Purinergic Receptor Expression and Activation in First Trimester and Term Human Placenta

Placenta ◽  
2007 ◽  
Vol 28 (4) ◽  
pp. 339-347 ◽  
Author(s):  
V.H.J. Roberts ◽  
L.H. Waters ◽  
T. Powell
Keyword(s):  
Human Placenta ◽  
Purinergic Receptor ◽  
First Trimester ◽  
Receptor Expression

scholarly journals Pregnancy-enhanced Ca2+ responses to ATP in uterine artery endothelial cells is due to greater capacitative Ca2+ entry rather than altered receptor coupling

2006 ◽  
Vol 190 (2) ◽  
pp. 373-384 ◽  
Author(s):  
Shannon M Gifford ◽  
Fu-Xian Yi ◽  
Ian M Bird
Keyword(s):  
Endothelial Cells ◽  
Uterine Artery ◽  
Purinergic Receptor ◽  
Cell Types ◽  
P2y Receptors ◽  
Receptor Expression ◽  
Receptor Subtype ◽  
Initial Transient ◽  
Receptor Coupling ◽  
Specific Variation

Uterine artery endothelial cells (UAEC) derived from pregnant (P-UAEC) and nonpregnant (NP-UAEC) ewes retain pregnancy-specific differences in cell signaling as well as vasodilator production through passage 4. In particular, when P- and NP-UAEC are stimulated with ATP over a 2.5 min recording period, they exhibit similar initial transient peaks in the intracellular free Ca2+ concentration ([Ca2+]i), but the P-UAEC show a heightened sustained phase. In order to establish whether thiswas due to an altered subclass of purinergic receptor (P2), both the dose dependencyof [Ca2+]i responses to ADP and UTP and the profile of purinergic receptor expression are determined in NP- and P-UAEC. Our findings indicate that while several isoforms of P2X and P2Y receptors are present, it is P2Y2 that is responsible for the ATP-induced initial transient peak in both cell types. We also characterized several key components of the ATP-induced Ca2+ signaling cascade, including the inositol 1,4,5-trisphosphate receptor and G-proteins, but could not confirm any pregnancy-specific variation in the protein expression that correlated with pregnancy-specific differences in prolonged Ca2+ signaling. We thus investigated whether such a difference may be inherent to the cell itself rather than specific to the purinergic receptor-signaling pathway. Using thapsigargin (Tg), we were able to demonstrate that the initial Tg-sensitive intracellular pool of Ca2+is nearly identical with the capacity in both cell types, but the P-UAEC is nonetheless capable of greater capacitative Ca2+ entry (CCE) than NP-UAEC. Furthermore, CCE induced by Tg could be dramatically inhibited by 2-aminoethoxydiphenyl borate, suggesting a role for store-operated channels in the ATP-induced [Ca2+]i response. We conclude that changes at the level of capacitative entry mechanisms rather than switching of receptor subtype or coupling to phospholipase C underlies pregnancy adaptation of UAEC at the level of Ca2+signaling.

scholarly journals Glucocorticoids modulate multidrug resistance transporters in the first trimester human placenta

2018 ◽  
Vol 22 (7) ◽  
pp. 3652-3660 ◽  
Author(s):  
Phetcharawan Lye ◽  
Enrrico Bloise ◽  
Lubna Nadeem ◽  
William Gibb ◽  
Stephen J. Lye ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Human Placenta ◽  
First Trimester ◽  
Multidrug Resistance Transporters

scholarly journals The Impact of Cold Storage on Adenosine Diphosphate-Mediated Platelet Responsiveness

TH Open ◽  
2020 ◽  
Vol 04 (03) ◽  
pp. e163-e172
Author(s):  
Juergen Koessler ◽  
Philipp Klingler ◽  
Marius Niklaus ◽  
Katja Weber ◽  
Angela Koessler ◽  
...  
Keyword(s):  
Cold Storage ◽  
Whole Blood ◽  
Room Temperature ◽  
Purinergic Receptor ◽  
Adenosine Diphosphate ◽  
Receptor Expression ◽  
Activation Markers ◽  
Inhibitory Pathways ◽  
The Impact ◽  
Induced Aggregation

Abstract Introduction Cold storage of platelets is considered to contribute to lower risk of bacterial growth and to more efficient hemostatic capacity. For the optimization of storage strategies, it is required to further elucidate the influence of refrigeration on platelet integrity. This study focused on adenosine diphosphate (ADP)-related platelet responsiveness. Materials and Methods Platelets were prepared from apheresis-derived platelet concentrates or from peripheral whole blood, stored either at room temperature or at 4°C. ADP-induced aggregation was tested with light transmission. Activation markers, purinergic receptor expression, and P2Y12 receptor function were determined by flow cytometry. P2Y1 and P2X1 function was assessed by fluorescence assays, cyclic nucleotide concentrations by immunoassays, and vasodilator-stimulated phosphoprotein (VASP)-phosphorylation levels by Western blot analysis. Results In contrast to room temperature, ADP-induced aggregation was maintained under cold storage for 6 days, associated with elevated activation markers like fibrinogen binding or CD62P expression. Purinergic receptor expression was not essentially different, whereas P2Y1 function deteriorated rapidly at cold storage, but not P2Y12 activity. Inhibitory pathways of cold-stored platelets were characterized by reduced responses to nitric oxide and prostaglandin E1. Refrigeration of citrated whole blood also led to the attenuation of induced inhibition of platelet aggregation, detectable within 24 hours. Conclusion ADP responsiveness is preserved under cold storage for 6 days due to stable P2Y12 activity and concomitant disintegration of inhibitory pathways enabling a higher reactivity of stored platelets. The ideal storage time at cold temperature for the highest hemostatic effect of platelets should be evaluated in further studies.

