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Department of Physiology and Biophysics (N.S., M.Z., R.K.S., C.M.T., S.E.N., M.R., G.G.) University of Illinois at Chicago, Chicago, Illinois 60612-7342; Faulkner Centre for Reproductive Medicine (M.Z., R.K.S.), Boston, Massachusetts 02130; and Heritable Disorders Branch (J.Y.C.), National Institute of Child Health and Human Development, Bethesda, Maryland 20892
Address all correspondence and requests for reprints to: Dr. Geula Gibori, Department of Physiology and Biophysics (M/C 901), University of Illinois at Chicago, 901 South Wolcott Avenue, Chicago, Illinois 60612-7342.
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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progesterone, LH, or PRL could be detected. This cell line also
expressed 20-hydroxysteroid dehydrogenase (20-HSD), but not
cholesterol side-chain cleavage cytochrome P450 (P450scc),
3ß-hydroxysteroid dehydrogenase, or aromatase cytochrome P450
(P450arom). Although the cells did not express the PRL receptor, they
did express Janus kinase (JAK2) and signal transducers and activators
of transcription (Stat5b), and, when transfected with the PRL receptor,
they responded to PRL with a marked inhibition in 20-HSD mRNA
expression. In addition, estradiol enhanced ER-ß expression in a
dose-dependent manner whereas cAMP stimulation caused a marked and
rapid increase in the expression of the orphan receptor nur 77. In
summary, a temperature-sensitive cell line was successfully established
from the large luteal cells of rat corpora lutea. These cells express
key genes encoding enzymes and receptors inherent to this defined
luteal cell population and respond to stimulation by PRL, estradiol,
and cAMP. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-hydroxysteroid
dehydrogenase (20-HSD), Janus kinase (JAK2), and signal transducer
and activator of transcription (Stat5), and the orphan nuclear receptor
nur 77, but also respond to estrogen with an enhanced expression of
ER-ß, to cAMP with a rapid induction of nur 77, and to progesterone
and glucocorticoid with an inhibition in 20-HSD (2). Since GG-CL
cells are devoid of PRL receptor, which is the focus of many ongoing
studies in our laboratory, we have successfully transfected this
receptor into these cells and showed that they also respond to PRL with
an inhibition in 20-HSD. The data in this report confirm many of our
previous observations in primary luteal cell culture and attest to the
great potential of the temperature-sensitive luteal cell line in the
study of luteal cell differentiation and gene regulation. |
Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-32P]deoxycytidine triphosphate (dCTP)
was from Amersham (Arlington Heights, IL). Twenty-five- or
75-cm2 culture flasks were from Becton Dickinson Co.
(Franklin Lakes, NJ). Taq DNA polymerase was from
Perkin-Elmer Co. (Foster City, CA). GeneScreen nylon membranes were
from New England Nuclear Systems (Boston, MA). Lipofectin and G418
sulfate (Geneticin) were from Life Technologies Inc. (Grand Island,
NY).
Animals
Pregnant Sprague-Dawley rats (day 1 = sperm positive)
purchased from Sasco Animal Laboratories (Madison, WI) were housed at
24 C with a 14-h light, 10-h dark cycle and allowed free access to
Purina rat chow and water. The care and handling of the rats conformed
with the NIH guidelines for animal research. The experimental protocol
was approved by the Institutional Animal Care and Use Committee.
Transformation of rat luteal cells by SV-40
Large luteal cells were purified to homogeneity by flow
cytometry from the corpus luteum of day 14 pregnant rats as reported
previously (3). Cells were cultured in medium (McCoy’s 5A-Ham’s F12,
1:1) containing 25 mM HEPES, 2% antibiotic-antimycotic
solution, and 5% FCS. After plating for 24 h, the cells were
washed several times and then infected with the SV-40 tsA209
mutant virus as previously reported (4). Transformed cells were
maintained at the permissive temperature (33 C) until colonies were
identified. Several colonies of the transformed cells were isolated and
passaged. One clone, designated GG-CL cells, was used in this study.
The GG-CL cells were cultured in a 25- or 75-cm2 flask with
the incubation medium (RPMI-1640 medium containing 2x
antibiotic-antimycotic solution, 1x nonessential amino acids, 1x
sodium pyruvate, 0.5% D-glucose, and 10% FBS) at the
permissive (33 C) and the nonpermissive (40 C) temperatures under an
atmosphere consisting of 5% CO2-95% air.
