Relevant bibliographies by topics / P2Z receptors

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'P2Z receptors'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'P2Z receptors.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "P2Z receptors"

1

Briner, V. A., and F. Kern. "ATP stimulates Ca2+ mobilization by a nucleotide receptor in glomerular endothelial cells." American Journal of Physiology-Renal Physiology 266, no. 2 (February 1, 1994): F210—F217. http://dx.doi.org/10.1152/ajprenal.1994.266.2.f210.

Full text
Abstract:
The present study investigates ATP effects on Ca2+ mobilization in bovine glomerular endothelial cells (GEC) and the receptors mediating ATP response. Extracellular ATP stimulated a rise in inositol 1,4,5-trisphosphate and cytosolic free Ca2+ concentration ([Ca2+]i) in a dose-dependent manner. Extracellular Ca2+ depletion did not prevent [Ca2+]i rise. ATP effects were not mediated by P1, P2x, and P2t purinoceptors, since the P1 receptor agonist adenosine and the P2x receptor agonist [alpha,beta-CH2]ATP had no effect on inositol 1-monophosphate (IP) formation and Ca2+ mobilization and ATP does not activate P2t receptors. The P2y receptor antagonist reactive blue (10(-3) M) had little inhibitory effect on ATP (10(-5) M)-stimulated IP formation (15.6 +/- 4.2%) and Ca2+ rise (7.0 +/- 3.0%). According to the classification of purinoceptors, ATP is less potent than 2-methylthioadenosine 5'-triphosphate (2-MeS-ATP) in stimulating P2y receptors. In GEC, however, the rank order of potency in stimulating IP and [Ca2+]i rise was ATP > 2-MeS-ATP > ADP. The pyrimidine nucleotide UTP (10(-3) M) induced maximal IP formation (653 +/- 37%) and Ca2+ mobilization (591 +/- 22 nM) similar to ATP (IP 647 +/- 27%; [Ca2+]i 583 +/- 15 nM). At submaximal (10(-5) M) but not at maximal (10(-3) M) doses ATP and UTP effects were additive. ATP and UTP induced specific cross-desensitization. It is concluded that the purinergic nucleotide ATP and pyrimidine nucleotide UTP mediate their effects by a common nucleotide receptor. This receptor differs from P2z and P2y1 receptors, since by definition UTP does not activate these receptors.(ABSTRACT TRUNCATED AT 250 WORDS)
APA, Harvard, Vancouver, ISO, and other styles
2

Schulze-Lohoff, Eckhard, Christian Hugo, Sylvia Rost, Susanne Arnold, Angela Gruber, Bernhard Brüne, and Ralf Bernd Sterzel. "Extracellular ATP causes apoptosis and necrosis of cultured mesangial cells via P2Z/P2X7receptors." American Journal of Physiology-Renal Physiology 275, no. 6 (December 1, 1998): F962—F971. http://dx.doi.org/10.1152/ajprenal.1998.275.6.f962.

Full text
Abstract:
Mesangial cells undergo cell death both by apoptosis and necrosis during glomerular disease. Since nucleotides are released from injured and destroyed cells in the glomerulus, we examined whether extracellular ATP and its receptors may regulate cell death of cultured mesangial cells. Addition of extracellular ATP (300 μM to 5 mM) to cultured rat mesangial cells for 90 min caused a 5.8-fold increase in DNA fragmentation (terminal deoxynucleotidyl transferase assay) and a 4.2-fold increase in protein levels of the tumor suppressor p53, which is thought to regulate apoptosis. Apoptotic DNA fragmentation was confirmed by the diphenylamine assay and by staining with the DNA-specific fluorochrome Hoechst 33258. The necrotic markers, release of lactate dehydrogenase and uptake of trypan blue, were not positive before 3 h of ATP addition. The effects of ATP on DNA fragmentation and p53 expression were reproduced by the purinergic P2Z/P2X7 receptor agonist, 3′- O-(4-benzoylbenzoyl)-ATP, and inhibited by the P2Z/P2X7 receptor blocker, oxidized ATP. Transcripts encoding the P2Z/P2X7 receptor were expressed by cultured mesangial cells as determined by Northern blot analysis. P2Z/P2X7 receptor-associated pore formation in the plasma membrane was demonstrated by the Lucifer yellow assay. We conclude that activation of P2Z/P2X7 receptors by extracellular ATP causes apoptosis and necrosis of cultured mesangial cells. Activation of purinergic P2Z/P2X7 receptors may play a role in causing death of mesangial cells during glomerular disease.
APA, Harvard, Vancouver, ISO, and other styles
3

