Alpha-enolase (ENO1)

Alpha-enolase (ENO1) is a highly conserved, multifunctional glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate in glycolysis[2][3]. It is ubiquitously expressed in cells and, in addition to its central metabolic role, acts on the cell surface as a plasminogen receptor, thereby promoting localized proteolysis during tissue remodeling, inflammation, and cancer invasion[1][4]. Alternative translation produces a nuclear form (MBP1), which regulates gene expression by repressing c-myc activity[3]. ENO1 is also a component of exosomes and participates in cytoskeletal reorganization and mitochondrial stability[4]. Differential expression and surface localization of alpha-enolase are associated with a broad range of pathological conditions, including cancer (where it facilitates tumor aggressiveness, metastasis, and chemoresistance), autoimmune disease (where it serves as an autoantigen), neurodegenerative disease, and infection. Due to these diverse roles, ENO1 is being explored as a therapeutic target and biomarker, though targeting is complicated by its essential metabolic functions and potential for inducing autoimmunity[1][2][3][4][5].

Other names

Enolase 12-phospho-D-glycerate hydrolasePlasminogen receptorENO1Tau-crystallinMyc-binding protein-1 (MBP1)

Antibody-mediated inhibition of ENO1 (blockade of plasminogen receptor activity, inhibition of tumor progression)[4]; Immunotherapeutic stimulation (activation of ENO1-specific CD8+ and CD4+ T cell responses in cancer)[4]; Regulation of transcription via MBP1 form (repression of c-myc expression)[3]