P29, an oestrogen receptor-associated protein, is down- regulated by mifepristone in first trimester human placenta and decidua

1991 ◽  
Vol 6 (9) ◽  
pp. 1338-1341 ◽  
Author(s):  
J. Rivera ◽  
N. C. W. Hill ◽  
A. López Bernal ◽  
I. Z. Mackenzie ◽  
A. Cano
Keyword(s):  
Human Placenta ◽  
Oestrogen Receptor ◽  
First Trimester ◽  
Receptor Associated Protein

Expression of granulocyte-colony stimulating factor and its receptor is regulated during the development of the human placenta

1996 ◽  
Vol 149 (2) ◽  
pp. 249-258 ◽  
Author(s):  
S McCracken ◽  
J E Layton ◽  
S C Shorter ◽  
P M Starkey ◽  
D H Barlow ◽  
...  
Keyword(s):  
Human Placenta ◽  
First Trimester ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Chorionic Villi ◽  
Temporal Regulation ◽  
Decidual Tissue ◽  
Weak Staining ◽  
Extravillous Cytotrophoblast ◽  
Stimulating Factor

Abstract The development of the placenta is dependent upon the regulated proliferation, invasion and differentiation of trophoblast. Expression of cytokines at the feto-maternal interface suggests that these molecules may participate in placentation. The expression of granulocyte-colony stimulating factor (G-CSF) and G-CSF receptor (G-CSFR) during the development of the human placenta was studied by immunohistochemistry using an anti-G-CSF monoclonal antibody (mAb) and two novel anti-G-CSFR mAbs. G-CSF was present in the stroma of fetal chorionic villi and maternal decidual tissues throughout pregnancy. G-CSFR was detected at high levels in fetal first and third, but not second trimester placental tissues. Staining for G-CSFR was undetectable in maternal decidual tissue from all gestational stages. In first trimester tissues, staining for placental G-CSFR was strongest in differentiated syncytiotrophoblast and invasive, extravillous cytotrophoblast, and weak staining was evident in undifferentiated cytotrophoblast. Immunohistochemical data suggesting temporal regulation of G-CSFR were corroborated by Western blotting and amplification by reverse transcription and PCR of G-CSFR mRNA. These data suggested that expression of G-CSFR in the human placenta is regulated both temporally and spatially, and that placental G-CSF is involved in paracrine regulation, and indicate a role for G-CSF and G-CSFR in trophoblast growth or function during placentation. Journal of Endocrinology (1996) 149, 249–258

scholarly journals SNAT4 isoform of system A amino acid transporter is expressed in human placenta

2006 ◽  
Vol 290 (1) ◽  
pp. C305-C312 ◽  
Author(s):  
M. Desforges ◽  
H. A. Lacey ◽  
J. D. Glazier ◽  
S. L. Greenwood ◽  
K. J. Mynett ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Expression ◽  
Western Blot ◽  
Human Placenta ◽  
Blot Analysis ◽  
First Trimester ◽  
Amino Acid Transporter ◽  
Full Term ◽  
System A ◽  
Acid Transporter

The system A amino acid transporter is encoded by three members of the Slc38 gene family, giving rise to three subtypes: Na+-coupled neutral amino acid transporter (SNAT)1, SNAT2, and SNAT4. SNAT2 is expressed ubiquitously in mammalian tissues; SNAT1 is predominantly expressed in heart, brain, and placenta; and SNAT4 is reported to be expressed solely by the liver. In the placenta, system A has an essential role in the supply of neutral amino acids needed for fetal growth. In the present study, we examined expression and localization of SNAT1, SNAT2, and SNAT4 in human placenta during gestation. Real-time quantitative PCR was used to examine steady-state levels of system A subtype mRNA in early (6–10 wk) and late (10–13 wk) first-trimester and full-term (38–40 wk) placentas. We detected mRNA for all three isoforms from early gestation onward. There were no differences in SNAT1 and SNAT2 mRNA expression with gestation. However, SNAT4 mRNA expression was significantly higher early in the first trimester compared with the full-term placenta ( P < 0.01). We next investigated SNAT4 protein expression in human placenta. In contrast to the observation for gene expression, Western blot analysis revealed that SNAT4 protein expression was significantly higher at term compared with the first trimester ( P < 0.05). Immunohistochemistry and Western blot analysis showed that SNAT4 is localized to the microvillous and basal plasma membranes of the syncytiotrophoblast, suggesting a role for this isoform of system A in amino acid transport across the placenta. This study therefore provides the first evidence of SNAT4 mRNA and protein expression in the human placenta, both at the first trimester and at full term.

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