Studies on the Specific Estradiol Binding Site on Rat Uterine Membranes / 대한내분비학회지
Journal of Korean Society of Endocrinology
;
: 510-516, 1996.
Article
in Korean
| WPRIM
| ID: wpr-765577
ABSTRACT
Backgroand In our previous study, it was demonstrated that estradiol-dependent prostaglandin synthesis may be mediated by cAMP elevation during the process of iplantation in rats. The present study was undertaken to investigate if estradio1, a hydrophobic molecule could interact with uterine plasma membrane, thereby influencing adenylate cyclase and cAMP. Methods:
The specific binding of [3H]estradiol to plasma membrane prepared from rat uterus has been identified and characterized.Results:
The association of [3H]estradiol to plasma membrane preparations reached equilibrium at 24 hrs. [3H]estradiol binding was directly proportional to the concentration of plasma membrane preparations and its binding was temperature-sensitive. This binding was saturable, reversible and binding site was one type with high affinity(Kd=0.16+0.03 nM) and high binding capacity(Bmax= 2.03 + 0.38pmol/mg protein). The dissociation constant was estimated as 1.6*10(-10)M. In a competition assay, binding was specific for estrogenic compounds. When 100% specific binding was detennined in the presence of 3*10(-6) M diethylstilbestrol, 17B-estradiol and tamoxifen displaced specific binding by 115% and 23%, respectively. Neither progesterone nor cortisol at 500-fold excess displaced the specific binding.Conclusion:
These data suggest the presence of specific binding sites on the plasma membrane for estradiol in the rat uterus.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Progesterone
/
Tamoxifen
/
Uterus
/
Binding Sites
/
Hydrocortisone
/
Signal Transduction
/
Cell Membrane
/
Adenylyl Cyclases
/
Diethylstilbestrol
/
Estradiol
Limits:
Animals
Language:
Korean
Journal:
Journal of Korean Society of Endocrinology
Year:
1996
Type:
Article
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