Schilling, William P., Tanya Wasylyna, George R. Dubyak, Benjamin D. Humphreys, and William G. Sinkins. "Maitotoxin and P2Z/P2X7purinergic receptor stimulation activate a common cytolytic pore." American Journal of Physiology-Cell Physiology 277, no. 4 (October 1, 1999): C766—C776. http://dx.doi.org/10.1152/ajpcell.1999.277.4.c766.

Full text
Abstract:
The effects of maitotoxin (MTX) on plasmalemma permeability are similar to those caused by stimulation of P2Z/P2X7ionotropic receptors, suggesting that 1) MTX directly activates P2Z/P2X7 receptors or 2) MTX and P2Z/P2X7 receptor stimulation activate a common cytolytic pore. To distinguish between these two possibilities, the effect of MTX was examined in 1) THP-1 monocytic cells before and after treatment with lipopolysaccharide and interferon-γ, a maneuver known to upregulate P2Z/P2X7receptor, 2) wild-type HEK cells and HEK cells stably expressing the P2Z/P2X7 receptor, and 3) BW5147.3 lymphoma cells, a cell line that expresses functional P2Z/P2X7 channels that are poorly linked to pore formation. In control THP-1 monocytes, addition of MTX produced a biphasic increase in the cytosolic free Ca2+ concentration ([Ca2+]i); the initial increase reflects MTX-induced Ca2+ influx, whereas the second phase correlates in time with the appearance of large pores and the uptake of ethidium. MTX produced comparable increases in [Ca2+]iand ethidium uptake in THP-1 monocytes overexpressing the P2Z/P2X7 receptor. In both wild-type HEK and HEK cells stably expressing the P2Z/P2X7 receptor, MTX-induced increases in [Ca2+]iand ethidium uptake were virtually identical. The response of BW5147.3 cells to concentrations of MTX that produced large increases in [Ca2+]ihad no effect on ethidium uptake. In both THP-1 and HEK cells, MTX- and Bz-ATP-induced pores activate with similar kinetics and exhibit similar size exclusion. Last, MTX-induced pore formation, but not channel activation, is greatly attenuated by reducing the temperature to 22°C, a characteristic shared by the P2Z/P2X7-induced pore. Together, the results demonstrate that, although MTX activates channels that are distinct from those activated by P2Z/P2X7 receptor stimulation, the cytolytic/oncotic pores activated by MTX- and Bz-ATP are indistinguishable.
APA, Harvard, Vancouver, ISO, and other styles
4

Ecelbarger, C. A., Y. Maeda, C. C. Gibson, and M. A. Knepper. "Extracellular ATP increases intracellular calcium in rat terminal collecting duct via a nucleotide receptor." American Journal of Physiology-Renal Physiology 267, no. 6 (December 1, 1994): F998—F1006. http://dx.doi.org/10.1152/ajprenal.1994.267.6.f998.

