Molecular forms of the estrogen receptor in breast cancer.
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.
Leclercq
Guy
G
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
D000818:Animals; D004958:Estradiol / Q000378:metabolism; D006801:Humans; D011487:Protein Conformation; D011960:Receptors, Estrogen / Q000737:chemistry / Q000378:metabolism*
D011960:Receptors, Estrogen; D004958:Estradiol