Ontology highlight
ABSTRACT:
SUBMITTER: Maaroufi Y
PROVIDER: S-EPMC13922 | biostudies-literature | 2000
REPOSITORIES: biostudies-literature
Maaroufi Y Y Lacroix M M Lespagnard L L Journé F F Larsimont D D Leclercq G G
Breast cancer research : BCR 20000906 6
Iodinated oestradiol-labeled oestrogen receptor (ER) isoforms devoid of amino-terminal ABC domains represent about two-thirds of the whole receptor population detected in cytosol samples from human breast cancers. This high frequency could not be ascribed to the expression of truncated mRNAs, or to the proteolysis of the native ER peptide at the time of homogenization or assay, suggesting an intracellular proteolysis. Free amino-terminal and ligand-binding domains maintained together within olig ...[more]