scholarly journals Participation of membrane progesterone receptor α in the inhibitory effect of progesterone on prolactin secretion

2018 ◽  
Vol 30 (9) ◽  
pp. e12614 ◽  
Author(s):  
M. A. Camilletti ◽  
J. Ferraris ◽  
A. Abeledo-Machado ◽  
A. Converse ◽  
E. Y. Faraoni ◽  
...  
Keyword(s):  
Progesterone Receptor ◽  
Inhibitory Effect ◽  
Prolactin Secretion ◽  
Membrane Progesterone Receptor

Deciphering the role of PGRMC1 during human decidualization using an in vitro approach

2021 ◽  
Author(s):  
Stefania Salsano ◽  
Roberto González-Martín ◽  
Alicia Quiñonero ◽  
Silvia Pérez-Debén ◽  
Francisco Domínguez
Keyword(s):  
Progesterone Receptor ◽  
Intracellular Transport ◽  
Transcriptional Profiling ◽  
Molecular Transport ◽  
In Silico Analysis ◽  
Prolactin Secretion ◽  
Mitochondrial Activity ◽  
Endometrial Stromal Cells ◽  
Membrane Progesterone Receptor

Abstract Context Non-classical membrane progesterone receptor (mPRs) and PGRMC1 expression have been detected in endometrium, but their role in decidualization was not yet investigated. We previously demonstrated PGRMC1 downregulation in receptive endometrium and that its overexpression inhibits decidualization. Furthermore, during decidualization, PGRMC1 mainly interacts with proteins involved in biosynthesis, intracellular transport and mitochondrial activity. Objective To determine PGRMC1 and mPRs signaling role during decidualization. Design and Interventions Isolated primary endometrial stromal cells (EnSC) were in vitro decidualized in presence of classic stimuli (E2+P4), PGRMC1 inhibitor (AG205), or membrane-impermeable P4 (P4-BSA). Setting and Participants Endometrial biopsies from 19 fertile oocyte donors attending IVI-Valencia IVF clinic. Main Outcome Measure(s) EnSC decidualization was evaluated by prolactin ELISA and F-actin immunostaining. Progesterone receptor localization was evaluated by immunofluorescence. EnSC transcriptomic profiles were analyzed by microarray technology. Result(s) PGRMC1 inhibition during EnSC decidualization (AG205dEnSC) does not interfere with EnSC cytoskeletal rearrangements and prolactin secretion. However, global transcriptional profiling revealed more differentially expressed genes in AG205dEnSC than in dEnSC, compared with non-decidualized EnSC (ndEnSC). In silico analysis showed that PGRMC1 inhibition upregulated more genes related to metabolism, molecular transport, and hormonal biosynthesis compared to control dEnSC. EnSC decidualized in the presence of P4-BSA showed a similar behavior as ndEnSC in terms of morphological features, absence of prolactin secretion, and transcriptomic pattern. Conclusion(s) Our findings associate PGRMC1 to hormonal biosynthesis, metabolism, and vesicular transport—important cellular functions for dEnSC supporting pregnancy. Activation of membrane P4 receptor signaling alone was unable to induce downstream effects needed for proper decidualization.

Long term exposure to dopamine reverses the inhibitory effect of endothelin-1 on prolactin secretion.

Endocrinology ◽  
1995 ◽  
Vol 136 (3) ◽  
pp. 990-994 ◽  
Author(s):  
B Kanyicska ◽  
J D Livingstone ◽  
M E Freeman
Keyword(s):  
Inhibitory Effect ◽  
Prolactin Secretion ◽  
Endothelin 1

scholarly journals Non-genomic progesterone receptors in the mammalian ovary: some unresolved issues

Reproduction ◽  
2003 ◽  
pp. 3-15 ◽  
Author(s):  
T Bramley
Keyword(s):  
Progesterone Receptor ◽  
Steroid Receptors ◽  
Surface Membrane ◽  
Progesterone Receptors ◽  
Signalling Pathways ◽  
Mediated Effects ◽  
Genomic Effects ◽  
Vitamin D 3 ◽  
Membrane Progesterone Receptor ◽  
Different Tissues

In addition to their well-documented genomic effects, steroid hormones may also exert actions that are: (i) rapid, (ii) insensitive to inhibitors of transcription, (iii) mimicked by steroids coupled to cell membrane-impermeant molecules, and (iv) demonstrable in cells that do not express the classic genomic progesterone receptor (gPR). Such 'non-genomic' effects have been described for all the major classes of steroids (progesterone, oestrogens, androgens and corticoids), as well as for thyroid hormones, retinoids and vitamin D(3). Rapid, membrane-mediated effects of progesterone have been studied most intensively in human spermatozoa and in the Xenopus oocyte. However, similar non-genomic actions of progesterone and other steroids have now been described in a wide variety of different tissues in many species. The first putative membrane steroid receptor to be cloned was that for the pig membrane progesterone receptor (mPR). Subsequently, similar genes were cloned from rats and cattle, and two related mPRs have been described in humans. Despite accumulating evidence for cell-surface membrane actions of steroids, a number of uncertainties remain as to the properties and identity of such 'receptors' and their cellular actions. Furthermore, some rapid steroid effects may be mediated through membrane-associated 'classical' steroid receptors, and steroid receptors may be capable of activating other signalling pathways non-classically. This review focuses on some of these unresolved issues, taking as its model the actions of progesterone in the mammalian ovary.

scholarly journals SUN-559 Involvement of Sarco/Endoplasmic Reticulum Ca- ATPase (SERCA) in Membrane Progesterone Receptor Alpha (PAQR7)-Mediated Progesterone Induction of Vascular Smooth Muscle Relaxation

