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Department of Physiology and Biophysics (C.M.T., T.G.P., L.Z., C.T.A., W.R.D., G.G.), College of Medicine, University of Illinois, Chicago, Illinois 60612; and Department of Biochemistry, Molecular Biology, and Cell Biology (D.L.C., D.I.H.L.), Northwestern University, Evanston, Illinois 60208
Address all correspondence and request for reprints to: Dr. Geula Gibori, Department of Physiology and Biophysics (M/C 901), University of Illinois, 835 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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-hydroxysteroid dehydrogenase (20-HSD), and PRL-R gene
expression was investigated during the time of luteolysis. Both
PRL-RL and PRL-RS mRNA and protein were
expressed in corpora lutea of pregnancy, with the long form being the
most dominant at all stages. Whereas no changes in mRNA level of either
PRL-RL or PRL-RS were found until day 20 of
gestation, a profound decline in PRL-R mRNA and protein for both
receptor types occurred at the end of pregnancy. This drop in PRL-R
expression was accompanied by a sharp and abrupt expression of
20-HSD mRNA. Studies performed in vivo and in
luteinized cells in culture indicate that PRL can up-regulate the
expression of the PRL-RL mRNA, an effect prevented by the
tyrosine kinase inhibitor, genistein. PRL-RL mRNA was also
selectively increased by cAMP. In summary, the results of this
investigation have established that: 1) the corpus luteum of pregnancy
expresses both the short and long forms of the PRL-R with the long form
being more abundant; 2) the mRNA for both forms of the PRL-R remains at
constant levels throughout pregnancy but drops before parturition; 3)
the decline in PRL-R mRNA at the end of pregnancy is accompanied by a
dramatic rise in 20-HSD; 4) PRL is able to increase the expression
of PRL-R mRNA; and that 5) both A kinase and tyrosine kinase mediated
pathways appear to participate in the up-regulatory mechanism involved
in PRL-R mRNA expression. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-hydroxysteroid dehydrogenase (20-HSD). PRL causes the
dephosphorylation and activation of EF2, a 100-kDa protein that plays
an important role in peptide elongation and is an essential component
of the protein synthetic machinery (2). When dephosphorylated, EF2
catalyzes the translocation of peptidyl-transfer RNA on ribosomes
leading to increased elongation (3). Whereas PRL appears to stimulate
overall protein synthesis acting at the translational level, it causes
a marked and selective inhibition in 20-HSD gene expression (4).
20-HSD is a 37-kDa enzyme responsible for the catabolism of
progesterone to the inactive progestagen, 20-dihydroprogesterone
(5, 6). This inhibitory action of PRL on 20-HSD gene expression is
essential for maintaining high levels of progesterone during pregnancy.
Whether or not the dephosphorylation of EF2 and the decreased
expression of 20-HSD induced by PRL are due to different signaling
mechanisms in the corpus luteum, perhaps through different receptors,
remains unknown. Indeed, in the rat, two distinct PRL receptors (PRL-R)
have been identified (7, 8, 9). These PRL-R have been classified as long
(PRL-RL) and short (PRL-RS) depending upon the
length of the cytoplasmic domain. Both receptor forms have identical
extracellular and transmembrane domains and a unique intracellular
sequence of 57 and 358 amino acids for the short and long forms,
respectively (10). Signaling through these two forms of the receptor
appears to differ. Whereas the JAK/Stat pathway and tyrosine
phosphorylation are involved in PRL signaling through the
PRL-RL (11, 12, 13), the signaling mechanism through the short
form is unknown. Our finding that PRL inhibition of 20-HSD gene
expression appears not to involve tyrosine phosphorylation (14) and our
recent discovery of a novel luteal protein that can associate with the
intracellular domain of the PRL-RS in an in
vitro system (15) led us to suggest that PRL action on the rat
corpus luteum may involve different forms of receptors. However, before
examining the role of the two forms of the receptor in PRL signaling,
we first had to establish whether indeed the rat corpus luteum of
pregnancy expresses PRL-RL and PRL-RS messenger
RNA (mRNA). Since the corpus luteum undergoes changes during pregnancy,
including a dramatic hypertrophy particularly at midpregnancy and a
marked drop in progesterone secretion late in pregnancy, and since the
maintenance and function of the corpus luteum are dependent on an
interplay of pituitary, ovarian, and placental hormones for its
existence (1), it is also important to characterize the developmental
and hormonal regulation of the PRL-R expression throughout pregnancy.
