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dc.contributor.authorDidiasova, Miroslava
dc.contributor.authorSchaefer, Liliana
dc.contributor.authorWygrecka, Malgorzata
dc.date.accessioned2022-11-18T09:55:13Z
dc.date.available2020-08-05T09:33:03Z
dc.date.available2022-11-18T09:55:13Z
dc.date.issued2019
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:hebis:26-opus-153756
dc.identifier.urihttps://jlupub.ub.uni-giessen.de//handle/jlupub/9561
dc.identifier.urihttp://dx.doi.org/10.22029/jlupub-8949
dc.description.abstractEnolase is a glycolytic enzyme, which catalyzes the inter-conversion of 2-phosphoglycerate to phosphoenolpyruvate. Altered expression of this enzyme is frequently observed in cancer and accounts for the Warburg effect, an adaptive response of tumor cells to hypoxia. In addition to its catalytic function, ENO-1 exhibits other activities, which strongly depend on its cellular and extracellular localization. For example, the association of ENO-1 with mitochondria membrane was found to be important for the stability of the mitochondrial membrane, and ENO-1 sequestration on the cell surface was crucial for plasmin-mediated pericellular proteolysis. The latter activity of ENO-1 enables many pathogens but also immune and cancer cells to invade the tissue, leading further to infection, inflammation or metastasis formation. The ability of ENO-1 to conduct so many diverse processes is reflected by its contribution to a high number of pathologies, including type 2 diabetes, cardiovascular hypertrophy, fungal and bacterial infections, cancer, systemic lupus erythematosus, hepatic fibrosis, Alzheimer´s disease, rheumatoid arthritis, and systemic sclerosis. These unexpected non-catalytic functions of ENO-1 and their contributions to diseases are the subjects of this review.en
dc.language.isoende_DE
dc.rightsNamensnennung 4.0 International*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectenolase-1en
dc.subjectmultitasking proteinen
dc.subjectglycolysisen
dc.subjectprotein compartmentalizationen
dc.subjectcanceren
dc.subject.ddcddc:610de_DE
dc.titleWhen Place Matters: Shuttling of Enolase-1 Across Cellular Compartmentsen
dc.typearticlede_DE
local.affiliationFB 11 - Medizinde_DE
local.opus.id15375
local.opus.instituteBiochemisches Institutde_DE
local.opus.fachgebietMedizinde_DE
local.source.urihttps://doi.org/10.3389/fcell.2019.00061
local.source.freetextFrontiers in Cell and Developmental Biology 7:61de_DE


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