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and ERß Expressed in Chinese Hamster Ovary Cells
Division of Endocrinology (E.R.L.) Long Beach Veterans Affairs
Medical Center Long Beach, California 90822
Departments
of Medicine (M.R., A.P., E.R.L.) and Pharmacology (E.R.L.)
University of California, Irvine Irvine, California 92717
The Ben May Institute (G.L.G.) University of Chicago
Chicago, Illinois 60637
The existence of a putative membrane estrogen
receptor (ER) has been supported by studies accomplished over the past
20 yr. However, the origin and functions of this receptor are not well
defined. To study the membrane receptor, we transiently transfected
cDNAs for ER
or ERß into Chinese hamster ovary (CHO) cells.
Transfection of ER resulted in a single transcript by Northern blot,
specific binding of labeled 17ß-estradiol
(E2), and expression of ER in both nuclear and
membrane cell fractions. Competitive binding studies in both
compartments revealed near identical dissociation constants
(Kds) of 0.283 and 0.287
nM, respectively, but the membrane receptor
number was only 3% as great as the nuclear receptor density.
Transfection of ERß also yielded a single transcript and nuclear and
membrane receptors with respective Kd values of
1.23 and 1.14 nM; the membrane receptor number
was only 2% compared with expressed nuclear receptors. Estradiol
binding to CHO-ER or CHO-ERß activated Gq and Gs proteins in
the membrane and rapidly stimulated corresponding inositol phosphate
production and adenylate cyclase activity. Binding by
17-ß-E2 to either expressed receptor
comparably enhanced the nuclear incorporation of thymidine, critically
dependent upon the activation of the mitogen-activated protein
kinase, ERK (extracellular regulated kinase). In contrast, c-Jun
N-terminal kinase activity was stimulated by
17-ß-E2 in ERß-expressing CHO, but was
inhibited in CHO-ER cells. In summary, membrane and nuclear ER can
be derived from a single transcript and have near-identical affinities
for 17-ß-E2, but there are considerably more
nuclear than membrane receptors. This is also the first report that
cells can express a membrane ERß. Both membrane ERs activate G
proteins, ERK, and cell proliferation, but there is novel differential
regulation of c-Jun kinase activity by ERß and ER.
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