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Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030
Address all correspondence and requests for reprints to: JoAnne S. Richards, Department of Cell Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030. E-mail: joanner{at}bcm.tmc.edu
The expression and function of estrogen receptor ER
/ß subtypes and
ERß variants in granulosa cells have been determined using several
integrated approaches: , Western blotting, indirect immunofluorescence,
RT-PCR, and transient transfection assays. Each of these approaches has
provided specific details concerning the dynamics of ER expression, ER
functional activity, and estradiol (E) regulation of target genes in
granulosa cells. Specifically, the studies presented herein document
that messenger RNAs (mRNAs) encoding ERß and its splice variants, as
well as mRNA encoding ER, are expressed in granulosa cells of
immature rats before and during culture in serum-free medium. The
results also provide the first documentation that functional (DNA
binding and transcriptionally active) ER is present in cultured
granulosa cells and that its ability to bind consensus estrogen
response element (ERE) oligonucleotide and to transactivate an ERE
promoter-reporter construct is associated with the level (type?) of
receptor protein as well as the stage of granulosa cell
differentiation. Using a labeled ERE consensus oligonucleotide and
antibodies specific for ERß and ER, we show that ERß but not
ER was detected (supershifted in electrophoretic mobility shift
assays) in extracts of granulosa cells cultured overnight (0 h) in
defined medium alone. When the cells were cultured with FSH and
testosterone (T) to stimulate their differentiation, ERß binding
activity, as well as immunoreactive ERß as determined by Western blot
analyses, decreased progressively from 24 to 48 h and was
undetectable by 72 h. ERß mRNA was low, and ERß binding
activity was not observed in luteinized granulosa cells. ER DNA
binding activity was not observed in any of the granulosa cell
cultures, although low levels of immunoreactive ER were detected by
Western blot analyses. Immunofluorescent analyses documented that
ERß, as well as ER, were localized to granulosa cell nuclei and
that the intensity of nuclear staining was related to agonist
stimulation and differentiation: forskolin increased, whereas E
decreased immunostaining for ERß and ER at 48 h. When an
ERE-E1b-luciferase vector was transfected into granulosa cells of
unprimed rats, basal luciferase activity was low but increased by
forskolin (3–4x) and by E (2x), responses to both agonists being
blocked by the ER antagonist, ICI. When the same vector was transfected
into differentiated granulosa cells (cultured for 48 h with
FSH/T), forskolin alone increased activity. Collectively, these results
show that ERß protein is preferentially expressed in immature
granulosa cells, is functionally active (binds DNA), can transactivate
(either as a homodimer or heterodimer with ER) ERE-containing
promoter constructs, and might be associated with increased expression
of the endogenous gene encoding c-Jun.
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