2020 ◽  
Vol 4 (Supplement_1) ◽  
Author(s):  
Yefei Pang ◽  
Peter Thomas
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Muscle ◽  
Progesterone Receptor ◽  
Protein Expression ◽  
Signaling Pathways ◽  
Muscle Relaxation ◽  
Critical Role ◽  
Akt Signaling ◽  
Membrane Progesterone Receptor ◽  
Membrane Progesterone Receptor Alpha

Abstract Progesterone (P4) exerts multiple beneficial effects on the human cardiovascular system through its actions on vascular endothelial cells and also by acting directly on vascular smooth muscle cells (VSMCs). Membrane progesterone receptor alpha (mPRα) has been shown to mediate the rapid P4-induction of human VSMC relaxation through activation of MAPK, Akt/Pi3k and RhoA/ROCK signaling pathways and the resulting reduction of calcium influx through calcium channels. In this study, we demonstrate that treatment of cultured human VSMCs with P4 for 1-2 hours increases both the mRNA and protein expression of sarco/endoplasmic reticulum Ca- ATPase (SERCA), the major transporter of calcium from the cytosol into the sarcoplasmic reticulum (SR) during muscle relaxation. Knockdown of mPRα with siRNA completely blocked this stimulatory effect of P4 as well as that of OD 02-0, a mPR selective agonist, on SERCA protein expression. In contrast, expression levels of phospholamban (PLB), a SR protein that reversibly inhibits SERCA were downregulated by this P4 treatment, and mRNA expression of a channel that releases calcium from the SR, inositol trisphosphate receptor (IP3R), was unaltered after treatment with P4. Moreover, treatments with P4 and OD 02-0, but not with R5020, a nuclear PR agonist, increased PLB phosphorylation, which would result in disinhibition of SERCA function. P4 and OD 02-0 significantly increased calcium levels in the SR detected with Fluo-5N, a specific SR calcium indicator, and caused VSMC relaxation. These effects were blocked by cyclopiazonic acid (CPA, a SERCA inhibitor), suggesting that SERCA plays a critical role in P4 induction of VSMC relaxation. Similarly, the effects of P4 and OD 02-0 on relaxation of umbilical artery rings measured with a myograph were significantly attenuated by CPA, which confirms the critical role of SERCA in the rapid action of P4 and 02-0 on vascular muscle relaxation. P4 has previously been shown to activate MAPK and Akt signaling pathways to induce VSMC relaxation. The P4- and OD 02-0-induced increases in calcium in the SR were blocked by MAPK and Akt/Pi3k signaling inhibitors, AZD6244 and wortmannin. Taken together, these results suggest that the direct, rapid effects of P4 on relaxation of VSMCs through mPRα involves regulation of the expression and function of the SR proteins SERCA and PLB through MAPK and Akt signaling pathways.

Approaches to the design of selective ligands for membrane progesterone receptor alpha

2013 ◽  
Vol 78 (3) ◽  
pp. 236-243 ◽  
Author(s):  
O. V. Lisanova ◽  
T. A. Shchelkunova ◽  
I. A. Morozov ◽  
P. M. Rubtsov ◽  
I. S. Levina ◽  
...  
Keyword(s):  
Progesterone Receptor ◽  
Receptor Alpha ◽  
Selective Ligands ◽  
Membrane Progesterone Receptor ◽  
Membrane Progesterone Receptor Alpha

scholarly journals Progesterone-induced activation of membrane-bound progesterone receptors in murine macrophage cells

2014 ◽  
Vol 224 (2) ◽  
pp. 183-194 ◽  
Author(s):  
Jing Lu ◽  
Joshua Reese ◽  
Ying Zhou ◽  
Emmet Hirsch
Keyword(s):  
Progesterone Receptor ◽  
Inflammatory Responses ◽  
Progesterone Receptors ◽  
Murine Macrophage ◽  
Induced Expression ◽  
Receptor Alpha ◽  
Downstream Target ◽  
Macrophage Cells ◽  
Membrane Progesterone Receptor ◽  
Membrane Progesterone Receptor Alpha

Parturition is an inflammatory process mediated to a significant extent by macrophages. Progesterone (P4) maintains uterine quiescence in pregnancy, and a proposed functional withdrawal of P4 classically regulated by nuclear progesterone receptors (nPRs) leads to labor. P4 can affect the functions of macrophages despite the reported lack of expression of nPRs in these immune cells. Therefore, in this study we investigated the effects of the activation of the putative membrane-associated PR on the function of macrophages (a key cell for parturition) and discuss the implications of these findings for pregnancy and parturition. In murine macrophage cells (RAW 264.7), activation of mPRs by P4 modified to be active only extracellularly by conjugation to BSA (P4BSA, 1.0×10−7 mol/l) caused a pro-inflammatory shift in the mRNA expression profile, with significant upregulation of the expression of cyclooxygenase 2 (COX2 (Ptgs2)), Il1B, and Tnf and downregulation of membrane progesterone receptor alpha (Paqr7) and oxytocin receptor (Oxtr). Pretreatment with PD98059, a MEK1/2 inhibitor, significantly reduced P4BSA-induced expression of mRNA of Il1B, Tnf, and Ptgs2. Inhibition of protein kinase A (PKA) by H89 blocked P4BSA-induced expression of Il1B and Tnf mRNA. P4BSA induced rapid phosphorylation of MEK1/2 and CREB (a downstream target of PKA). This phosphorylation was inhibited by pretreatment with PD98059 and H89, respectively, revealing that MEK1/2 and PKA are two of the components involved in mPR signaling. Taken together, these results indicate that changes in membrane progesterone receptor alpha expression and signaling in macrophages are associated with the inflammatory responses; and that these changes might contribute to the functional withdrawal of P4 related to labor.

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