We were specially interested in determining whether one of the two
forms of the PRL-R decline at the end of pregnancy, since at this stage
the corpus luteum becomes nonresponsive to PRL and PRL-like hormone
from placental origin. |
Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-32P]deoxycytidine triphosphate (dCTP) was from
Amersham Corp. (Arlington Heights, IL); the oligonucleotides used as
primers in the RT-PCR analysis were obtained from Life Technologies
(Grand Island, NY). Genistein was obtained from ICN Biomedicals
(Aurora, OH). Ovine PRL (oPRL) was provided by the NIADDK (ovine
PRL-18, 30 IU/mg, Bethestha, MD). Antibiotic-antimycotic mixture and
FBS were obtained from GIBCO-BRL (Gaithersburg, MD) and Hyclone
(Logan, UT) respectively. DMEM-Ham’s F12 (DMEM/F12), 8-bromo-cAMP,
human CG (hCG), and all other reagent grade chemicals were purchased
from Sigma Chemical Co. (St. Louis, MO).
Animals
Pregnant (day 1 = sperm positive) and immature female (day
26 of age) Sprague-Dawley rats were obtained from Sasco Animal Labs
(Madison, WI). They were kept under controlled conditions of light
(lights on 0700–1900 h) and temperature (22–24 C) with free access to
standard rat chow and water. Animals were handled according to the
procedures approved by the Institutional Animal Care and Use
Committee.
Experimental procedures
For the developmental studies, rats were obtained at various
stages of pregnancy from days 4 to 22 (day of parturition) and at the
day after parturition. Corpora lutea were dissected from the ovaries
under a stereoscopic microscope. Follicles were also obtained from day
14 pregnant rats. All tissues were frozen in liquid nitrogen and stored
at -80 C until processed for RNA or protein. Blood samples were
collected for assays of serum progesterone and
20-dihydroprogesterone levels.
To determine the effect of PRL on PRL-R mRNA in corpora lutea, pregnant rats were hypophysectomized on day 3 of pregnancy and injected sc with 125 µg PRL (NIDDK oPRL-18, 30 IU/mg twice daily) in 50% polyvinylpyrrolidone, pH 9.0, for 4 days.
To neutralize circulating LH at the end of pregnancy, rats were injected sc with 1 ml LH antiserum generated in a mare against bovine LH as used previously (16, 17). Control rats were injected with normal horse serum. Corpora lutea were removed on the morning of day 22 of pregnancy, before parturition, which usually occurs on the afternoon of day 22 in this rat strain.
Granulosa cell culture
Maturation of preovulatory follicles was stimulated by treatment
of immature rats at day 28 of age with 0.15 IU hCG sc twice daily for 2
days (18). Luteinization of these preovulatory follicles was
subsequently achieved by an ovulatory dose (10 IU) of hCG on the third
day via the tail vein. Luteinized granulosa cells were harvested from
preovulatory follicles 7 h after the iv injection of hCG. Briefly,
follicles were incubated sequentially in DMEM/F12 1:1, containing 6
mM EGTA and 0.5 M sucrose, respectively, and
granulosa cells were harvested by needle pricking the follicles. The
cells were plated in 60-mm culture dishes at 8 x 105
cells/ml and incubated at 37 C under 95% air/5% CO2
atmosphere in DMEM/F12 containing 15 mM HEPES, 1% FBS, 100
IU/ml penicilin G, 100 µg/ml streptomycin, and 0.25 mg/ml
amphotericin B. After 72 h of incubation, the medium was changed,
cells were treated during 12 h with different hormones or
reagents, and total RNA was extracted.
RNA isolation and RT-PCR analysis
Total RNA from frozen corpora lutea was purified by
homogenization in guanidinium thiocyanate and centrifugation through a
cesium chloride cushion (19), whereas total RNA from cultured cells was
isolated by a one-step guanidinium-thiocyanate-phenol-chloroform
extraction procedure (20).
