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Division of Endocrinology, Veterans Affairs Medical Center, Long Beach, Long Beach 90822; and Departments of Medicine and Pharmacology, University of California, Irvine, Irvine, California 92717
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ABSTRACT |
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 TOP
 ABSTRACT
 INTRODUCTION
NUCLEAR RECEPTORS
MEMBRANE RECEPTORS
FUTURE RESEARCH DIRECTIONS
REFERENCES
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The existence of binding proteins for the
female sex steroid, 17
-estradiol, has been known for almost 50 years. Presently, two estrogen receptors (ERs), ER-
and ER-, have
been cloned in mammals, and they are expressed in many cell types of
metazoans. ERs act primarily as nuclear transcription factors, and this
effect is enhanced by ligand binding. Emerging data have identified a separate pool of receptors for this steroid in the plasma membrane, but
the mechanisms of action and cellular functions of these proteins are
just beginning to be defined. In this review, the known details of the
nuclear and plasma membrane ER functions will be discussed. A
particular focus will be to define the signaling pathways from the
membrane that lead to important cell physiology effects of estrogen.
The potential interactions of membrane ER with other local proteins
will also be discussed, and the unique but often complementary roles of
the receptor pools will be highlighted. These details may be of
additional relevance to other steroid receptors, since there is
evidence of their existence in the cell membrane.
nuclear receptors; apoptosis; membrane receptors; steroid receptors; signal transduction; cell proliferation
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INTRODUCTION |
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TOP
ABSTRACT
INTRODUCTION
NUCLEAR RECEPTORS
MEMBRANE RECEPTORS
FUTURE RESEARCH DIRECTIONS
REFERENCES
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ESTROGEN RECEPTORS (ERs) mediate the
important actions of the endogenous steroid hormone, 17-estradiol
(E2), and thereby participate in various aspects of
cellular physiology. ER is synthesized in many cell types as two
protein forms, ER- (19, 20) and ER- (30, 48,
79), which are the products of separate genes. Alternatively
spliced transcripts for the receptors largely account for the
differential length binding proteins in discrete cell types. In many
cells, the receptors coexist either as homodimers or as heterodimers
(11, 55), but the distribution of the two receptors does
not completely overlap. ER- exists as the predominant receptor in
most target organs (38). However, ER- is prominently expressed in ovary, prostate, lung, and hypothalamus (9,
31), and recent evidence indicates that there are specific
actions of E2 that can be attributed to one receptor but
not the other (30, 70, 81). The actions of E2
occur on binding ER, and at least the nuclear pool of these receptors
then transactivates relevant genes (17, 21). In some
circumstances, the ER subtypes differentially transactivate target
genes that participate in the cell biological effects of the steroid
hormone (52, 76, and reviewed in Refs. 50 and 67).
Gene deletion of each of the two receptor proteins has revealed the importance of E2 for normal female sex organ development and function (10, 30, 38). Both in vivo and in vitro studies in mammals have suggested that E2 has significant actions for the preservation of bone (74) and blood vessel integrity (44, 71) and contributes to brain function (42) and the modulation of immunity (86). Estrogen also appears to be a significant growth and survival factor for human breast cancer cells (45, 64). Several of the actions of estrogen (as well as other steroid hormones) occur rapidly and are therefore considered to be nongenomic (reviewed in Ref. 35). These effects include the enactment of signal transduction originating from the plasma membrane.
Insight into the rapid, nongenomic actions of E2 began to
take substance more than 20 years ago when a second pool of ERs was
identified (57, 58). Subsequent work has begun to clarify the location and function of this binding protein in the cell plasma
membrane (7, 8, 63, 68). The membrane receptor(s) has not
been isolated or sequenced to date, but there appears to be ER- that
is structurally very similar to the nuclear receptor in many cell types
(53). The membrane ERs probably also include ER-
(63). Various signal transduction pathways have been
recently identified to be rapidly triggered by E2, and
these contribute to the cell biological effects of this steroid.