Full text
Abstract:
Recent studies in a variety of cell types have revealed several receptor subtypes that bind ATP and trigger increases in intracellular Ca2+ concentration ([Ca2+]i). The present studies were aimed at determining whether similar receptors are present in the rat terminal inner medullary collecting duct (IMCD). [Ca2+]i was measured using fura 2 in tubules dissected from collagenase-treated rat kidneys. ATP (1–100 microM) caused a rapid increase in [Ca2+]i with a prolonged late phase after an initial peak. A similar rise was observed in tubules exposed to UTP or to the poorly hydrolyzable analogue, adenosine 5–-O-(3-thiotriphosphate) (ATP gamma S). In contrast, agonists that bind P2x, P2y, P2z, and P2t purinergic receptors did not affect [Ca2+]i. Removal of extracellular Ca2+ inhibited the response to ATP by approximately 50% with obliteration of the late phase. Furthermore, indomethacin attenuated the rise in [Ca2+]i produced by ATP. Adenosine analogues also increased [Ca2]i apparently by binding to distinct adenosine receptors rather than to the ATP receptor. We conclude that there is a nucleotide receptor in the rat terminal IMCD, which, when occupied, mobilizes intracellular Ca2+.
APA, Harvard, Vancouver, ISO, and other styles
5

Zaborina, Olga, Namita Misra, Jan Kostal, Shilpa Kamath, Vinayak Kapatral, M. El-Azami El-Idrissi, B. S. Prabhakar, and A. M. Chakrabarty. "P2Z-Independent and P2Z Receptor-Mediated Macrophage Killing by Pseudomonas aeruginosa Isolated from Cystic Fibrosis Patients." Infection and Immunity 67, no. 10 (October 1, 1999): 5231–42. http://dx.doi.org/10.1128/iai.67.10.5231-5242.1999.

Full text
Abstract:
ABSTRACT We demonstrate that a mucoid, alginate-producing strain ofPseudomonas aeruginosa isolated from the lungs of a cystic fibrosis (CF) patient secretes multiple enzymes with nucleoside diphosphate kinase (Ndk), ATPase, adenylate kinase, 5′-nucleotidase, and ATP-modifying enzymatic activities. The secretion is triggered at high cell density and in complex media but is greatly reduced when the mucoid cells are grown in mineral salts media or in presence of 5.0 mM Ca2+ or Mg2+. Interestingly, the secretion is triggered primarily in the mucoid CF isolate of strain 8821M (or in strain FRD1) but not in a nonmucoid laboratory strain, PAO1. The purified secreted Ndk shows 100% match in its N-terminal amino acid sequence with that of purified intracellular Ndk and demonstrates similar enzymatic properties. The N-terminal sequence of the purified ATPase isolated from an ndk knockout mutant shows its identity with that of the heat shock chaperonin Hsp60. During fractionation, the flowthrough fraction from a Mono Q column demonstrates the presence of 5′-nucleotidase, adenylate kinase, and a putative ATP reductase activity. These fractions demonstrate high cytotoxic activities for murine peritoneal primary macrophages which can be further stimulated in the presence of ATP or inhibited by pretreatment of macrophages with oxidized ATP (oATP). The cytotoxicity associated with ATP-induced stimulation is believed to be due to activation of macrophage surface-associated P2Z (P2X7) receptors, which are one of the purinergic receptors responsible for pore formation on macrophage membrane. Blocking of these receptors by pretreatment with oATP blocks ATP-induced macrophage cell death. Thus mucoid P. aeruginosa cells elaborate enzymes that modulate the external ATP levels of macrophages, thereby modulating macrophage cell death through P2Z receptor activation. Evidence for the presence of secreted cytotoxic agents that act independently of P2Z receptor activation is also presented.
APA, Harvard, Vancouver, ISO, and other styles
6

Turner, J. T., L. A. landon, S. J. Gibbons, and B. R. Talamo. "Salivary Gland P2 Nucleotide Receptors." Critical Reviews in Oral Biology & Medicine 10, no. 2 (April 1999): 210–24. http://dx.doi.org/10.1177/10454411990100020701.