For detection of long and short form PRL-R mRNAs by RT-PCR, three
oligonucleotide primers were synthesized as described earlier (21). To
detect each form of PRL-R mRNA, a sense strand oligonucleotide from the
common extracellular domain coding region
(5'-AAAGTATCTTGTCCAGACTCGCTG-3') was combined with either a
PRL-RL specific primer (5'-AGCAGTTCTTCAGACTTGCCCTT-3') or a
PRL-RS specific primer (5'-TTGTATTTGCTTGGAGAGCCAGT-3')
corresponding to the first 23 nucleotides of the unique cytoplasmic
coding region. For 20-HSD mRNA analysis, oligonucleotide primers of
21 nucleotides were designed based on the sequence of the rat 20-HSD
gene (22) (5'-CAACCAGGTAGAATGCCAATCT-3' and
5'-TTCGAGCAGAAC-TCATGGCTA-3'). In each reaction, an additional pair
of 21 nucleotides (5'-CTGAAGGTCAAAGGGAATGTG-3' and
5'-GGACAGAGTCTTG-ATATCTC-3') specific to the rat ribosomal protein
L19 mRNA was included for use as an internal control (23). The
predicted sizes of the PCR-amplified products were 279 bp for both
PRL-RL and PRL-RS, 440 bp for 20-HSD, and
194 bp for L19. RNA samples were assayed for DNA contamination by PCR
without prior reverse transcription. One microgram of total RNA was
reverse transcribed at 37 C using random hexamer primers (Pharmacia,
Piscataway, NJ) and Moloney murine leukemia virus-RT (Life
Technologies, Grand Island, NY) in a 20-µl reaction mixture. The
reaction mixture was added to tubes containing specific oligonucleotide
primer (50 pmol each) for amplification of either form of the PRL-R or
20-HSD complementary DNAs. A mix containing the oligonucleotide
primers for L19 mRNA (50 pmol each), Taq DNA polymerase (2.5
U), and [-32P]deoxy-CTP (2 µCi of 3000 Ci/mmol) was
added to each tube, and the final volume was increased to 90 µl with
1 x PCR buffer [20 mM Tris (pH 8.4), 50
mM KCl and 2.5 mM MgCl2 ]. The
samples were overlaid with light mineral oil, and PCR was carried out
for 20 cycles with an annealing temperature of 65 C in a
Perkin-Elmer/Cetus Thermal Cycler (Norwalk, CT), except for the
experiments shown in Figs. 1
and 2, where a 60 C annealing temperature was
used. The conditions were such that the amplification of the products
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. After autoradiography, data were
analyzed using a Molecular Dynamics PhosphorImager and ImageQuant
version 3 software (Molecular Dynamics, Sunnyvale, CA). The intensity
of the PRL-RL, PRL-RS, and 20-HSD signals
were normalized to that of the ribosomal protein L19 internal control.
Data were examined by one-way ANOVA followed by Duncan’s multiple
range test. When appropriate, Student’s t test was used. A
level of P < 0.05 was accepted as statistically
significant.
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RIAs
Serum progesterone concentrations were measured using a
commercially obtained kit (Diagnostic Products Corporation, Los
Angeles, CA). The sensitivity of the assay was 0.02 ng/ml, and the
inter- and intraassay coefficients of variation were 5% and 6%,
respectively. Serum 20-dihydroprogesterone was assayed after hexane
extraction using a highly specific antiserum kindly provided by Dr.
Quadri (Department of Anatomy/Physiology, Kansas State University,
Manhattan, KS). The sensitivity of the assay was 0.01 ng/assay tube,
and the inter- and intraassay coefficients of variation were less than
10%.
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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We first examined and compared the mRNA expression of
PRL-RL and PRL-RS in corpora lutea and
follicles of rats at the same stage of pregnancy (day 14). As shown in
Fig. 1
, both PRL-RL and PRL-RS were detected in
both ovarian tissues with PRL-RL being the most abundant.
However, levels of both receptor mRNAs were much higher in the corpus
luteum than in the follicle (P < 0.05).
Developmental studies shown in Fig. 2A indicate that both forms of the
PRL-R mRNA are expressed in the corpus luteum throughout pregnancy. The
amount of the RT-PCR product corresponding to the long form of the
PRL-R mRNA was consistently higher than that obtained for the short
form of the PRL-R mRNA (Fig. 2B). Throughout gestation and until day 20
of pregnancy, there were no significant changes in mRNA levels of
either form of the PRL-R in the corpus luteum. However, most
interestingly, between days 20 and 22, just before parturition, an
abrupt decline in mRNA for both forms of the receptor occurred. Using a
polyclonal antiserum that recognizes both forms of the receptor, we
examined by Western analysis (Fig. 3) the
expression of PRL-R protein in corpora lutea of early (day 4) and late
(day 22) pregnancy. PRL-RL and PRL-RS proteins
were detected in the rat corpus luteum at 66 and 45 kDa, respectively.
Similarly to PRL-RL and PRL-RS mRNA expression,
the PRL-RL protein was expressed at higher levels than the
PRL-RS, and lower levels of both receptor forms were found
on day 22 when compared with day 4 of pregnancy.