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NUCLEAR RECEPTORS |
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TOP
ABSTRACT
INTRODUCTION
NUCLEAR RECEPTORS
MEMBRANE RECEPTORS
FUTURE RESEARCH DIRECTIONS
REFERENCES
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The identification of receptors for E2 was most
advanced by work from the laboratories of Jensen and Gorski (4,
23, 78). Subsequent purification of the binding protein (now
known as ER-) resulted in antibodies being generated
(19), and this led to the localization of receptors in the
nucleus of target cells for E2 action (28).
The cDNA for the human ER- was cloned in 1985 (82); in
the 1990s, evidence of complex interactions with coactivator proteins
and basal transcriptional machinery proteins was provided (reviewed in
Ref. 40) (Fig. 1).
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An important discovery of a second ER, ER-, was reported in 1996 (32, 48, 79). ER- and ER- are individually well conserved through mammalian species (54, 79), and there is evidence of a newly identified receptor, ER-
, in teleost fish (22). The two nuclear receptors are homologous mainly in
their DNA binding and ligand pocket binding domains but less so in
their respective hinge and ligand-independent activation function
(AF-1) region. Alternative splicing of the mRNA of ER- gives rise to several protein isoforms, and a recently described 46-kDa ER- isoform may be important in breast cancer (17).
The steroid receptor translocates to the nuclear membrane from the cytosol in a ligand-independent fashion (54) and can activate transcription independently of ligand. However, ligand serves to recruit coactivator proteins (and leads to the displacement of corepressors), functioning mainly through the AF-2 domain of the receptors. The transcriptional effects of the nuclear receptors can be mediated through several mechanisms. E2-ER complexes bind classical inverse palindromic (CAGGTCAnnnTGACCTGA) or nonclassical estrogen response elements on the promoters of target genes. Alternatively, E2-ER complexes transactivate genes through protein-protein interactions with 1) transcription factors such as activator protein 1 or Sp-1 that bind DNA, 2) coaccessory proteins (Src, ACTR), some of which have histone acetylase activity, and 3) RNA polymerase II complex proteins (43). There is evidence that ligation of the two nuclear receptors can differentially transactivate genes (52) and, as mentioned, that the receptors can form heterodimers in vivo (11, 55). In addition, ERs serve to repress genes (80), and this also plays important roles in E2 action.
Traditionally, many of the functions of E2 are proposed to
be mediated through target gene upregulation, considered to be the main
function of the nuclear ER (reviewed in Ref. 10). This is
most apparent in sex organ development and function in females. ER-
also has an important but unanticipated role in fertility and sperm
maturation and function, as demonstrated in the ER- knockout male
mouse (14). Estrogen also affects central nervous system
functions and the neuroendocrine-gonadal axis in both sexes and seems
to preserve bone density (10). Thus the loss of estrogen action after menopause is considered a major risk factor in the development of osteoporosis in women (reviewed in Ref.
62). There is also epidemiological and experimental data
supporting the importance of estrogen to prevent atherosclerosis
(44, 75) and to affect immunity (41, 86).
Estrogen promotes breast cancer propagation (69) and
mediates complex sexual behaviors, at least in rodents
(56). In some of these situations, the genes that serve as
targets for transactivation by the nuclear ER and participate in
estrogen-induced cell biology have been identified. However, in many
instances, the important target genes are unknown. Another caveat is
the recent identification of membrane ER (see below). Because
E2 can induce rapid signaling from the membrane, it is
likely that the cell biology of estrogen action is more complex than
originally anticipated by invoking the nuclear model. Determining the
relative contributions by each of these two receptor pools is an
important focus in understanding the overall actions of the sex steroid.
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MEMBRANE RECEPTORS |
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TOP
ABSTRACT
INTRODUCTION
NUCLEAR RECEPTORS
MEMBRANE RECEPTORS
FUTURE RESEARCH DIRECTIONS
REFERENCES
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Background.
