scholarly journals Expression and Regulation of CD73 during the Estrous Cycle in Mouse Uterus

2021 ◽  
Vol 22 (17) ◽  
pp. 9403
Author(s):  
Jihyun Lee ◽  
Haeun Park ◽  
Sohyeon Moon ◽  
Jeong-Tae Do ◽  
Kwonho Hong ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Progesterone Receptor ◽  
Immune Responses ◽  
Estrous Cycle ◽  
Mouse Uterus ◽  
Ovariectomized Mice ◽  
Uterine Environment ◽  
Cd73 Expression ◽  
Cluster Of Differentiation ◽  
Antagonist Ru486

Cluster of differentiation 73 (CD73, also known as ecto-5′-nucleotidase) is an enzyme that converts AMP into adenosine. CD73 is a surface enzyme bound to the outside of the plasma membrane expressed in several cells and regulates immunity and inflammation. In particular, it is known to inhibit T cell-mediated immune responses. However, the regulation of CD73 expression by hormones in the uterus is not yet clearly known. In this study, we investigated the expression of CD73 in ovariectomized mice treated with estrogen or progesterone and its regulation in the mouse uterus during the estrous cycle. The level of CD73 expression was dynamically regulated in the uterus during the estrous cycle. CD73 protein expression was high in proestrus, estrus, and diestrus, whereas it was relatively low in the metestrus stage. Immunofluorescence revealed that CD73 was predominantly expressed in the cytoplasm of the luminal and glandular epithelium and the stroma of the endometrium. The expression of CD73 in ovariectomized mice was gradually increased by progesterone treatment. However, estrogen injection did not affect its expression. Moreover, CD73 expression was increased when estrogen and progesterone were co-administered and was inhibited by the pretreatment of the progesterone receptor antagonist RU486. These findings suggest that the expression of CD73 is dynamically regulated by estrogen and progesterone in the uterine environment, and that there may be a synergistic effect of estrogen and progesterone.

scholarly journals BIRC5 Expression Is Regulated in Uterine Epithelium during the Estrous Cycle

Genes ◽  
2020 ◽  
Vol 11 (3) ◽  
pp. 282
Author(s):  
Minha Cho ◽  
Ok-Hee Lee ◽  
Eun Mi Chang ◽  
Sujin Lee ◽  
Sohyeon Moon ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Estrous Cycle ◽  
Pcr Analysis ◽  
Inhibitor Of Apoptosis ◽  
Rt Pcr ◽  
Mouse Uterus ◽  
Differentiated Cells ◽  
Ovariectomized Mice ◽  
Antagonist Ru486 ◽  
Cell Division Control

Baculoviral inhibitor of apoptosis repeat-containing 5 (Birc5), also known as survivin, is a member of the inhibitor of apoptosis (IAP) family of proteins and regulates the size of tissues through cell division control. The uterus is the most dynamically sized organ among tissues during the estrous cycle. Although Birc5 is expressed in some terminally differentiated cells, the regulation of its expression in the uterus remains unknown. We investigated the regulation of Birc5 expression in the mouse uterus. RT-PCR analysis showed that Birc5 was expressed in various tissues, including the uterus; the expression level of Birc5 was significantly higher at the diestrus stage. Immunohistochemistry and Western blotting analysis revealed that Birc5 was more active in luminal and glandular epithelium than in endometrial stroma. In ovariectomized mice, Birc5 expression in the uterus was gradually increased by estrogen treatment; however, progesterone injection decreased its expression. Estrogen-induced Birc5 expression was blocked by treatment with estrogen receptor antagonist, ICI 182, 780 and progesterone-reduced Birc5 expression was inhibited by the progesterone receptor antagonist RU486. These results suggest that Birc5 expression is dynamically regulated by a combination of estrogen and progesterone via their receptor-mediated signaling.

Hormonal modulation of prolyl endopeptidase and dipeptidyl peptidase IV activities in the mouse uterus and ovary

1992 ◽  
Vol 127 (3) ◽  
pp. 262-266 ◽  
Author(s):  
Naoshi Ohta ◽  
Takayuki Takahashi ◽  
Takao Mori ◽  
Min Kyun Park ◽  
Seiichiro Kawashima ◽  
...  
Keyword(s):  
Estrous Cycle ◽  
Marked Change ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Prolyl Endopeptidase ◽  
Dopamine Antagonist ◽  
Mouse Uterus ◽  
Ovariectomized Mice ◽  
Endopeptidase Activity ◽  
Hormonal Modulation