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-HSD at the end of pregnancy-HSD gene is negatively regulated by PRL, and
therefore we would predict an increase in the level of the 20-HSD
mRNA at day 22 and after parturition. As depicted in Fig. 4 (A and B), PRL-RL and
PRL-RS mRNA levels decreased markedly on day 21 and
remained at low levels until a day after parturition; at these times,
20-HSD mRNA levels increased dramatically (Fig. 4C). 20-HSD could
not be detected before day 21, but became abruptly and highly expressed
from day 21 until the day after parturition. The rapid rise in luteal
20-HSD mRNA was accompanied (Fig. 5, A
and B) by a sharp increase in 20-dihydroprogesterone and a
corresponding fall in progesterone in the circulation of the same
animals. The decline in PRL-R expression appears to render the corpus
luteum less responsive to the inhibitory action of PRL and allows for
the increase in 20-HSD mRNA levels and the catabolism of
progesterone to 20-dihydroprogesterone.
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indicate that neutralization of LH at
the end of preg-nancy caused a marked decrease (P <
0.01) in PRL-RL and PRL-RS mRNA levels
indicating that LH may have an up-regulatory rather than a
down-regulatory role in PRL-R expression.
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).
Interestingly, the up-regulation was restricted to the long form of the
receptor (P < 0.05).
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(A and C), PRL caused a
significant increase in PRL-RL mRNA levels, but not in the
short form of the PRL-R (Fig. 8, B and C).
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2-macroglobulin in the corpus luteum (28). As shown in Fig. 9, PRL induced within 12 h a
significant increase (P < 0.05) in PRL-RL
mRNA (panel A); however, when genistein was added along with PRL (panel
B), a sharp decrease (P < 0.05) in PRL-R expression
was observed, suggesting that PRL stimulation of PRL-R gene expression
involves tyrosine kinase (s). Similar to the effect of PRL,
8-bromo-cAMP (Fig. 10) also caused the
up-regulation of the long but not the short form of the PRL-R,
suggesting that both protein kinase A and a tyrosine kinase pathway are
involved in the regulation of PRL-R mRNA expression in ovarian
cells.
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-HSD gene expression at the end of
pregnancy. Using RT-PCR and Western analysis, both forms of the PRL-R were found to be expressed in the rat corpus luteum with the PRL-RL being the most abundant at all stages of pregnancy. A similar pattern was observed in the whole ovary of pregnant mice which express, however, three different forms of the PRL-RS (31). In the rat, the short form of the PRL-R is encoded by a transcript of 1.8 kb, whereas the long form is encoded by three larger transcripts (8, 32). Although the heterogeneity of PRL-R mRNA species appears to arise from alternative splicing (8, 32), it is evident from recent data (33, 34) that differential transcriptional initiation and alternative polyadenylation also contribute to the mRNA heterogeneity.
Coexpression of both PRL-R forms has been reported in several
tissues of pregnant rats (35). However, in contrast to rat liver and
mammary gland where PRL-RS is the major receptor (8, 36),
it is the PRL-RL that predominates in the corpus luteum.
The developmental expression during pregnancy of the PRL-R also differs
in these three major PRL target tissues. Whereas in both mammary gland
and liver PRL-R mRNA levels remain low during pregnancy but increase
just before parturition (36), the receptor mRNA levels in the corpus
luteum are elevated throughout pregnancy and drop just before
parturition. Thus, in spite of the similar hormonal environment during
pregnancy, a marked difference in the developmental expression of the
PRL-R takes place in these three major PRL target tissues. Differential
regulation may be due not only to particular sets of transcription
factors present and active at a given time, but also to different
promoters that may be regulated differently. Indeed the recent finding
of three alternative promoters in the 5'-untranslated region of the
PRL-R gene may provide the molecular basis of this tissue specificity
in the developmental regulation of the PRL-R expression (33). Whereas
the rise in PRL-R in the mammary gland just before parturition helps in
preparing this gland to become highly responsive to PRL, a hormone
crucial for lactation, the drop in PRL-R mRNA and protein at the end of
pregnancy found in this investigation appears to play a crucial role in
terminating pregnancy. Indeed for years it was known that despite very
high levels of placental lactogen in the circulation, progesterone
secretion by the corpus luteum declines abruptly at the end of
pregnancy. Recently we have cloned 20-HSD, the enzyme responsible
for the catabolism of progesterone (22), and have shown that the
expression of this gene is silenced by PRL, rat placental lactogen-1,
and rat placental lactogen-2 (14). However, despite high levels of rat
placental lactogen-2 in the circulation and the rise of pituitary PRL
(26, 27), 20-HSD mRNA and protein become abruptly expressed just
before parturition (Ref. 4 and present study). We originally thought
that 20-HSD mRNA may be induced, despite high levels of PRL, by the
rise in LH at the end of pregnancy. Indeed, a recent report indicates
the ability of ovine LH to stimulate 20-HSD activity in corpora
lutea of late pregnancy (37). However, based on a preliminary study in
which we examined LH and cAMP stimulation of 20-HSD expression in
cultured cells that express the PRL-R, it became apparent that PRL
totally blocks the stimulatory effect of both LH and cAMP on 20-HSD
expression (38). The more detailed study reported in this investigation
clearly indicates that 20-HSD mRNA, which is undetectable on day 20
of pregnancy, becomes highly expressed within 24 h and remains
elevated the day of parturition (day 22) and the day following
parturition exactly at a time when a profound decline in the expression
of both forms of the PRL-R occurs. This decrease in PRL-R expression
most probably renders the corpus luteum less responsive to the
circulating PRL and PRL-related hormones and diminishes the
PRL-mediated inhibition of 20-HSD expression.