Pietras and Szego (57, 58) originally described an
E2-binding protein in cell membranes that triggered the
rapid generation of cAMP. Subsequent work from many investigators
indicated that E2 rapidly activates signaling, such as
calcium flux (77), phospholipase C activation
(34), and inositol trisphosphate (IP3)
generation (36). In most studies, these actions appear to
require E2 binding to ERs. In neural cells, ERs can
activate protein kinase C and protein kinase A and uncouple opioidergic
and gabanergic receptors from their effector signaling molecules
(reviewed in Ref. 27). These signaling events are likely
to arise from the activation of G proteins by E2, and this
was directly shown for Gs and Gq in
Chinese hamster ovary (CHO) cells expressing either subtype of ER
(63). Thus ERs appear to be part of the large family of G-protein-coupled receptors (GPCR). After several G proteins are activated, E2-ER can then trigger signaling cascades that
culminate in a cell biological function.
Signaling pathways activated by estrogen and implications for cell
physiology.
An important pathway for E2 action is the stimulation of
the proline-directed, threonine/serine kinase, extracellular-regulated kinase (ERK). This member of the mitogen-activated protein (MAP) kinase
family is rapidly (5 min) activated by E2 and results from more proximal kinase activation, including Ras, Src, raf, and MAP
kinase kinase stimulation in MCF-7 breast cancer cells
(45). ERK activation via this cascade contributes to
E2-induced proliferation (6) and survival of
MCF-7 cells (64) and prostate cancer cell proliferation
(46), whereas specific ER antagonists such as ICI-182780
inhibit E2 activation of this (and many) signals. Recently,
Kousteni et al. (29) showed that E2
signaled through the same pathway, to the survival of osteoblasts.
Interestingly, osteoblast survival could also be shown in HeLa cells,
mediated by targeting the E domain of ER- to the cell membrane (but
not to the nucleus), suggesting the role of the plasma membrane ER in
this cell action. ERK activation by E2 also underlies the
stimulation of nitric oxide production in endothelial cells (ECs) and
prevents glutaminergic, excitotoxicity-induced neuronal necrosis
(72). Augmentation of ERK may also induce the activation
of immediate early genes such as c-fos (84),
which then transactivate other genes that are important for the cell
biological effects of this steroid.
isoform of the MAP kinase family,
leading to activation of the threonine/serine MAPKAP-2 kinase and the
phosphorylation of heat shock protein 27 (HSP27) (65). By
expressing dominant-negative mutants of these three molecules,
E2 was shown to utilize this pathway to protect ECs from
metabolic disruption of the actin cytoskeleton and hypoxia-induced cell
death and to stimulate angiogenesis.
In ER-expressing CHO cells, it was also demonstrated that
E2 activates a third MAP kinase, c-Jun
NH2-terminal kinase (JNK), via ER- but inhibits this
kinase via ER- (63). These results indicate that the
two subtypes of ER can differentially modulate signaling pathways. The
physiological relevance of this observation was recently demonstrated
in breast cancer cells. Both chemotherapy and radiation treatment kill
cells mainly by inducing apoptosis via a JNK-dependent
mechanism. It has recently been shown that E2 rapidly
blocks JNK activation in this setting, preventing the JNK-induced,
inactivating phosphorylation of Bcl-2 and Bcl-xl proteins, the
subsequent stimulation of the caspase cascade, and cell death
(64). In this way, E2 can act as a survival
factor, initiated through membrane signaling. Interestingly, tamoxifen, an estrogen antagonist that prevents the primary occurrence or recurrence of breast cancer in women, activates apoptosis of
breast cancer cells through a JNK-dependent mechanism
(39). With regard to the regulation of JNK activity, the
ability of E2 to prevent osteoclast formation in bone stems
from the inhibition of regulating receptor activation of NF-
B
ligand-induced JNK activation. This is likely to occur from a membrane
ER expressed on monocytes (74).
Localization of membrane ER.
