We are analyzing https://link.springer.com/article/10.1007/bf01806018.

Title:
Antiestrogen action in breast cancer cells: Modulation of proliferation and protein synthesis, and interaction with estrogen receptors and additional antiestrogen binding sites | Breast Cancer Research and Treatment
Description:
Antiestrogens have proven to be effective in controlling the growth of hormone-responsive breast cancers. At the concentrations of antiestrogens achieved in the blood of breast cancer patients taking antiestrogens (up to 2 × 10−6 M), antiestrogens selectively inhibit the proliferation of estrogen receptor-containing breast cancer cells, and this inhibition is reversible by estradiol. Antiestrogens also inhibit estrogen-stimulation of several specific protein synthetic activities in breast cancer cells, including increases in plasminogen activator activity, progesterone receptor levels and production of several secreted glycoproteins and intracellular proteins. Antiestrogens bind with high affinity to the estrogen receptor and to additional microsomal binding sites to which estrogens do not bind. These latter sites, called antiestrogen binding sites (AEBS), are present in equal concentrations in estrogen receptor-positive and -negative breast cancer cells and are present in a wide variety of tissues, with highest concentrations being found in the liver. The antiestrogenic and growth suppressive potencies of a variety of antiestrogens correlate best with their affinity for estrogen receptor and not with affinity for AEBS. Antiestrogens undergo bioactivation and metabolismin vivo and hydroxylated forms of the antiestrogen have markedly enhanced affinities for the estrogen receptor. Detailed studies with high affinity radiolabelled antiestrogens indicate that antiestrogens induce important conformational changes in receptor that are reflected in the enhanced maintenance of a 5 S form of the estrogen receptor complex; reduced interaction with DNA; and altered activation and dissociation kinetics of the antiestrogen-estrogen receptor complex. These conformational changes effected by antiestrogens likely result in different interactions with chromatin, causing altered cell proliferation and protein synthesis. Analyses of the rates of synthesis and turnover of the estrogen receptor through pulse-chase experiments utilizing the covalently attaching antiestrogen, tamoxifen aziridine, and studies employing dense amino acid labeling of estrogen receptor reveal that the antiestrogen-occupied receptor is degraded at a rate (t 1/2 = 4 h) similar to that of the control unoccupied receptor. Hence, antiestrogens do not prevent estrogen receptor synthesis and they do not either accelerate or block estrogen receptor degradation. Our findings raise serious doubts about the role of the AEBS in mediating directly the growth suppressive actions of antiestrogens, and suggest that interaction with the estrogen receptor is most likely the mechanism underlying the growth-inhibitory effects of antiestrogens. At present, the role of the AEBS in the actions of antiestrogens or in possible antiestrogen metabolism remains unclear.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Health & Fitness
Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

google, scholar, cancer, pubmed, estrogen, breast, receptor, antiestrogen, katzenellenbogen, antiestrogens, cells, binding, human, res, mcf, sites, tamoxifen, chem, affinity, article, cell, biol, endocrinology, synthesis, miller, biochem, high, sutherland, research, action, interaction, receptors, mcguire, protein, robertson, privacy, cookies, content, treatment, mullick, growth, specific, plasminogen, liver, effects, access, lippman, eckert, rat, biophys,

Topics {✒️}

n-pyrro-lidinyl-ethoxy-phenyl]-α′-nitrostilbene α-[4-pyrrolidinoethoxy]phenyl-4-hydroxy-α′-nitro-stilbene tritium-labeled 4-hydroxy-α-[p hormone-responsive breast cancers triphenylethylene anti-estrogen-binding sites month download article/chapter blonk-van der wijst pulse-chase experiments utilizing biolog-ically-important metabolite estrogen recep-tor-positive plasminogen activator-inducing activities antiestrogen-estrogen receptor complex long-term tissue culture human breast cancer antiestrogen-estrogen receptor complexes antiestrogen binding sites breast cancer cells microsomal binding sites antiestrogen pharmacology monsma fj jr high affinity antiestrogen breast cancer advances uterine estrogen receptors advanced breast cancer privacy choices/manage cookies antiestrogen-binding protein intracellular proteins mcf-7 cell cytosol hormonal control steroid receptor sites growth suppressive potencies full article pdf tritium-labeled u23 estrogen receptor-dna interaction estrogen receptor-positive estrogen receptor complex antiestrogen-occupied receptor covalently attaching antiestrogen covalently-attaching antiestrogen salt-resistant form rough microsomal membranes estrogen receptor complexes tritium-labeled form plasminogen activator secretion binding sites density shift experiments growth suppressive actions activated nuclear receptor nuclear estrogen receptor margaret ann miller

