_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</pubmed_abstract><journal>Scientific reports</journal><pagination>3841</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5476664</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface.</pubmed_title><pmcid>PMC5476664</pmcid><pubmed_authors>Perconti G</pubmed_authors><pubmed_authors>Maranto C</pubmed_authors><pubmed_authors>Romancino DP</pubmed_authors><pubmed_authors>Rubino P</pubmed_authors><pubmed_authors>Giallongo A</pubmed_authors><pubmed_authors>Bongiovanni A</pubmed_authors><pubmed_authors>Feo S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface.</name><description>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</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jun</publication><modification>2025-04-25T19:22:16.1Z</modification><creation>2019-03-27T02:47:58Z</creation></dates><accession>S-EPMC5476664</accession><cross_references><pubmed>28630480</pubmed><doi>10.1038/s41598-017-04185-8</doi></cross_references></HashMap>