Transfection of GG-CL cells with the PRL receptor
For the stable transfection of GG-CL cells with the PRL
receptor, we adopted the procedure of Felgner et al. (5)
with slight modifications. GG-CL cells were plated in six-well Falcon
dishes and grown at 33 C to 33% confluency in RPMI-1640 medium
containing 5% FBS. Cells were washed with serum-free medium with no
antibiotics and were transfected using Lipofectin according to the
manufacturer’s protocol. The cells were transfected with 10 µg of
the expression vector pMT2poly containing the PRL receptor
complementary DNA (cDNA) and with pSV2neo vector, both generously
provided by Dr. Daniel Linzer (Northwestern University, Chicago, IL).
After transfection the medium was replaced with the growth medium
containing 5% FBS and antibiotics and incubated for 48 h. After
48 h, medium was again replaced with fresh growth medium and
treated with 100 µg/ml of G418 sulfate. G418 sulfate addition was
continued every alternate day until G418 sulfate-resistant colonies
were identified. These colonies were picked and cultured in the growth
medium containing 5% FBS until the cells were confluent. For
identifying the successful stable transfection with PRL receptor, cells
were grown and passaged several times. PRL receptor messenger RNA
(mRNA) expression in these cells was determined by RT-PCR using PRL
receptor-specific primers.
Treatment of GG-CL cells
To examine the effects of estradiol on ER-ß mRNA expression
and of cAMP on the orphan nuclear receptor nur 77 mRNA expression,
GG-CL cells were cultured at 33 C until 50% confluent and shifted to
40 C for 2 days. Cells were then treated with either 17ß-estradiol
for 6 h, or with 8-bromo-cAMP (100 µM) in the
presence or absence of cycloheximide (10 µg/ml) for either 30, 60, or
120 min. To examine the effect of PRL on 20-HSD mRNA expression in
GG-CL cells, GG-CL cells transfected with PRL receptor were cultured at
33 C until 50% confluent and then shifted to 40 C for 2 days. Cells
were then treated with ovine PRL (1 µg/ml; NIDDK oPRL-20, 31 IU/mg)
for either 4, 8, 24, or 48 h. After culture, the cells were washed
with PBS several times and stored at -80 C for RNA isolation.
Isolation of total RNA and RT-PCR
Total RNA from the cells was isolated by the
guanidinium-isothiocyanate-phenol-chloroform extraction procedure (6).
For mRNA analysis by RT-PCR, oligonucleotide primers shown in Table 1
were designed based on each cDNA
sequence. Each reaction also included primers
(5'-CTGAAGGTCAAAGGGAATGTG-3' and 5'-GGACAGAGTCTTGATGATCTC-3') to
amplify ribosomal protein L19 or primers (5'-CGTTCACCTTGATGAGCCCATT-3'
and 5'-TCCAAGGGTCCGCTGCAGTC-3') to amplify ribosomal protein S16. Both
L19 and S16 were used as internal controls (20, 21). The predicted size
of the PCR-amplified product was 194 bp for L19 and 100 bp for S16. One
to 3 µg of total RNA were reverse-transcribed at 42 C in a 20-µl
reaction mixture [1 x PCR buffer, 2.5 mM
deoxynucleoside triphosphates, 5 µM random hexamer
primers, 1.5 mM MgCl2, and 200 U Moloney murine
leukemia virus reverse transcriptase (Life Technologies)]. For PCR
amplification, a mixture containing oligonucleotide primers (sequences
shown in Table 1; 50 pmol), [-32P]dCTP (2 µCi at
3000 Ci/mmol), and Taq DNA polymerase (2.5 U) was added to
each reaction. The total volume was increased to 90 µl with 1 x
PCR buffer, and the samples were overlaid with mineral oil.
Amplification was carried out for 30 cycles using a 65 C annealing
temperature in a Perkin-Elmer/Cetus (Norwalk, CT) thermal cycler. The
conditions were such that amplification of the product was in the
exponential phase, and the assay was linear with respect to the amount
of input RNA. Reaction products were electrophoresed on a 8%
polyacrylamide nondenaturing gel. Each RT-PCR reaction included L19 or
S16 ribosomal protein mRNA primers to normalize the data. After
autoradiography, data were quantified using a PhosphorImager (Molecular
Dynamics, Sunnyvale, CA).