Full text
Abstract:
The effects of ATP on salivary glands have been recognized since 1982. Functional and pharmacological studies of the P2 nucleotide receptors that mediate the effects of ATP and other extracellular nucleotides have been supported by the cloning of receptor cDNAs, by the expression of the receptor proteins, and by the identification in salivary gland cells of multiple P2 receptor subtypes. Currently, there is evidence obtained from pharmacological and molecular biology approaches for the expression in salivary gland of two P2X ligand-gated ion channels, P2Z/P2X7 and P2X4, and two P2Y G protein-coupled receptors, P2Y1 and P2Y2. Activation of each of these receptor subtypes increases intracellular Ca2+, a second messenger with a key role in the regulation of salivary gland secretion. Through Ca2+ regulation and other mechanisms, P2 receptors appear to regulate salivary cell volume, ion and protein secretion, and increased permeability to small molecules that may be involved in cytotoxicity. Some localization of the various salivary P2 receptor subtypes to specific cells and membrane subdomains has been reported, along with evidence for the co-expression of multiple P2 receptor subtypes within specific salivary acinar or duct cells. However, additional studies in vivo and with intact organ preparations are required to define clearly the roles the various P2 receptor subtypes play in salivary gland physiology and pathology. Opportunities for eventual utilization of these receptors as pharmacotherapeutic targets in diseases involving salivary gland dysfunction appear promising.
APA, Harvard, Vancouver, ISO, and other styles
7

Pérez-Andrés, Encarnación, María Fernández-Rodriguez, Mónica González, Ana Zubiaga, Ainara Vallejo, Itxaso García, Carlos Matute, et al. "Activation of phospholipase D-2 by P2X7 agonists in rat submandibular gland acini." Journal of Lipid Research 43, no. 8 (August 2002): 1244–55. http://dx.doi.org/10.1194/jlr.m100372-jlr200.

Full text
Abstract:
Exogenous ATP stimulated phospholipase D (PLD), but not sphingomyelinase in rat submandibular gland (SMG) acini. PLD activation was dependent upon extracellular Ca2+ and did not involve intracellular Ca2+ mobilization or phosphoinositide-specific phospholipase C activation. ATP-stimulated PLD was attenuated by inhibition or downregulation of protein kinase C (PKC). PLD activation was fully blocked by the cytosolic phospholipase A2 (PLA2) inhibitor ONO-RS-082 and partially attenuated by the selective Ca2+-dependent cytosolic PLA2 inhibitor, arachidonyl trifluoromethylketone (AACOCF3), or by bromoenol lactone, an inhibitor of Ca2+-independent cytosolic PLA2. Magnesium, which decreases the concentration of ATP4−, and nickel, which blocks nonspecific cation channels coupled to purinergic receptors, inhibited PLD activation by ATP. Using reverse transcription-polymerase chain reaction and Northern blotting techniques, we demonstrated that the PLD isoform stimulated by ATP was PLD-2. Among various ATP analogs, only the P2Z/P2X7 purinergic receptor agonist benzoyl-benzoyl ATP stimulated PLD-2. The response to ATP was inhibited by the nonselective P2X purinergic antagonist suramin and by oxidized ATP, a potent P2Z/P2X7 receptor antagonist.It is concluded that in rat SMG acinar cells, PLD-2 is upregulated by exogenous ATP through a mechanism involving Ca2+ influx, cytosolic PLA2, and PKC. Also, the data suggest an involvement of P2X7 receptors in PLD-2 stimulation by ATP.
APA, Harvard, Vancouver, ISO, and other styles
8

Coutinho-Silva, Robson, Pedro M. Persechini, Rodrigo Da Cunha Bisaggio, Jean-Luc Perfettini, Ana Cristina Torres De Sa Neto, Jean M. Kanellopoulos, Iris Motta-Ly, Alice Dautry-Varsat, and David M. Ojcius. "P2Z/P2X7receptor-dependent apoptosis of dendritic cells." American Journal of Physiology-Cell Physiology 276, no. 5 (May 1, 1999): C1139—C1147. http://dx.doi.org/10.1152/ajpcell.1999.276.5.c1139.

