Unique Estrogen-Binding Properties of Rat Pregnancy Plasma

Soloff, Melvyn S.; Creange, John E.; Potts, Gordon O.

doi:10.1210/endo-88-2-427

Cited by 67 publications

(8 citation statements)

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“…In addition to albumin, these plasmas are known to contain aFP, which has high affinity for E 2 (14)(15)(16)(17)(18). Such high affinity sites are demonstrated by the significant slope of E 2 binding to pregnancy plasmas (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…2, 5 and 6). Some workers have used competition studies to show that DES either does not compete with E 2 for binding to aFP at all (14,16,29) or is a weak competitor (15,30,31), while others have employed semiquantitative nonequilibrium methods to examine DES and aFP interaction (17). With TEBG, competition studies have suggested that DES is a weak binder (32,33).…”

Section: Discussionmentioning

confidence: 99%

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Diethylstilbestrol and Estradiol Binding to Serum Albumin and Pregnancy Plasma of Rat and Human*

1979

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The equilibrium binding of diethylstilbestrol (DES) and 17 beta-estradiol (E2) to plasma proteins has been characterized. DES exhibits a 10- to 20-fold greater binding affinity index for bovine serum albumin and rat plasma than E2. As expected, E2 gave high values for binding to plasma from pregnant mice or rats, reflecting the presence of alpha-fetoprotein. DES bound to these samples as it did to bovine albumin and rat plasma. These results suggested that DES ineracts weakly with alpha-fetoprotein. This was verified by Scatchard plots of DES and E2 binding to rat and human pregnancy plasma. High affinity, low capacity binding was demonstrated with E2 but not with DES. The significantly lower binding of DES suggests that increased delivery of DES to the fetus may be at least partially responsible for the transplacental toxicity and carcinogenicity of DES.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Diethylstilbestrol and Estradiol Binding to Serum Albumin and Pregnancy Plasma of Rat and Human*

1979

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“…In addition to albumin, which under physiological conditions does not bind much estrogens, there is, in the human [29] and in the rat [36,41] plasma, an estrogen-binding protein (EBP) which binds estradiol with a high affinity (equilibrium constant Ka = approx. 109 m-1).…”

Section: Transportmentioning

confidence: 99%

Estrogens and Antiestrogens

Geynet¹,

Millet²,

Truong³

et al. 1972

Gynecol Obstet Invest

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This paper contains: A review of the features implicated in estrogen action on uterine cells: metabolism, transport, entry, cytosol receptor, and first effects. (2) New results concerning the interaction of several estrogens and antiestrogens with the receptor. Binding of radioactive estrogens: at equilibrium at 0 °C, K_D (in nM) of estradiol 0.2–0.5, estrone 2.0, and estriol 1.3. Inhibition constant at equilibrium measured by competition with nonradioactive compounds of natural and synthetic steroid and nonsteroidal estrogens, new stilbene derivatives, phytoestrogens, etc. (28 compounds). Kinetic studies. Same dissociation rate constant for estradiol, estrone and estriol and association rate constant greater for estradiol. Formation of the neonuclear steroid receptor complex by estrone and estriol, implicating that estradiol is not unique for promoting the cytosol receptor translocation to the nucleus. (3) A review of possible mechanisms for antiestrogen action.

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“…At high concentration, nafoxidine has an antiestrogenic activity since it is both a partial agonist in vivo on uterine wet weight [11 ] and a complete inhibitor of estradiol binding to its receptor in vitro, as shown in this paper. Several hypotheses can account for the difference in estrogenic action in vivo between estradiol and nafoxidine: they could be carried differently in blood since estradiol, but not nafoxidine, binds to specific plasma protein [12]. Another possibility is that the U.…”

Section: Total Inhibitionmentioning

confidence: 99%