Prolyl endopeptidase and dipeptidyl peptidase IV are proline-specific peptidases, and are ubiquitously distributed in various tissues in mammals. The specific activities of these peptidases in both uterus and ovary were examined in the SHN strain of mice at estrus or diestrus. A marked change in prolyl endopeptidase activity was found in the uterus and ovary in intact mice during the estrous cycle, the activity being high at estrus and low at diestrus. In ovariectomized mice, prolyl endopeptidase activity was significantly higher in the uterus treated with progesterone or estradiol than in the uterus treated with vehicle oil only or a dopamine antagonist (perphenazine) which stimulates prolactin secretion. On the other hand, notable change in dipeptidyl peptidase IV activity during the estrous cycle was found only in the uterus of intact mice. The activity was low at estrus and high at diestrus. In ovariectomized mice, the uterus exposed to estradiol showed a lower dipeptidyl peptidase IV activity than the uteri treated with progesterone, the dopamine antagonist or vehicle oil. These findings reveal that there is a close correlation between the circulating level of ovarian steroids and the activities of these prolinespecific enzymes.

scholarly journals Research Resource: Genome-Wide Profiling of Progesterone Receptor Binding in the Mouse Uterus

2012 ◽  
Vol 26 (8) ◽  
pp. 1428-1442 ◽  
Author(s):  
Cory A. Rubel ◽  
Rainer B. Lanz ◽  
Ramakrishna Kommagani ◽  
Heather L. Franco ◽  
John P. Lydon ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Progesterone Receptor ◽  
Binding Sites ◽  
Molecular Mechanisms ◽  
Target Genes ◽  
Massively Parallel Sequencing ◽  
Mouse Uterus ◽  
Ovariectomized Mice ◽  
Genome Wide ◽  
Uterine Function

Progesterone (P4) signaling through its nuclear transcription factor, the progesterone receptor (PR), is essential for normal uterine function. Although deregulation of PR-mediated signaling is known to underscore uterine dysfunction and a number of endometrial pathologies, the early molecular mechanisms of this deregulation are unclear. To address this issue, we have defined the genome-wide PR cistrome in the murine uterus using chromatin immunoprecipitation (ChIP) followed by massively parallel sequencing (ChIP-seq). In uteri of ovariectomized mice, we identified 6367 PR-binding sites in the absence of P4 ligand; however, this number increased at nearly 3-fold (18,432) after acute P4 exposure. Sequence analysis revealed that approximately 73% of these binding sites contain a progesterone response element or a half-site motif recognized by the PR. Many previously identified P4 target genes known to regulate uterine function were found to contain PR-binding sites, confirming the validity of our methodology. Interestingly, when the ChIP-seq data were coupled with our microarray expression data, we identified a novel regulatory role for uterine P4 in circadian rhythm gene expression, thereby uncovering a hitherto unexpected new circadian biology for P4 in this tissue. Further mining of the ChIP-seq data revealed Sox17 as a direct transcriptional PR target gene in the uterus. As a member of the Sox transcription factor family, Sox17 represents a potentially novel mediator of PR action in the murine uterus. Collectively, our first line of analysis of the uterine PR cistrome provides the first insights into the early molecular mechanisms that underpin normal uterine responsiveness to acute P4 exposure. Future analysis promises to reveal the PR interactome and, in turn, potential therapeutic targets for the diagnosis and/or treatment of endometrial dysfunction.

scholarly journals Secreted phosphoprotein 1 (osteopontin) is expressed by stromal macrophages in cyclic and pregnant endometrium of mice, but is induced by estrogen in luminal epithelium during conceptus attachment for implantation

Reproduction ◽  
2006 ◽  
Vol 132 (6) ◽  
pp. 919-929 ◽  
Author(s):  
Frankie J White ◽  
Robert C Burghardt ◽  
Jianbo Hu ◽  
Margaret M Joyce ◽  
Thomas E Spencer ◽  
...  
Keyword(s):  
Estrous Cycle ◽  
Immune Cells ◽  
Luminal Epithelium ◽  
Apical Surface ◽  
Wild Type ◽  
Mouse Uterus ◽  
Ovariectomized Mice ◽  
Vaginal Plug ◽  
Secreted Phosphoprotein 1