Full text
Abstract:
Macrophages and thymocytes express P2Z/P2X7nucleotide receptors that bind extracellular ATP. These receptors play a role in immune development and control of microbial infections, but their presence on dendritic cells has not been reported. We investigated whether extracellular ATP could trigger P2Z/P2X7receptor-dependent apoptosis of dendritic cells. Apoptosis could be selectively triggered by tetrabasic ATP, since other purine/pyrimidine nucleotides were ineffective, and it was mimicked by the P2Zreceptor agonist, benzoylbenzoyl ATP, and blocked by magnesium and the irreversible antagonist, oxidized ATP. RT-PCR analysis confirmed the mRNA expression of the P2Z/P2X7receptor and the absence of P2X1. Caspase inhibitors and cycloheximide had only a partial effect on the apoptosis, suggesting that a caspase-independent mechanism may also be operative. Brief treatment with ATP led to an increase in the intracellular calcium concentration and permeabilization of the plasma membrane to Lucifer yellow, which diffused throughout the dendritic cell cytosol. Other small extracellular molecules may thus attain a similar intracellular distribution, perhaps activating endogenous proteases that contribute to initiation of apoptosis.
APA, Harvard, Vancouver, ISO, and other styles
9

Hickman, SE, J. el Khoury, S. Greenberg, I. Schieren, and SC Silverstein. "P2Z adenosine triphosphate receptor activity in cultured human monocyte- derived macrophages." Blood 84, no. 8 (October 15, 1994): 2452–56. http://dx.doi.org/10.1182/blood.v84.8.2452.2452.

Full text
Abstract:
Abstract The present study shows that human mononuclear phagocytes express a P2Z- like purinergic membrane receptor activity. Extracellular adenosine triphosphate (ATP) induces the formation of nonselective membrane pores in human mononuclear phagocytes that allow the entry of otherwise membrane impermeant fluorescent dyes (YO-PRO-1 or Lucifer yellow) into the cytoplasm of these cells. The percentage of mononuclear phagocytes that was permeabilized by ATP increased as monocytes matured into macrophages. Their response to ATP was inhibited by Mg2+ and oxidized ATP. Benzoylbenzoic-ATP (BzBzATP) was approximately 60% as effective as ATP and adenosine-5 -O-(thiophosphate) (ATP gamma S) was less than 20% as effective as ATP in permeabilizing human macrophages to YO-PRO-1 or Lucifer Yellow. Thus, the human P2Z-like receptor differs from its murine counterpart because BzBzATP, ATP, and ATP gamma S are equally efficacious in permeabilizing murine macrophage-like J774 cells to these dyes. UTP, GTP, and CTP were ineffective in permeabilizing human or murine macrophages to YO-PRO-1. Taken together, these data indicate that human monocyte-derived macrophages express a P2Z-like activity that is pharmacologically distinct from that expressed by their murine counterparts and that expression of these receptors is developmentally regulated in human mononuclear phagocytes.
APA, Harvard, Vancouver, ISO, and other styles
10

Hickman, SE, J. el Khoury, S. Greenberg, I. Schieren, and SC Silverstein. "P2Z adenosine triphosphate receptor activity in cultured human monocyte- derived macrophages." Blood 84, no. 8 (October 15, 1994): 2452–56. http://dx.doi.org/10.1182/blood.v84.8.2452.bloodjournal8482452.

Full text
Abstract:
The present study shows that human mononuclear phagocytes express a P2Z- like purinergic membrane receptor activity. Extracellular adenosine triphosphate (ATP) induces the formation of nonselective membrane pores in human mononuclear phagocytes that allow the entry of otherwise membrane impermeant fluorescent dyes (YO-PRO-1 or Lucifer yellow) into the cytoplasm of these cells. The percentage of mononuclear phagocytes that was permeabilized by ATP increased as monocytes matured into macrophages. Their response to ATP was inhibited by Mg2+ and oxidized ATP. Benzoylbenzoic-ATP (BzBzATP) was approximately 60% as effective as ATP and adenosine-5 -O-(thiophosphate) (ATP gamma S) was less than 20% as effective as ATP in permeabilizing human macrophages to YO-PRO-1 or Lucifer Yellow. Thus, the human P2Z-like receptor differs from its murine counterpart because BzBzATP, ATP, and ATP gamma S are equally efficacious in permeabilizing murine macrophage-like J774 cells to these dyes. UTP, GTP, and CTP were ineffective in permeabilizing human or murine macrophages to YO-PRO-1. Taken together, these data indicate that human monocyte-derived macrophages express a P2Z-like activity that is pharmacologically distinct from that expressed by their murine counterparts and that expression of these receptors is developmentally regulated in human mononuclear phagocytes.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "P2Z receptors"

