Radiation inactivation of estrogen receptor in intact human breast cancer cells (MCF-7). Lack of energy transfer to the estradiol binding domain.
Whole MCF-7 human breast-cancer cells were irradiated at - 78 degrees C in a calibrated Gammacel 60Co irradiator. Freezing or storing conditions induce neither an alteration of the viability of cells nor a change in estradiol binding activity. Hexosaminidase was used as internal marker, and we measured the radiation inactivation size (RIS) of the estrogen receptor in whole cells. After various cell treatments, the estradiol binding unit always presents a molecular mass of 25 kDa. This value, which corresponds to the size of the defined hormone binding domain of the estrogen receptor, suggests that the energy delivered to the protein by the radiation is efficient to inactivate estradiol binding only when the hit occurs directly in the smaller hormone binding domain.
Toulas
C
C
Laboratoire d'Endocrinologie Expérimentale, CHU Rangueil, Toulouse, France.
Beauregard
G
G
Delassus
F
F
Thauvette
L
L
Potier
M
M
Bayard
F
F
Faye
J C
JC
D001665:Binding Sites / Q000528:radiation effects; D001943:Breast Neoplasms / Q000737:chemistry*; D002470:Cell Survival / Q000528:radiation effects; D004958:Estradiol / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D011839:Radiation, Ionizing; D011960:Receptors, Estrogen / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects*; D013696:Temperature; D014407:Tumor Cells, Cultured; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism
D011960:Receptors, Estrogen; D004958:Estradiol; D001619:beta-N-Acetylhexosaminidases