Secreted phosphoprotein 1 (SPP1, osteopontin) is the most highly upregulated extracellular matrix/adhesion molecule/cytokine in the receptive phase human uterus, and Spp1 null mice manifest decreased pregnancy rates during mid-gestation as compared with wild-type counterparts. We hypothesize that Spp1 is required for proliferation, migration, survival, adhesion, and remodeling of cells at the conceptus–maternal interface. Our objective was to define the temporal/spatial distribution and steroid regulation of Spp1 in mouse uterus during estrous cycle and early gestation.In situhybridization localizedSpp1to luminal epithelium (LE) and immune cells. LE expression was prominent at proestrus, decreased by estrus, and was nearly undetectable at diestrus. During pregnancy,Spp1mRNA was not detected in LE until day 4.5 (day 1 = vaginal plug).Spp1-expressing immune cells were scattered within the endometrial stroma throughout the estrous cycle and early pregnancy. Immunoreactive Spp1 was prominent at the apical LE surface by day 4.5 of pregnancy and Spp1 protein was also co-localized with subsets of CD45-positive (leukocytes) and F4/80-positive (macrophages) cells. In ovariectomized mice, estrogen, but not progesterone, inducedSpp1mRNA, whereas estrogen plus progesterone did not induceSpp1in LE. These results establish that estrogen regulates Spp1 in mouse LE and are the first to identify macrophages that produce Spp1 within the peri-implantation endometrium of any species. We suggest that Spp1 at the apical surface of LE provides a mechanism to bridge conceptus to LE during implantation, and that Spp1-positive macrophages within the stroma may be involved in uterine remodeling for conceptus invasion.

Inhibition of TMEM16A impedes embryo implantation and decidualization in mice

Reproduction ◽  
2018 ◽  
Author(s):  
Qianrong Qi ◽  
Yifan Yang ◽  
Kailin Wu ◽  
Qingzhen Xie
Keyword(s):  
Progesterone Receptor ◽  
Stromal Cells ◽  
Embryo Implantation ◽  
Mouse Uterus ◽  
Endometrial Stromal Cells ◽  
Uterine Endometrium ◽  
Molecule Inhibitor ◽  
Pathway Inhibition ◽  
And Function ◽  
Reproductive Processes

Recent studies revealed that TMEM16A is involved in several reproductive processes, including ovarian estrogen secretion and ovulation, sperm motility and acrosome reaction, fertilization, and myometrium contraction. However, little is known about the expression and function of TMEM16A in embryo implantation and decidualization. In this study, we focused on the expression and regulation of TMEM16A in mouse uterus during early pregnancy. We found that TMEM16A is up-regulated in uterine endometrium in response to embryo implantation and decidualization. Progesterone treatment could induce TMEM16A expression in endometrial stromal cells through progesterone receptor/c-Myc pathway, which is blocked by progesterone receptor antagonist or the inhibitor of c-Myc signaling pathway. Inhibition of TMEM16A by small molecule inhibitor (T16Ainh-A01) resulted in impaired embryo implantation and decidualization in mice. Treatment with either specific siRNA of Tmem16a or T16Ainh-A01 inhibited the decidualization and proliferation of mouse endometrial stromal cells. In conclusion, our results revealed that TMEM16A is involved in embryo implantation and decidualization in mice, compromised function of TMEM16A may lead to impaired embryo implantation and decidualization.

scholarly journals With an Ear up Against the Wall: An Update on Mechanoperception in Arabidopsis.

Plants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1587
Author(s):  
Sara Behnami ◽  
Dario Bonetta
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Immune Responses ◽  
Mechanical Stress ◽  
Mechanosensitive Channels ◽  
Compensatory Responses ◽  
Cell Wall Damage ◽  
Mechanical Signals ◽  
Hormone Signalling

Cells interpret mechanical signals and adjust their physiology or development appropriately. In plants, the interface with the outside world is the cell wall, a structure that forms a continuum with the plasma membrane and the cytoskeleton. Mechanical stress from cell wall damage or deformation is interpreted to elicit compensatory responses, hormone signalling, or immune responses. Our understanding of how this is achieved is still evolving; however, we can refer to examples from animals and yeast where more of the details have been worked out. Here, we provide an update on this changing story with a focus on candidate mechanosensitive channels and plasma membrane-localized receptors.

scholarly journals Plasma Membrane Calcium ATPase Regulates Stoichiometry of CD4+ T-Cell Compartments

2021 ◽  
Vol 12 ◽  
Author(s):  
Maylin Merino-Wong ◽  
Barbara A. Niemeyer ◽  
Dalia Alansary
Keyword(s):  
Plasma Membrane ◽  
T Cell ◽  
Immune Responses ◽  
Chromatin Immunoprecipitation ◽  
Expression Patterns ◽  
Calcium Atpase ◽  
Cd4 T Cell ◽  
Plasma Membrane Calcium Atpase ◽  
Cell Compartments