1

Gargett, Caroline Eve, and mikewood@deakin edu au. "Studies of the human lymphocyte P2Z receptor and its activation of phospholipase D." Deakin University, 1997. http://tux.lib.deakin.edu.au./adt-VDU/public/adt-VDU20060727.144101.

Full text
Abstract:
Extracellular adenosine 5′-triphosphate (ATP) is an agonist for the P2Z receptor of human leukaemic lymphocytes and opens a Ca 2+-selective ion channel, which also conducts Ba2+, Sr2+ and the small fluorescent dye, ethidium+. A wide range of receptor agonists, many of which raise cytosolic [Ca2+] activate phospholipase D (PLD). In the present study, it was shown that both ATP and 3′-O-(4-benzoylbenzoyl)-ATP (BzATP) stimulated PLD activity in a concentration-dependent manner, and the inhibitory effects of suramin, oxidised ATP, extracellular Na+ and Mg2+ suggested that the effect of these agonists is mediated by P2Z receptors. The role of divalent cations in ATP-stimulated PLD activity was investigated. Several agonists (eg ATP, thapsigargin, ionomycin) stimulated a rise in cytosolic [Ca2+] in human lymphocytes, but only ATP and ionomycin stimulated PLD activity. When Ca2+ influx was prevented by EGTA, the majority of ATP-stimulated and all of ionomycin-stimulated PLD activity was inhibited. Preloading cells with the Ca2+ chelator, BAPTA, reduced cytosolic [Ca2+] and, paradoxically, ATP-stimulated PLD activity was potentiated. ATP-stimulated PLD activity was supported by both Ba2+ and Sr2+ when they were substituted for extracellular Ca2+. Furthermore, both ATP-stimulated PLD activity and ATP-stimulated 133Ba2+ influx showed a linear dependence on extracellular [Ba2+]. Thus it was concluded that ATP stimulated PLD activity in direct proportion to the influx of divalent cations through the P2Z ion channel and this PLD activity was insensitive to changes in bulk cytosolic [Ca2+]. The calmodulin (Ca2+/CaM) inhibitor, trifluoperazine (TFP) inhibited ionomycin- and ATP-stimulated PLD activity and ATP-stimulated apoptosis, but had no effect on PLD activity already activated by ATP. However, TFP inhibited ATP-stimulated Ca2+, Ba2+ and ethidium+ fluxes, at concentrations below those which inhibit Ca2+/CaM, suggesting that TFP inhibits the P2Z receptor. Similarly, the isoquinolinesulphonamide, KN-62, a selective inhibitor of Ca2+/CaM-dependent protein kinase II (CaMKII), also prevented ATP-stimulated apoptosis, but had no effect on pre-activated PLD. In addition, KN-62, and an analogue, KN-04, which has no effect on CaMKII, potently inhibited ATP-stimulated Ba2+ influx (IC50 12.7 ± 1.5 and 17.3 ± 2.7 nM, respectively), ATP-stimulated ethidium+ uptake (IC50 13.1 ± 2.6 and 37.2 ± 8.9 nM, respectively), ATP-stimulated phospholipase D activity (50% inhibition 5.9 ± 1.2 and 9.7 ± 2.8 nM, respectively) and ATP-induced shedding of the surface adhesion molecule, L-selectin (IC50 31.5 ± 4.5 and 78.7 ± 10.8 nM, respectively). They did not inhibit phorbol ester- or ionomycin-stimulated PLD activity or phorbol ester-induced L-selectin shedding. Neither KN-62 nor KN-04 (both 500 nM) have any effect on UTP-stimulated Ca2+ transients in fura-2-loaded human neutrophils, a response which is mediated by the P2Y2 receptor, neither did they inhibit ATP-stimulated contractile responses mediated by the P2X1 receptor of guinea pig urinary bladder. Thus, KN-62 and KN-04 are almost equipotent as P2Z inhibitors with IC50s in the nanomolar, indicating that their actions cannot be due to CaMKII