English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

During the past ten years much information has been accumulated concerning the interaction of tritilated estrogens with hormone-dependent tissues. Their striking affinity for estradiol, both in vivo'-5 and in vitro,6-9 first suggested that such target tissues as uterus, vagina, and anterior pituitary possess unique components called "estrogen receptors." Strong but reversible association of hormone with receptor, without chemical transformation of the steroid molecule, appears to be a primary step in the uterotrophic process, not affected by such inhibitors of early estrogen response as puromycin or actinomycin D.1 The interaction of estradiol with target tissues involves two distinct phenomena uptake and retention; the latter process, but not the former, becomes saturated in vivo if the hormone administered exceeds the physiological level. 1 Centrifugal fractionation experiments"0-14 demonstrate two sites of estrogen binding in uterine cells. As confirmed by autoradiography,1' 16 most estradiol, both in endometrium and in myometrium, resides in the nuclei, but a certain amount is bound to a macromolecular substance appearing in the supernatant fraction. Toft and Gorski'7 made the important observation that the radioactive estradiol-receptor complex in the supernatant fraction can be characterized by ultracentrifugation in sucrose density gradients where it migrates with a sedimentation coefficient of 9.5S; disruption of the complex by proteases but not by nucleases suggests that the receptor substance is a protein. We have confirmed these findings and have observed further8-20 that a different estradiol-receptor complex, sedimenting at about 5S, cani be extracted from uterine nuclei by cold 0.3 Ml KC1, which solubilizes little uterine DNA.2' Although the 9.5S complex does not appear to be a simple aggregate of the 5S, the two receptor substances show many similar characteristics, discussed in more detail elsewhere.22 An important difference is the ability of the 9.5S complex to form spontaneously on addition of tritiated estradiol to supernatant fraction;'9 20, 23 the 5S complex is not produced by adding estradiol to nuclear extract,24 although it can be formed in the whole homogenate. This paper presents evidence that the 9.5S receptor is extranuclear and involved in estrogen uptake, whereas the nuclear 5S complex, probably responsible for hormone retention and growth initiation, is formed from the 9.5S complex by a process which consumes 9.5S receptor and which is retarded at low temperature. Materials and Methods.-These investigations used estradiol-6, 7-H3 (spec. act. 57.4 c/mmole), KRH buffer (pH 7.3, Krebs-Ringer-Henseleit-glucose, containing in gm/liter: NaCl, 8.0; KCI, 0.20; Na2HPO4 7H20, 1.73; KH2PO4, 0.20; CaC12, 0.10; MgC12, 0.048; and glucose, 1.0), and Tris-EDTA buffer (pH 7.4, 0.01 Al 2-amino-2-hydroxymethyl-1,3-propanediol plus 0.0015 M4 ethylenediaminetetraacetic acid, disodium salt).

A two-step mechanism for the interaction of estradiol with rat uterus.