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Antiestrogen action in breast cancer cells: Modulation of proliferation and protein synthesis, and interaction with estrogen receptors and additional antiestrogen binding sites
         description:Antiestrogens have proven to be effective in controlling the growth of hormone-responsive breast cancers. At the concentrations of antiestrogens achieved in the blood of breast cancer patients taking antiestrogens (up to 2 × 10−6 M), antiestrogens selectively inhibit the proliferation of estrogen receptor-containing breast cancer cells, and this inhibition is reversible by estradiol. Antiestrogens also inhibit estrogen-stimulation of several specific protein synthetic activities in breast cancer cells, including increases in plasminogen activator activity, progesterone receptor levels and production of several secreted glycoproteins and intracellular proteins. Antiestrogens bind with high affinity to the estrogen receptor and to additional microsomal binding sites to which estrogens do not bind. These latter sites, called antiestrogen binding sites (AEBS), are present in equal concentrations in estrogen receptor-positive and -negative breast cancer cells and are present in a wide variety of tissues, with highest concentrations being found in the liver. The antiestrogenic and growth suppressive potencies of a variety of antiestrogens correlate best with their affinity for estrogen receptor and not with affinity for AEBS. Antiestrogens undergo bioactivation and metabolismin vivo and hydroxylated forms of the antiestrogen have markedly enhanced affinities for the estrogen receptor. Detailed studies with high affinity radiolabelled antiestrogens indicate that antiestrogens induce important conformational changes in receptor that are reflected in the enhanced maintenance of a 5 S form of the estrogen receptor complex; reduced interaction with DNA; and altered activation and dissociation kinetics of the antiestrogen-estrogen receptor complex. These conformational changes effected by antiestrogens likely result in different interactions with chromatin, causing altered cell proliferation and protein synthesis. Analyses of the rates of synthesis and turnover of the estrogen receptor through pulse-chase experiments utilizing the covalently attaching antiestrogen, tamoxifen aziridine, and studies employing dense amino acid labeling of estrogen receptor reveal that the antiestrogen-occupied receptor is degraded at a rate (t 1/2 = 4 h) similar to that of the control unoccupied receptor. Hence, antiestrogens do not prevent estrogen receptor synthesis and they do not either accelerate or block estrogen receptor degradation. Our findings raise serious doubts about the role of the AEBS in mediating directly the growth suppressive actions of antiestrogens, and suggest that interaction with the estrogen receptor is most likely the mechanism underlying the growth-inhibitory effects of antiestrogens. At present, the role of the AEBS in the actions of antiestrogens or in possible antiestrogen metabolism remains unclear.
         datePublished:
         dateModified:
         pageStart:231
         pageEnd:243
         sameAs:https://doi.org/10.1007/BF01806018
         keywords:
            antiestrogens
            antiestrogen binding sites
            breast cancer
            estrogen receptors
            growth inhibition
            mechanism of antiestrogen action
            tamoxifen
            Oncology
         image:
         isPartOf:
            name:Breast Cancer Research and Treatment
            issn:
               1573-7217
               0167-6806
            volumeNumber:5
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Martinus Nijhoff/Dr. W. Junk Publishers
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Benita S. Katzenellenbogen
               affiliation:
                     name:University of Illinois College of Medicine at Urbana-Champaign
                     address:
                        name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Margaret Ann Miller
               affiliation:
                     name:University of Illinois College of Medicine at Urbana-Champaign
                     address:
                        name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Alaka Mullick
               affiliation:
                     name:University of Illinois College of Medicine at Urbana-Champaign
                     address:
                        name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Yhun Yhong Sheen
               affiliation:
                     name:University of Illinois College of Medicine at Urbana-Champaign
                     address:
                        name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Antiestrogen action in breast cancer cells: Modulation of proliferation and protein synthesis, and interaction with estrogen receptors and additional antiestrogen binding sites
      description:Antiestrogens have proven to be effective in controlling the growth of hormone-responsive breast cancers. At the concentrations of antiestrogens achieved in the blood of breast cancer patients taking antiestrogens (up to 2 × 10−6 M), antiestrogens selectively inhibit the proliferation of estrogen receptor-containing breast cancer cells, and this inhibition is reversible by estradiol. Antiestrogens also inhibit estrogen-stimulation of several specific protein synthetic activities in breast cancer cells, including increases in plasminogen activator activity, progesterone receptor levels and production of several secreted glycoproteins and intracellular proteins. Antiestrogens bind with high affinity to the estrogen receptor and to additional microsomal binding sites to which estrogens do not bind. These latter sites, called antiestrogen binding sites (AEBS), are present in equal concentrations in estrogen