Immune responses involve mobilization of T cells within naïve and memory compartments. Tightly regulated Ca2+ levels are essential for balanced immune outcomes. How Ca2+ contributes to regulating compartment stoichiometry is unknown. Here, we show that plasma membrane Ca2+ ATPase 4 (PMCA4) is differentially expressed in human CD4+ T compartments yielding distinct store operated Ca2+ entry (SOCE) profiles. Modulation of PMCA4 yielded a more prominent increase of SOCE in memory than in naïve CD4+ T cell. Interestingly, downregulation of PMCA4 reduced the effector compartment fraction and led to accumulation of cells in the naïve compartment. In silico analysis and chromatin immunoprecipitation point towards Ying Yang 1 (YY1) as a transcription factor regulating PMCA4 expression. Analyses of PMCA and YY1 expression patterns following activation and of PMCA promoter activity following downregulation of YY1 highlight repressive role of YY1 on PMCA expression. Our findings show that PMCA4 adapts Ca2+ levels to cellular requirements during effector and quiescent phases and thereby represent a potential target to intervene with the outcome of the immune response.

scholarly journals Dynamic accumulation of a helper NLR at the plant-pathogen interface underpins pathogen recognition

2021 ◽  
Author(s):  
Cian Duggan ◽  
Eleonora Moratto ◽  
Zachary Savage ◽  
Eranthika Hamilton ◽  
Hiroaki Adachi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Immune Responses ◽  
Subcellular Localization ◽  
Plant Pathogen ◽  
Coiled Coil ◽  
Dynamic Changes ◽  
Pathogen Effectors ◽  
Mediate Response ◽  
Potato Famine ◽  
Irish Potato Famine

Plants employ sensor-helper pairs of NLR immune receptors to recognize pathogen effectors and activate immune responses. Yet the subcellular localization of NLRs pre- and post- activation during pathogen infection remains poorly known. Here we show that NRC4, from the 'NRC' solanaceous helper NLR family, undergoes dynamic changes in subcellular localization by shuttling to and from the plant-pathogen haustorium interface established during infection by the Irish potato famine pathogen Phytophthora infestans. Specifically, prior to activation, NRC4 accumulates at the extra-haustorial membrane (EHM), presumably to mediate response to perihaustorial effectors, that are recognized by NRC4-dependent sensor NLRs. However not all NLRs accumulate at the EHM, as the closely related helper NRC2, and the distantly related ZAR1, did not accumulate at the EHM. NRC4 required an intact N- terminal coiled coil domain to accumulate at the EHM, whereas the functionally conserved MADA motif implicated in cell death activation and membrane insertion was dispensable for this process. Strikingly, a constitutively autoactive NRC4 mutant did not accumulate at the EHM and showed punctate distribution that mainly associated with the plasma membrane, suggesting that post-activation, NRC4 probably undergoes a conformation switch to form clusters that do not preferentially associate with the EHM. When NRC4 is activated by a sensor NLR during infection however, NRC4 formed puncta mainly at the EHM and to a lesser extent at the plasma membrane. We conclude that following activation at the EHM, NRC4 may spread to other cellular membranes from its primary site of activation to trigger immune responses.

HYPERTROPHY AND HYPERPLASIA IN THE MOUSE UTERUS AFTER OESTROGEN TREATMENT: AN AUTORADIOGRAPHIC STUDY

1973 ◽  
Vol 56 (1) ◽  
pp. 133-NP ◽  
Author(s):  
L. MARTIN ◽  
C. A. FINN ◽  
GAIL TRINDER
Keyword(s):  
Cell Death ◽  
Dna Synthesis ◽  
Proliferative Response ◽  
Autoradiographic Study ◽  
Luminal Epithelium ◽  
Uterine Tissue ◽  
Mouse Uterus ◽  
Oestrogen Treatment ◽  
Ovariectomized Mice

SUMMARY The uteri of untreated ovariectomized mice consisted almost entirely of myometrium and connective tissue stroma. After oestrogenic stimulation these tissues underwent marked hypertrophy, but showed little proliferation. The luminal epithelium underwent marked hyperplasia, with most cells dividing twice to quadruple cell numbers by 35–40 h, when they made up 10–12% of the uterine tissue volume and 20% of the total uterine cell population. The proliferative response was rapid, highly synchronized and short-lived. The number of cells incorporating [3H]thymidine first increased 8·5 h after oestradiol-17β and by 13–16 h 60–70% were engaged in DNA synthesis. Up to 21 h cell-death was minimal. From 21 h onwards the proliferation rate declined and the rate of cell death increased. A second injection of oestrogen prevented the rise in death rate and produced a second smaller burst of DNA synthesis. Cells in DNA synthesis or mitosis were insensitive to oestrogen. A smaller proliferative response occurred in the glands: only 25% of cells entered DNA synthesis after the first injection of oestradiol and none after the second. Gland cells appeared to die in situ and there was no evidence that they migrated into the luminal epithelium.

Sign in / Sign up

Export Citation Format

Share Document