To better understand the function of the membrane ER, we need to know
the physical structure of the receptor and where it resides within the
lipid bilayer. The endogenous receptor has not yet been isolated and
sequenced. However, we know that a variety of antibodies directed
against multiple epitopes of the nuclear ER- identify an endogenous
membrane protein in several cell types (53). In addition,
expression in CHO cells of a single cDNA for ER- results in both
membrane and nuclear pools of receptors (63). Therefore,
it appears that the membrane receptor must be very similar to the
nuclear receptor. Recent work has begun to clarify the location of this
receptor within the plasma membrane. Signaling by growth factor
receptors and non-growth factor tyrosine kinases as well as G protein
receptors occurs at least in part after localization to plasma membrane
microstructures, known as caveolae (1). This organelle
facilitates signal transduction through the localization of signaling
molecules (51), and this interaction is dependent on the
high-cholesterol content and a structural coat protein family, the
caveolins. It is believed that caveolin-1 can serve as a scaffold
protein, associating with a variety of signaling molecules to organize
their activation within the caveolae domains. Although caveolin
indirectly facilitates signaling, it may directly inhibit various
signal molecules. It is appreciated that caveolin-1 physically
associates with endothelial nitric oxide synthase (eNOS). After calcium
activation, calmodulin competitively displaces caveolin-1 from binding
to eNOS (15) and caveolin-1 moves out of the membrane
(26). These events are necessary for the activation of
eNOS. Recently, ER has been shown to localize mainly to caveolae but
also to noncaveolar fractions of the EC plasma membrane (7,
26). It is primarily within caveolae that E2
activates eNOS after E2-ER binding (7). We recently found that caveolin-1 physically associates with ERs in
several cell compartments and that caveolin may impact the ability of
ERs to both signal and localize to the plasma membrane (Razandi M,
Pedram A, and Levin ER, unpublished observations).
Complementary role of membrane and nuclear ER. Although ERs in the membrane and nuclear compartments appear to act by very different mechanisms (signaling vs. transcriptional transactivation), the cell biological roles may overlap or be complementary. As mentioned, there is precedent for E2 to activate gene transcription from both receptor pools. One may envision that kinase signaling can rapidly activate transcription, which can then be sustained by the nuclear receptor. As mentioned, the latter's action is probably facilitated by the phosphorylation of coactivator proteins, and this could result from ER signaling from the membrane. Signaling from the membrane may also amplify the actions of the nuclear receptor. Furthermore, signaling appears to play an important role in the posttranslational modification of proteins that can be upregulated in their synthesis via the nuclear receptor.
One example of this is the important anti-apoptotic protein, Bcl-2. It is well described that this gene can be activated by E2, in part through an Sp-1 site contained within the Bcl-2 promoter (59). Moreover, it has recently been shown that the survival function of Bcl-2 can be downregulated by phosphorylation within the "loop domain" of the protein (73). E2 has been shown to prevent the inactivating phosphorylation of this protein by JNK, thereby enhancing breast cancer cell survival (64). Thus the activity and concentrations of this protein are modified by discrete cellular pools of ERs; this allows both rapid and prolonged regulation of this important protein. Another example is the HSP27. Along with other family members, this protein is known to associate with ERs, especially in breast cancer (87). The HSP27 gene is an acknowledged target for nuclear ER transcriptional upregulation (60). Recently, it has been shown that the modulation of HSP27 phosphorylation occurs in response to E2 acting at membrane ER and that this is critical to the actions of E2 in ECs (65). Again, the membrane and nuclear pools of ERs have different but complementary actions to regulate the short and longer term cell biological consequences of HSP27 function.Mechanisms of signaling from the membrane.
How does the membrane ER signal? If we assume that the structure of
this protein is very similar to the nuclear receptor protein, there
does not appear to be a catalytic or kinase domain present. However,
E2 can activate a variety of signaling events, many of which functionally link to activation of G-protein-effected pathways (27, 35). For instance, E2 rapidly activates
membrane adenylate cyclase (2, 57) (often a
Gs function), whereas IP3 generation and
intracellular calcium increases are noted in a variety of cell types
(34) (often a Gq or G function).