What induces the drop in both forms of the PRL-R at the end of pregnancy remains unclear. We originally thought that the rise in LH may be responsible for such an event; however, neutralization of LH with a dose of LH antiserum known to block LH action (16, 17) caused a further decline in PRL-R mRNA expression, suggesting that LH is more likely to be involved in the up-regulation of this receptor. PRL also can up-regulate the expression of the PRL-R in the rat corpus luteum. Our finding that PRL causes a selective increase in the expression of PRL-RL with little, if any, effect on that of PRL-RS mRNA suggests that PRL and rat placental lactogen may be responsible for the higher expression of the long form of the receptor in the rat corpus luteum during pregnancy. Both receptor types appear to be derived from a single primary transcript and whether PRL’s effect is at the level of RNA splicing or mRNA stability remains to be investigated.
Since the increase in PRL-RL mediated by PRL was blocked by the tyrosine kinase inhibitor genistein, and also since cAMP up-regulates the expression of PRL-RL, it appears that the up-regulation of PRL-RL mRNA may involve both protein kinase A and tyrosine kinase pathways.
In summary, results of this investigation have established that: 1) the
corpus luteum of pregnancy expresses both the short and the long form
of the PRL-R with the long form being much more abundant; 2) the PRL-R
mRNA remains elevated throughout pregnancy but drops before
parturition; 3) the decline in PRL-R mRNA at the end of pregnancy is
accompanied by a dramatic rise in 20-HSD; 4) PRL is able to increase
the expression of PRL-R mRNA; and 5) both A kinase- and tyrosine
kinase-mediated pathways appear to participate in the up-regulatory
mechanism of PRL-R mRNA expression.
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Acknowledgments |
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-dihydroprogesterone antibody and to the NIDDK and National
Hormonal and Pituitary Program (NIH) for the oPRL, R. Clepper for
animal care, L. Alaniz-Avila for photography, and V. Rogala for the
preparation of the manuscript. We especially wish to thank Dr. J. Ou
for his expert assistance. |
Footnotes |
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2 These authors contributed equally to this work.
3 NIH Merit Awardee (HD-11119).
Received April 28, 1997.