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-32P]dCTP (3000 Ci/mmol) and was purified from
the unincorporated radionucleotide by column chromatography. The blots
were prehybridized and hybridized in a buffer containing 50%
formamide, 0.6 M NaCl, 1 mM EDTA, 25
mM HEPES (pH 6.5), 50 mM sodium phosphate (pH
6.5), 0.1% SDS, 5x Denhardt’s solution, 10% dextran sulfate
(hybridization only), and salmon sperm DNA (100 µg/ml) at 42 C for
18 h. Blots were washed with 2x SSC (containing 0.1% SDS) for 10
min, 1x SSC (containing 0.1% SDS) for 10 min, and 0.5x SSC
(containing 0.1% SDS) for 5 min at 68 C. The resultant blots were
exposed to Kodak X-Omat film (Eastman Kodak Co., Rochester, NY) using
intensifying screens at -80 C. |
Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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To demonstrate that GG-CL cells are indeed temperature sensitive, cells
were plated at the density of 105 cells per flask in a
25-cm2 tissue culture flask and cultured at 33 C for 10
days. Cells were also cultured at 33 C for 2 days and were then shifted
to 40 C and cultured for 10 days. Cells were harvested at each time
point by trypsinization and counted by the trypan blue dye exclusion
method. At 33 C, cells rapidly divided and became confluent, whereas
cells that were moved to 40 C ceased to divide and were able to grow
only as monolayers (Fig. 1).
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, GG-CL cells exhibited
remarkable morphological change when they were shifted from 33 C to 40
C. At 33 C, the cells seemed to be small and compact and showed a lower
cytoplasm-to-nucleus ratio (Fig. 2, upper panel). At 40 C,
these cells assumed a monolayer appearance; they became differentiated
and flat, with an increased cytoplasm-to-nucleus ratio and a typical
appearance resembling the primary culture (Fig. 2, lower
panel).
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or the newly identified ER-ß (8). ER mRNA
could not be detected in these cells by RT-PCR (data not shown),
whereas ER-ß mRNA was clearly expressed (Fig. 3A). The level of expression of this
receptor was increased at 40 C when the cells became fully
differentiated (Fig. 3A). Since estrogen has been reported to modulate
ER levels in several estrogen target tissues, such as the uterus and
mammary gland (23, 24, 25), we examined whether estradiol can influence the
expression of ER-ß in this luteal cell-derived cell line. As shown in
Fig. 3, B and C, the GG-CL cells responded to the estradiol challenge
with a dose-dependent increase in ER-ß mRNA expression. The rat
corpus luteum does not express the progesterone receptor (PR) but does
express the GR (2, 26), and we recently have shown that the tropic
action of progesterone in the corpus luteum is through the GR (2).
Indeed, as reported previously (2), no PR could be detected in the
GG-CL cells (Fig. 4A) whereas the GR mRNA
was expressed at 33 C and was markedly increased at 40 C (Fig. 4B).
Once we established the expression of steroid receptors in these cells,
we examined for membrane receptors known to be highly expressed in the
rat corpus luteum: the PRL receptor and LH receptor. We also examined
for IL-6 receptor expression since this receptor was recently shown to
be expressed and regulated in the rat corpus luteum (27). As shown in
Fig. 5A, IL-6 receptor mRNA was readily
expressed in the GG-CL cells at both temperatures. However, neither the
PRL receptor (Fig. 5B) nor the LH receptor mRNA (Fig. 5C) could be
detected in these cells although they were highly expressed in the
corpus luteum used as a control. Although the GG-CL cells did not
express the LH receptor, they did respond to cAMP stimulation with an
increase in nur 77 mRNA expression. Nur 77, also known as NGFI-ß, is
an immediate-early gene whose expression is stimulated by cAMP and
whose mRNA is stabilized by cycloheximide (28, 29). As shown in Fig. 6, cAMP caused a rapid induction of nur
77 mRNA. No nur 77 expression could be detected in GG-CL cells
untreated with cAMP (lane 1). However, within 30 min of cAMP treatment,
nur 77 mRNA became expressed (lane 2) and reached peak value at 60 min
(lane 4). A marked decline was seen thereafter (lane 6). Treatment with
cycloheximide caused a superinduction of nur 77 mRNA (lanes 3, 5, and
7).
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-HSD, a gene that we
recently cloned (14) and showed to be under the control of PRL (30, 31), we have also examined the expression of this enzyme in GG-CL cells
maintained at both temperatures. As shown in Fig. 7, B, C, and D, P450scc, 3ß-HSD, and
P450 aromatase mRNAs were undetectable in GG-CL cells, although they
were highly expressed in the corpus luteum used as a control. However,
20-HSD mRNA was expressed at both temperatures with much higher
expression when the cells were differentiated at 40 C (Fig. 7A).