Direct evidence that ERs can activate several G protein -subunits
and the resulting signaling comes from CHO cell membranes expressing
either ER- or ER- (63). Here, IP3 and
cAMP are rapidly generated in response to E2, associated
with the activation of Gs and Gq. Evidence of direct G protein activation in cells expressing endogenous ER,
however, has not yet been shown. Because both G proteins and ERs exist
in caveolae, it is likely that an interaction may take place within
this membrane domain. Alternatively, it has recently been reported, at
least in MCF-7 breast cancer cells expressing endogenous ER, that
E2 can activate a membrane orphan GPCR, GPR30 (16). This was reported to lead to the activation of ERK.
Curiously, these events were reported to occur independently of ER,
through an undefined mechanism. Many GPCRs have been shown to activate ERK in some cell types through the generation of heparin-binding EGF
and the subsequent activation and signaling by the EGF receptor (61). This may contribute to the ability of E2
to activate ERK, especially in MCF-7 cells (16), and would
provide an additional cross-talk mechanism for the observed
interdependence of ER and EGF receptor in modulating uterine and breast
cancer cell biology (12).
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FUTURE RESEARCH DIRECTIONS |
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TOP
ABSTRACT
INTRODUCTION
NUCLEAR RECEPTORS
MEMBRANE RECEPTORS
FUTURE RESEARCH DIRECTIONS
REFERENCES
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It is now appreciated that there are multiple pools of endogenous
ER expressed in a wide variety of target cells for E2
action. In fact, an important direction for ER research will be to
define the potential roles of the poorly understood cytosolic-
localized ER. As an anti-apoptotic factor, cytosolic
E2-ER complexes may locally regulate mitochondrial membrane
potential, In support of this idea, it has been shown that
E2 can modulate mitochondrial enzymes (88). It
will also be necessary to continue to define rapid, nongenomic actions
of E2 at the membrane receptor, establishing new signal
transduction pathways for this receptor, and to learn their impact on
cell biology (Fig. 2).
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The complementary functions of both membrane and nuclear ERs will best
be defined when specific reagents become available to activate or
antagonize one receptor but not the other. We also need to understand
the unique and overlapping functions of E2 mediated through
ER- and ER-, particularly defining the results of
heterodimerization in cells expressing both receptors. This is likely
to be relevant to both the nongenomic and genomic actions of the sex
steroid. Details of how the nuclear receptor organizes the
transcriptional apparatus to induce genes and how E2/ER
modulates histone and chromatin will be (and currently is) a topic of
much investigation. Equally important is the need to know the structure of the membrane receptor, to understand how it translocates to discrete
domains within the membrane, and to understand how it precisely induces
signal transduction. It is hoped that by modulating the function of
discrete cellular pools of ER with specific agonists/antagonists, we
might be able to avoid the unwanted effects of this sex steroid (venous
thrombosis, breast cancer promotion, and so forth) but accrue the
desirable cardiovascular, bone, and perhaps central nervous system
actions of estradiol.
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ACKNOWLEDGEMENTS |
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This work was supported by grants from the Research Service of the Department of Veterans Affairs, Avon Products Breast Cancer Research Foundation, Department of Defense Breast Cancer Research Program (Grant BC990915), and the National Heart, Lung, and Blood Institute (Grant HL-59890 to E. R. Levin).
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FOOTNOTES |
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Address for reprint requests and other correspondence: E. R. Levin, Medical Service (111-I), Long Beach VA Medical Center, 5901 E. 7th St., Long Beach, CA 90822 (E-mail: ellis.levin{at}med.va.gov).