inhibition, but rather that they are potent and direct inhibitors of the P2Z receptor. Extracellular ATP-induced shedding of L-selectin from lymphocytes into the medium is a Ca2+-independent response. L-selectin is either cleaved by a metalloproteinase or a PLD with specificity for glycosylphosphatidylinositol (GPI). The novel hydroxamic acid-based zinc chelator, Ro-31-9790 blocks ATP-induced L-selectin shedding, but was without effect on ATP-induced Ba2+ influx or ATP-stimulated PLD activity. Furthermore, another zinc chelator, 1,10-phenanthroline, an inhibitor of a GPI-PLD, potentiated rather than inhibited ATP-stimulated PLD activity, suggesting that ATP-induced L-selectin shedding and ATP-stimulated PLD activity are independent of each other. Although extracellular ATP is the natural ligand for the lymphocyte P2Z receptor, it is less potent than BzATP in stimulating Ba2+ influx. Concentration-response curves for BzATP- and ATP-stimulated ethidium+ influx gave EC50s 15.4 ± 1.4 µM and 85.6 ± 8.8 µM, respectively. The maximal response to ATP was only 69.8 ± 1.9% of that for BzATP. Hill coefficients were 3.17 ± 0.24 and 2.09 ± 0.45 for BzATP and ATP respectively, suggesting greater positive cooperativity for BzATP than for ATP in opening the P2Z-operated ion channel. A rank order of agonist potency of BzATP > ATP = 2MeSATP > ATPγS was observed for agonist-stimulated ethidium+ influx, while maximal influxes followed a rank order of BzATP > ATP > 2MeSATP > ATPγS. When ATP (300 -1000 µM) was added simultaneously with 30 µM BzATP (EC90), it reduced both ethidium+ and Ba2+ fluxes by 30 - 40% relative to values observed with BzATP alone. KN-62, previously shown to be a specific inhibitor of the lymphocyte P2Z receptor, was a less potent antagonist of BzATP-induced fluxes than ATP, when maximal concentrations of both agonists (50 and 500 µM respectively) were used. However, when BzATP (18 µM) was used at a concentration equiactive with a maximally effective ATP concentration, KN-62 showed the same inhibitory potency for both agonists. The ecto-ATPase antagonist, ARL-67156, inhibited both ATP- and BzATP-stimulated Ba2+ influx, suggesting that the lower efficacy of ATP compared with BzATP was not due to preferential hydrolysis of ATP. Thus, the natural ligand, ATP, is a partial agonist for the P2Z receptor while BzATP is a full agonist. Moreover the competitive studies show that only a single class of P2-receptor (P2Z class) is expressed on human leukaemic lymphocytes. Both ATP- and BzATP-stimulated PLD activity were significantly inhibited (P < 0.05) when cells were suspended in iso-osmotic choline Cl medium. Choline+ was found to be a permeant for the P2Z ion channel, since ATP induced a large uptake of [14C]choline+ (60 to 150 µmol/ml intracellular water) during a 5 min incubation, which remained in the cells for several hours, and ATP was used to load cells with these levels of choline+. Intracellular choline+ inhibited ATP-, BzATP-, PMA- and ionomycin-stimulated PLD activity. Brief exposure of lymphocytes to ATP increased the subsequent basal rate of ethidium+ uptake, and this was prevented by intracellular choline+. It is proposed that P2Z-mediated Ca2+ influx in lymphocytes activates PLD leading to significantly changes of the phospholipid composition of the plasma membrane, which subsequently produces a permeability lesion, which in turn contributes to cell death.
APA, Harvard, Vancouver, ISO, and other styles
2

