Modulation of the estrogen receptor structure, evidence of a heterogeneity

Journal Article · Mon Jan 01 00:00:00 EST 1990 · Journal of Receptor Research; (USA)

DOI:https://doi.org/10.3109/10799899009064654· OSTI ID:5988321

Toulas, C; Guilbaud, N; Delassus, F; Bayard, F; Faye, J C ^[1]

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1. INSERM U168, CHU Rangueil, Toulouse (France)

In order to analyse the molecular weight polymorphism of the estrogen receptor (ER) in MCF-7 cells, we have developed a procedure which allowed in situ linkage of ER by (3H) tamoxifen aziridine and provided labelled proteins in conditions which minimized protease activities. After labelling, cell lysis was performed in SDS buffer containing various concentrations of mercaptoethanol. Proteins extracted with phenolic solution and precipitated by cold acetone were analysed by SDS PAGE. It appears that beside the form of 67 kDa already described, binding entities of tamoxifen aziridine were also present at a molecular mass of 110 kDa and 45 kDa. On the other hand, investigations on the effect of 12-0-Tetradecanoyl Phorbol 13-Acetate (TPA) showed that TPA induces a decrease of the 67 kDa entity.

• OSTI ID: 5988321
• Journal Information: Journal of Receptor Research; (USA), Vol. 10:1-2; ISSN 0197-5110
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ESTROGENS
RECEPTORS
PHORBOL ESTERS
BIOLOGICAL EFFECTS
MOLECULAR STRUCTURE
ELECTROPHORESIS
ENZYME ACTIVITY
MOLECULAR WEIGHT
PEPTIDE HYDROLASES
TRACER TECHNIQUES
TRITIUM COMPOUNDS
TUMOR CELLS
ANIMAL CELLS
CARCINOGENS
ENZYMES
ESTERS
HORMONES
HYDROGEN COMPOUNDS
HYDROLASES
ISOTOPE APPLICATIONS
MEMBRANE PROTEINS
ORGANIC COMPOUNDS
PROTEINS
STEROID HORMONES
550201* - Biochemistry- Tracer Techniques
560300 - Chemicals Metabolism & Toxicology