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REFERENCES |
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INTRODUCTION
NUCLEAR RECEPTORS
MEMBRANE RECEPTORS
FUTURE RESEARCH DIRECTIONS
REFERENCES
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 J. A. Arreguin-Arevalo and T. M. Nett A Nongenomic Action of 17{beta}-Estradiol as the Mechanism Underlying the Acute Suppression of Secretion of Luteinizing Hormone Biol Reprod, July 1, 2005; 73(1): 115 - 122. [Abstract] [Full Text] [PDF]
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 C. Bolego, A. Cignarella, P. Sanvito, V. Pelosi, F. Pellegatta, L. Puglisi, and C. Pinna The Acute Estrogenic Dilation of Rat Aorta Is Mediated Solely by Selective Estrogen Receptor-{alpha} Agonists and Is Abolished by Estrogen Deprivation J. Pharmacol. Exp. Ther., June 1, 2005; 313(3): 1203 - 1208. [Abstract] [Full Text] [PDF]
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X. Guo, M. Razandi, A. Pedram, G. Kassab, and E. R. Levin Estrogen Induces Vascular Wall Dilation: MEDIATION THROUGH KINASE SIGNALING TO NITRIC OXIDE AND ESTROGEN RECEPTORS {alpha} AND {beta} J. Biol. Chem., May 20, 2005; 280(20): 19704 - 19710. [Abstract] [Full Text] [PDF]
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C. K. Osborne and R. Schiff Estrogen-Receptor Biology: Continuing Progress and Therapeutic Implications J. Clin. Oncol., March 10, 2005; 23(8): 1616 - 1622. [Full Text] [PDF]
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C. J. Fabian and B. F. Kimler Selective Estrogen-Receptor Modulators for Primary Prevention of Breast Cancer J. Clin. Oncol., March 10, 2005; 23(8): 1644 - 1655. [Full Text] [PDF]
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A. Hatzoglou, M. Kampa, C. Kogia, I. Charalampopoulos, P. A. Theodoropoulos, P. Anezinis, C. Dambaki, E. A. Papakonstanti, E. N. Stathopoulos, C. Stournaras, et al. Membrane Androgen Receptor Activation Induces Apoptotic Regression of Human Prostate Cancer Cells in Vitro and in Vivo J. Clin. Endocrinol. Metab., February 1, 2005; 90(2): 893 - 903. [Abstract] [Full Text] [PDF]
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F. Acconcia, P. Ascenzi, A. Bocedi, E. Spisni, V. Tomasi, A. Trentalance, P. Visca, and M. Marino Palmitoylation-dependent Estrogen Receptor {alpha} Membrane Localization: Regulation by 17{beta}-Estradiol Mol. Biol. Cell, January 1, 2005; 16(1): 231 - 237. [Abstract] [Full Text] [PDF]
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M. Razandi, A. Pedram, I. Merchenthaler, G. L. Greene, and E. R. Levin Plasma Membrane Estrogen Receptors Exist and Functions as Dimers Mol. Endocrinol., December 1, 2004; 18(12): 2854 - 2865. [Abstract] [Full Text] [PDF]
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 L.-M. Kow and D. W. Pfaff The membrane actions of estrogens can potentiate their lordosis behavior-facilitating genomic actions PNAS, August 17, 2004; 101(33): 12354 - 12357. [Abstract] [Full Text] [PDF]
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I. Heilmann, M. S. Pidkowich, T. Girke, and J. Shanklin From the Cover: Switching desaturase enzyme specificity by alternate subcellular targeting PNAS, July 13, 2004; 101(28): 10266 - 10271. [Abstract] [Full Text] [PDF]
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 K. Sengupta, S. Banerjee, N. K. Saxena, and S. K. Banerjee Thombospondin-1 Disrupts Estrogen-Induced Endothelial Cell Proliferation and Migration and Its Expression Is Suppressed by Estradiol Mol. Cancer Res., March 1, 2004; 2(3): 150 - 158. [Abstract] [Full Text] [PDF]
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 P. N. Hopkins and E. A. Brinton Estrogen Receptor 1 Variants and Coronary Artery Disease: Shedding Light Into a Murky Pool JAMA, November 5, 2003; 290(17): 2317 - 2319. [Full Text] [PDF]
