Biol Reprod Lalor Postdoctoral Fellowships -- Application Deadline January 15, 2009
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moats, R. K.
Right arrow Articles by Ramirez, V. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moats, R. K., 2nd
Right arrow Articles by Ramirez, V. D.
Agricola
Right arrow Articles by Moats, R. K.
Right arrow Articles by Ramirez, V. D.

Biology of Reproduction, Vol 58, 531-538, Copyright © 1998 by Society for the Study of Reproduction

ARTICLES

Rapid uptake and binding of estradiol-17beta-6-(O- carboxymethyl)oxime:125I-labeled BSA by female rat liver

RK Moats 2nd and VD Ramirez
Department of Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, Urbana 61801, USA.

To investigate potential membrane-mediated responses to estrogen, a membrane-impermeant, radioiodinated, steroid-BSA conjugate--estradiol- 17beta-6-(O-carboxymethyl)oxime:125I-labeled BSA (17beta-E-6-125I-BSA)-- or related steroid conjugates, or 125I-BSA was injected into female Sprague-Dawley rats, and tissues were collected at varying times postinjection. The liver, adrenal, and spleen displayed the most prominent uptake of 17beta-E-6-125I-BSA, reaching a maximum of 43 times blood levels in sonicated liver samples at 5 min postinjection, but no uptake of 125I-BSA. Isolation of liver membranes by differential centrifugation showed that over 50% of recovered radioactivity was in association with microsomes and plasmalemma (P3 fraction) at 30 sec postinjection. By 60 min postinjection, over 75% of recovered radioactivity was in association with mitochondrial and lysosomal membranes (P2 fraction), and less than 10% remained in the P3 fraction. In vitro competition assays demonstrated two binding sites in liver P3 fractions. The spleen and liver also showed saturable binding in vivo. These data suggest the presence of at least one membrane-binding protein for estrogen in liver, adrenal, and spleen. Initial studies of affinity-purified liver P3 fractions using ligand blots indicated the presence of two binding proteins. These potential membrane estrogen- binding proteins may be involved in a very rapid shuttling of estrogen from the plasmalemma to mitochondria and lysosomes.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
P. I. Moreira, J. Custodio, A. Moreno, C. R. Oliveira, and M. S. Santos
Tamoxifen and Estradiol Interact with the Flavin Mononucleotide Site of Complex I Leading to Mitochondrial Failure
J. Biol. Chem., April 14, 2006; 281(15): 10143 - 10152.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
M. A. Valverde, P. Rojas, J. Amigo, D. Cosmelli, P. Orio, M. I. Bahamonde, G. E. Mann, C. Vergara, and R. Latorre
Acute Activation of Maxi-K Channels (hSlo) by Estradiol Binding to the  Subunit
Science, September 17, 1999; 285(5435): 1929 - 1931.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by the Society for the Study of Reproduction.