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References |
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J. D. Curlewis, S. P. Tam, P. Lau, D. H. L. Kusters, J. L. Barclay, S. T. Anderson, and M. J. Waters A Prostaglandin F2{alpha} Analog Induces Suppressors of Cytokine Signaling-3 Expression in the Corpus Luteum of the Pregnant Rat: A Potential New Mechanism in Luteolysis Endocrinology, October 1, 2002; 143(10): 3984 - 3993. [Abstract] [Full Text] [PDF]
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N. Baran, P. A. Kelly, and N. Binart Characterization of a Prolactin-Regulated Gene in Reproductive Tissues Usingthe Prolactin Receptor Knockout Mouse Model Biol Reprod, April 1, 2002; 66(4): 1210 - 1218. [Abstract] [Full Text] [PDF]
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S. P. Tam, P. Lau, J. Djiane, D. J. Hilton, and M. J. Waters Tissue-Specific Induction of SOCS Gene Expression by PRL Endocrinology, November 1, 2001; 142(11): 5015 - 5026. [Abstract] [Full Text] [PDF]
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 N. P. Vlahos, E. M. Bugg, M. J. Shamblott, J. Y. Phelps, J. D. Gearhart, and H. A. Zacur Prolactin receptor gene expression and immunolocalization of the prolactin receptor in human luteinized granulosa cells Mol. Hum. Reprod., November 1, 2001; 7(11): 1033 - 1038. [Abstract] [Full Text] [PDF]
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A. Zetser, T. Kisliouk, E. Ivakin, and M. Lahav Dependence on Prolactin of the Luteolytic Effect of Prostaglandin F2{alpha} in Rat Luteal Cell Cultures Biol Reprod, October 1, 2001; 65(4): 1082 - 1091. [Abstract] [Full Text] [PDF]
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K. K. Olson, L. E. Anderson, M. C. Wiltbank, and D. H. Townson Actions of Prostaglandin F2{{alpha}} and Prolactin on Intercellular Adhesion Molecule-1 Expression and Monocyte/Macrophage Accumulation in the Rat Corpus Luteum Biol Reprod, March 1, 2001; 64(3): 890 - 897. [Abstract] [Full Text]
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 M. E. Freeman, B. Kanyicska, A. Lerant, and G. Nagy Prolactin: Structure, Function, and Regulation of Secretion Physiol Rev, October 1, 2000; 80(4): 1523 - 1631. [Abstract] [Full Text] [PDF]
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D. L. Russell and J. S. Richards Differentiation-Dependent Prolactin Responsiveness and Stat (Signal Transducers and Activators of Transcription) Signaling in Rat Ovarian Cells Mol. Endocrinol., December 1, 1999; 13(12): 2049 - 2064. [Abstract] [Full Text]
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C. Campino, C. Torres, S. Ampuero, S. Diaz, G.B. Gonzalez, and M. Seron-Ferre Bioactivity of prolactin isoforms: lactation and recovery of menses in nursing women Hum. Reprod., April 1, 1999; 14(4): 898 - 905. [Abstract] [Full Text] [PDF]
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C. M. Telleria, J. Ou, N. Sugino, S. Ferguson, and G. Gibori The Expression of Interleukin-6 in the Pregnant Rat Corpus Luteum and Its Regulation by Progesterone and Glucocorticoid Endocrinology, August 1, 1998; 139(8): 3597 - 3605. [Abstract] [Full Text] [PDF]
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P. Nokelainen, H. Peltoketo, R. Vihko, and P. Vihko Expression Cloning of a Novel Estrogenic Mouse 17{beta}-Hydroxysteroid Dehydrogenase/ 17-Ketosteroid Reductase (m17HSD7), Previously Described as a Prolactin Receptor-Associated Protein (PRAP) in Rat Mol. Endocrinol., July 1, 1998; 12(7): 1048 - 1059. [Abstract] [Full Text]
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D.A. Douglas, A. Houde, J.H. Song, R. Farookhi, P.W. Concannon and, and B.D. Murphy Luteotropic Hormone Receptors in the Ovary of the Mink (Mustela vison) during Delayed Implantation and Early-Postimplantation Gestation Biol Reprod, July 1, 1998; 59(3): 571 - 578. [Abstract] [Full Text]
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N. Sugino, M. Hirosawa-Takamori, L. Zhong, C. M. Telleria, K. Shiota, and G. Gibori Hormonal Regulation of Copper-Zinc Superoxide Dismutase and Manganese Superoxide Dismutase Messenger Ribonucleic Acid in the Rat Corpus Luteum: Induction by Prolactin and Placental Lactogens Biol Reprod, July 1, 1998; 59(3): 599 - 605. [Abstract] [Full Text]
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C. M. Telleria, L. Zhong, S. Deb, R. K. Srivastava, K. S. Park, N. Sugino, O.-K. Park-Sarge, and G. Gibori Differential Expression of the Estrogen Receptors {alpha} and {beta} in the Rat Corpus Luteum of Pregnancy: Regulation by Prolactin and Placental Lactogens Endocrinology, May 1, 1998; 139(5): 2432 - 2442. [Abstract] [Full Text] [PDF]
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 C. O. Stocco, L. Zhong, Y. Sugimoto, A. Ichikawa, L. F. Lau, and G. Gibori Prostaglandin F2alpha -induced Expression of 20alpha -Hydroxysteroid Dehydrogenase Involves the Transcription Factor NUR77 J. Biol. Chem., November 17, 2000; 275(47): 37202 - 37211. [Abstract] [Full Text] [PDF]
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