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J. Qiu, M. A. Bosch, S. C. Tobias, D. K. Grandy, T. S. Scanlan, O. K. Ronnekleiv, and M. J. Kelly Rapid Signaling of Estrogen in Hypothalamic Neurons Involves a Novel G-Protein-Coupled Estrogen Receptor that Activates Protein Kinase C J. Neurosci., October 22, 2003; 23(29): 9529 - 9540. [Abstract] [Full Text] [PDF]
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J. K. Wong, H. H. Le, A. Zsarnovszky, and S. M. Belcher Estrogens and ICI182,780 (Faslodex) Modulate Mitosis and Cell Death in Immature Cerebellar Neurons via Rapid Activation of p44/p42 Mitogen-Activated Protein Kinase J. Neurosci., June 15, 2003; 23(12): 4984 - 4995. [Abstract] [Full Text] [PDF]
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S. Balasenthil and R. K. Vadlamudi Functional Interactions between the Estrogen Receptor Coactivator PELP1/MNAR and Retinoblastoma Protein J. Biol. Chem., June 6, 2003; 278(24): 22119 - 22127. [Abstract] [Full Text] [PDF]
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B. D. Boyan, V. L. Sylvia, T. Frambach, C. H. Lohmann, J. Dietl, D. D. Dean, and Z. Schwartz Estrogen-Dependent Rapid Activation of Protein Kinase C in Estrogen Receptor-Positive MCF-7 Breast Cancer Cells and Estrogen Receptor-Negative HCC38 Cells Is Membrane-Mediated and Inhibited by Tamoxifen Endocrinology, May 1, 2003; 144(5): 1812 - 1824. [Abstract] [Full Text] [PDF]
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P. A. Orihuela, A. Parada-Bustamante, P. P. Cortes, C. Gatica, and H. B. Croxatto Estrogen Receptor, Cyclic Adenosine Monophosphate, and Protein Kinase A Are Involved in the Nongenomic Pathway by Which Estradiol Accelerates Oviductal Oocyte Transport in Cyclic Rats Biol Reprod, April 1, 2003; 68(4): 1225 - 1231. [Abstract] [Full Text] [PDF]
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V. Znamensky, K. T. Akama, B. S. McEwen, and T. A. Milner Estrogen Levels Regulate the Subcellular Distribution of Phosphorylated Akt in Hippocampal CA1 Dendrites J. Neurosci., March 15, 2003; 23(6): 2340 - 2347. [Abstract] [Full Text] [PDF]
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C. B. Wade and D. M. Dorsa Estrogen Activation of Cyclic Adenosine 5'-Monophosphate Response Element-Mediated Transcription Requires the Extracellularly Regulated Kinase/Mitogen-Activated Protein Kinase Pathway Endocrinology, March 1, 2003; 144(3): 832 - 838. [Abstract] [Full Text] [PDF]
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M. Razandi, A. Pedram, S. T. Park, and E. R. Levin Proximal Events in Signaling by Plasma Membrane Estrogen Receptors J. Biol. Chem., January 17, 2003; 278(4): 2701 - 2712. [Abstract] [Full Text] [PDF]
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S.A. Adeoya-Osiguwa, S. Markoulaki, V. Pocock, S.R. Milligan, and L.R. Fraser 17{beta}-Estradiol and environmental estrogens significantly affect mammalian sperm function Hum. Reprod., January 1, 2003; 18(1): 100 - 107. [Abstract] [Full Text] [PDF]
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A. Pedram, M. Razandi, M. Aitkenhead, C. C. W. Hughes, and E. R. Levin Integration of the Non-genomic and Genomic Actions of Estrogen. MEMBRANE-INITIATED SIGNALING BY STEROID TO TRANSCRIPTION AND CELL BIOLOGY J. Biol. Chem., December 20, 2002; 277(52): 50768 - 50775. [Abstract] [Full Text] [PDF]
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 K. J. Ho and J. K. Liao Nonnuclear Actions of Estrogen Arterioscler Thromb Vasc Biol, December 1, 2002; 22(12): 1952 - 1961. [Abstract] [Full Text] [PDF]
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 D. M. Brownson, N. G. Azios, B. K. Fuqua, S. F. Dharmawardhane, and T. J. Mabry Flavonoid Effects Relevant to Cancer J. Nutr., November 1, 2002; 132(11): 3482S - 3489. [Abstract] [Full Text] [PDF]
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