TY - JOUR
T1 - A middle-affinity estrogen-specific binding protein in livers of vitellogenic and nonvitellogenic Xenopus laevis
AU - Hayward, Marshall A.
AU - Shapiro, David J.
N1 - Funding Information:
This research was supported by Grant PCM 79-206’71 from the National Science Foundation. D. Shapiro is a Research Career Development Awardee from the National Heart, Lung, and Blood Institute and M. Hayward is a National Institutes of Health Predoctoral Trainee. We are grateful to K. Carlson for helpful advice concerning sucrose gradient methodology and to Drs. B. and J. Katzenellenbogen for reading the manuscript.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1981/12
Y1 - 1981/12
N2 - Administration of estradiol-17β to male Xenopus laevis evokes massive liver synthesis of the egg yolk precursor protein, vitellogenin, and its cognate mRNA. Since previous experiments had implicated only a nuclear estrogen receptor in vitellogenesis, we examined Xenopus liver cytosol for other estrogen-binding proteins. Cytoplasmic extracts from unstimulated Xenopus liver contain high levels (approximately 500,000 sites/cell) of an estrogen-specific binding protein. This protein exhibits a Kd of approximately 4 × 10-8M for estradiol-17β, binds estrogenic steroids only, and has a sedimentation coefficient in the range 2-3 S. It is not a classical estrogen receptor, as it does not translocate into the nucleus following estrogen administration. We discuss possible functions of this protein, which include a role in the ontogeny of the vitellogenic response, and in the cytoplasmic transport and storage of estrogen.
AB - Administration of estradiol-17β to male Xenopus laevis evokes massive liver synthesis of the egg yolk precursor protein, vitellogenin, and its cognate mRNA. Since previous experiments had implicated only a nuclear estrogen receptor in vitellogenesis, we examined Xenopus liver cytosol for other estrogen-binding proteins. Cytoplasmic extracts from unstimulated Xenopus liver contain high levels (approximately 500,000 sites/cell) of an estrogen-specific binding protein. This protein exhibits a Kd of approximately 4 × 10-8M for estradiol-17β, binds estrogenic steroids only, and has a sedimentation coefficient in the range 2-3 S. It is not a classical estrogen receptor, as it does not translocate into the nucleus following estrogen administration. We discuss possible functions of this protein, which include a role in the ontogeny of the vitellogenic response, and in the cytoplasmic transport and storage of estrogen.
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U2 - 10.1016/0012-1606(81)90177-9
DO - 10.1016/0012-1606(81)90177-9
M3 - Article
C2 - 7308579
AN - SCOPUS:0019802011
VL - 88
SP - 333
EP - 340
JO - Developmental Biology
JF - Developmental Biology
SN - 0012-1606
IS - 2
ER -