receptor-positive and -negative breast cancer cells and are present in a wide variety of tissues, with highest concentrations being found in the liver. The antiestrogenic and growth suppressive potencies of a variety of antiestrogens correlate best with their affinity for estrogen receptor and not with affinity for AEBS. Antiestrogens undergo bioactivation and metabolismin vivo and hydroxylated forms of the antiestrogen have markedly enhanced affinities for the estrogen receptor. Detailed studies with high affinity radiolabelled antiestrogens indicate that antiestrogens induce important conformational changes in receptor that are reflected in the enhanced maintenance of a 5 S form of the estrogen receptor complex; reduced interaction with DNA; and altered activation and dissociation kinetics of the antiestrogen-estrogen receptor complex. These conformational changes effected by antiestrogens likely result in different interactions with chromatin, causing altered cell proliferation and protein synthesis. Analyses of the rates of synthesis and turnover of the estrogen receptor through pulse-chase experiments utilizing the covalently attaching antiestrogen, tamoxifen aziridine, and studies employing dense amino acid labeling of estrogen receptor reveal that the antiestrogen-occupied receptor is degraded at a rate (t 1/2 = 4 h) similar to that of the control unoccupied receptor. Hence, antiestrogens do not prevent estrogen receptor synthesis and they do not either accelerate or block estrogen receptor degradation. Our findings raise serious doubts about the role of the AEBS in mediating directly the growth suppressive actions of antiestrogens, and suggest that interaction with the estrogen receptor is most likely the mechanism underlying the growth-inhibitory effects of antiestrogens. At present, the role of the AEBS in the actions of antiestrogens or in possible antiestrogen metabolism remains unclear.
      datePublished:
      dateModified:
      pageStart:231
      pageEnd:243
      sameAs:https://doi.org/10.1007/BF01806018
      keywords:
         antiestrogens
         antiestrogen binding sites
         breast cancer
         estrogen receptors
         growth inhibition
         mechanism of antiestrogen action
         tamoxifen
         Oncology
      image:
      isPartOf:
         name:Breast Cancer Research and Treatment
         issn:
            1573-7217
            0167-6806
         volumeNumber:5
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Martinus Nijhoff/Dr. W. Junk Publishers
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Benita S. Katzenellenbogen
            affiliation:
                  name:University of Illinois College of Medicine at Urbana-Champaign
                  address:
                     name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Margaret Ann Miller
            affiliation:
                  name:University of Illinois College of Medicine at Urbana-Champaign
                  address:
                     name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Alaka Mullick
            affiliation:
                  name:University of Illinois College of Medicine at Urbana-Champaign
                  address:
                     name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Yhun Yhong Sheen
            affiliation:
                  name:University of Illinois College of Medicine at Urbana-Champaign
                  address:
                     name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Breast Cancer Research and Treatment
      issn:
         1573-7217
         0167-6806
      volumeNumber:5
Organization:
      name:Martinus Nijhoff/Dr. W. Junk Publishers
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Illinois College of Medicine at Urbana-Champaign
      address:
         name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
         type:PostalAddress
      name:University of Illinois College of Medicine at Urbana-Champaign
      address:
         name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
         type:PostalAddress
      name:University of Illinois College of Medicine at Urbana-Champaign
      address:
         name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
         type:PostalAddress
      name:University of Illinois College of Medicine at Urbana-Champaign
      address:
         name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Benita S. Katzenellenbogen
      affiliation:
            name:University of Illinois College of Medicine at Urbana-Champaign
            address:
               name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
               type:PostalAddress
            type:Organization
      name:Margaret Ann Miller
      affiliation:
            name:University of Illinois College of Medicine at Urbana-Champaign
            address:
               name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
               type:PostalAddress
            type:Organization
      name:Alaka Mullick
      affiliation:
            name:University of Illinois College of Medicine at Urbana-Champaign
            address:
               name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
               type:PostalAddress
            type:Organization
      name:Yhun Yhong Sheen
      affiliation:
            name:University of Illinois College of Medicine at Urbana-Champaign
            address:
               name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
      name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
      name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
      name:Department of Physiology and Biophysics, 524 Burill Hall, University of Illinois College of Medicine at Urbana-Champaign, Urbana, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(132)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.29s.

LINK . SPRINGER . COM {}