title: Molecular forms of the estrogen receptor in breast cancer.
abstract: Estrogen receptors (ERs) of which two isoforms have been identified (alpha and beta) are subjected to phosphorylation, glycozylation, ubiquitination and other post-transcriptional conformational changes giving rise to a very high molecular heterogeneity. Partial proteolysis of these receptors, as well as their high tendency to associate within oligomeric structures, reinforces this property. Investigations demonstrated that this heterogeneity is not a biochemical artefact suggesting some biological relevance. Our purpose was to review this topic, especially with regard to ERalpha from breast cancers.
authors.affiliation: Laboratoire J.-C. Heuson de Cancérologie Mammaire 1, Institut Jules Bordet, Service de Médecine Interne, rue héger-Bordet, 1-1000 Brussels, Belgium. lcanmamm@ulb.ac.be
authors.forename: Guy
authors.initials: G
authors.lastname: Leclercq
mesh_terms: D000818:Animals; D004958:Estradiol / Q000378:metabolism; D006801:Humans; D011487:Protein Conformation; D011960:Receptors, Estrogen / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011960:Receptors, Estrogen; D004958:Estradiol