Breast Cancer Research

official impact factor 5.79

Open Access Research article

Estrogen receptor of primary breast cancers: evidence for intracellular proteolysis

Younes Maaroufi, Marc Lacroix, Laurence Lespagnard, Fabrice Journé, Denis Larsimont and Guy Leclercq*

Author Affiliations

Institut Jules Bordet, Brussels, Belgium

For all author emails, please log on.

Breast Cancer Res 2000, 2:444-454 doi:10.1186/bcr92

Published: 6 September 2000

Abstract

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 oligomeric structure(s); increase of ionic strength separated them. The amino-terminal region was consistently detected in the cell nucleus by specific immunohistochemistry leading to the concept of a potential intranuclear association between ER cleavage products and/or other regulatory proteins.

Keywords:
estrogen receptor domains; hydroxylapatite; immunohistochemistry; primary breast cancer