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-HSD, we examined whether these cells
express the JAK2/Stat5b system known to mediate PRL signaling in many
cells including luteal cells (31, 32, 33, 34, 35). We used liver tissue as a
control, which is known to highly express the JAK2 kinase and the Stat5
transcriptional factors (36). As shown in Fig. 8, the GG-CL cells readily expressed both
JAK2 and Stat5b mRNA. We therefore transfected these cells with the PRL
receptor and examined whether they become responsive to PRL. The
results shown in Fig. 9 indicate that the
cells transfected with the PRL receptor (Fig. 9A) respond to PRL with
an inhibition in 20-HSD mRNA expression (Fig. 9B).
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The GG-CL cells express many genes characteristic to the corpus luteum,
although they have lost their ability to produce progesterone upon
transformation. However, this lack of progesterone production has
proven to be an asset in our attempts to determine the effect of
progesterone on the corpus luteum. For years we were trying to
determine whether progesterone can act as a local luteotropin. The
absence of PR in the rat corpus luteum, as well as the copious amounts
of progesterone produced by the primary luteal cells themselves, has
hampered these investigations. Very recently, using this cell line, we
were able to demonstrate that progesterone acts through the GR and
decreases the expression of 20-HSD, an enzyme responsible for the
catabolism of progesterone (2).
Estradiol plays an important role in the regulation of the luteal
function (38). Our results indicate that the GG-CL cells express the
ER-ß but not ER-. The ER-ß was recently shown to be expressed
predominantly in the ovary (8, 39) and corpus luteum (40), and this is,
to the best of our knowledge, the first cell line described that
expresses only ER-ß. The ER-ß in the GG-CL cell appears to be
functional and to mediate estradiol action since estradiol treatment
caused a dose-dependent increase in ER-ß mRNA levels. It seems
therefore that GG-CL cells confer a unique model by which to study and
elucidate ER-ß regulation and function independently from the
ER-.
Another focus of our laboratory is the regulation of 20-HSD by PRL
(14, 30, 31). The GG-CL cells express 20-HSD mRNA endogenously, as
well as the tyrosine kinase JAK2 and the transcriptional factor Stat5b.
The latter two molecules are known to be involved in PRL signaling in
many cells, including luteal cells (31, 32, 33, 34, 35). However, no PRL receptor
mRNA could be detected in GG-CL cells. We have therefore transfected
the GG-CL cells with the PRL receptor. The cells transfected with the
PRL receptor responded to PRL treatment with an inhibition of 20-HSD
mRNA expression, similar to the cells of origin.
Although the GG-CL cells do not express the LH receptor, they do
respond to cAMP with a rapid increase in the expression of the
immediate-early gene nur 77 (28, 29). In addition, the superinduction
of nur 77 mRNA caused by cycloheximide indicates the presence of
proteins involved in nur 77 mRNA degradation in GG-CL cells. We have
chosen to examine the effect of cAMP on nur 77 in these cells because
we have recently demonstrated two response elements for this
transcription factor in the 20-HSD promoter (41). This orphan
nuclear receptor is a potent transcriptional activator of the P450 c21
(28) and P450 c17 genes (42). The finding that cAMP up-regulates
20-HSD in ovarian cells (43, 44), together with the cAMP mediated
up-regulation of nur 77 and the response elements present in the
20-HSD promoter, raises the interesting possibility that nur 77 may
stimulate 20-HSD gene expression.
In summary, we have successfully established a cell line derived from the large luteal cells of the rat corpus luteum. These cells showed a temperature-dependent phenotype with respect to morphology and growth. They also express key genes encoding enzymes and receptors inherent to this defined luteal cell population and respond to stimulation by estradiol, PRL, and cAMP.
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Acknowledgments |
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Footnotes |
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2 Recipient of an NIH Merit Award (HD-11119).
Received October 29, 1997.
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References |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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in the rat corpus luteum through the glucocorticoid receptor.
Endocrinology 138:4497–4500-hydroxysteroid dehydrogenase. Biochem Biophys Res Commun 201:1289–1295[CrossRef][Medline]
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Endocrinology 134:2453–2460-hydroxysteroid dehydrogenase
gene expression and the tyrosine kinase system. Biochem Biophys Res
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2-macroglobulin
gene in rat ovarian granulosa cells: Stat5 activation and binding to
the interleukin-6 response element. Mol Endocrinol 10:171–1842-macroglobulin (2 M) promotor:
relation to the expression of 2 M in the rat ovary. Biol Reprod 55:1029–1038[Abstract]
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dehydrogenase gene promoter. Biol Reprod 54:A356 (Abstract)
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activity in granulosa cells of immature rat ovary. Endocrinology 104:711–714-hydroxysteroid dehydrogenase luteal activities in late pregnant
rats. J Endocrinol 150:423–429This article has been cited by other articles:
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