Mateos-Trigos, Gabriela. "P2 receptors (P2Y₁ and P2Y₁₂) of equine platelets." Thesis, University of Cambridge, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.620715.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Alberto, Anael Viana Pinto. "Caracterização dos receptores P2 em eosinófilos de ratos e do poro associado ao receptor P2X7." Instituto Oswaldo Cruz, 2012. https://www.arca.fiocruz.br/handle/icict/6938.

Full text
Abstract:
Submitted by Alessandra Portugal (alessandradf@ioc.fiocruz.br) on 2013-09-20T15:33:03Z No. of bitstreams: 1 Anael Viana Pinto Alberto.pdf: 4150812 bytes, checksum: 9ce0a5d780533302dcc603ae65f510fe (MD5)
Made available in DSpace on 2013-09-20T15:33:03Z (GMT). No. of bitstreams: 1 Anael Viana Pinto Alberto.pdf: 4150812 bytes, checksum: 9ce0a5d780533302dcc603ae65f510fe (MD5) Previous issue date: 2012-10-31
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Rio de Janeiro, RJ, Brasil
ATP e outros nucleotídeos são liberados para o meio extracelular por vias reguladas ou pela perda da integridade de membrana. Uma vez fora da célula, esses compostos podem ativar receptores P2: P2X (receptores ionotrópicos) e P2Y (receptores acoplados a proteínas G). Além disso, O receptor P2X7 é um importante membro da família P2X, já que sua ativação pode levar a abertura de um poro membranar que permite a passagem de moléculas de até 900 Da. Os eosinófilos são as principais células efetoras em respostas alérgicas e estão associados com diversos processos fisiológicos e patológicos. Nesse trabalho investigamos a expressão de receptores P2 e suas funções em eosinófilos. Nesse contexto, nosso primeiro passo foi investigar a expressão e funcionalidade dos receptores P2X por patch clamping. Nossos resultados sugerem a presença de P2X1, de P2X2 e de P2X7. Em seguida, avaliamos por microfluorimetria a funcionalidade dos receptores P2Y, e verificamos com base na ordem de potência a possível presença de P2Y2, de P2Y4, de P2Y6 e de P2Y11. Além disso, confirmamos nossos dados por imunofluorescência. Realizamos também ensaios de migração in vitro e in vivo, para verificar se os nucleotídeos extracelulares poderiam atrair eosinófilos. O ATP foi capaz de induzir a migração dos eosinófilos, enquanto a suramina, um bloqueador P2, aboliu esse efeito, tanto in vitro, utilizando transwell, como in vivo, utilizando um modelo de pleurisia alérgica em ratos. Em seguida, avaliamos o possível papel da panexina-1 como poro associado ao receptor P2X7. Nesse trabalho utilizamos inibidores de hemicanais em experimentos de patch clamp e em ensaios de permeabilização de corante. Os resultados indicam que os inibidores de hemicanais não bloquearam a geração de corrente ou a captação de corante após a ativação do receptor P2X7 em macrófagos de ratos e camundongos. Demonstramos que eosinófilos de rato expressam receptores P2X e P2Y por imunofluorescência. Além disso, demonstramos que a ativação de receptores P2 pode aumentar a migração de eosinófilos in vitro e in vivo. Além disso, foi demonstrado que inibidores de panexina-1 não bloqueiam a captação do corante ou a corrente gerada pela ativação do receptor P2X7. Os nossos resultados demostraram que panexina-1 não é o poro associado ao receptor P2X7 em macrófagos
ATP and other nucleotides are released from cells through regulated pathways or following the loss of plasma membrane integrity. Once outside the cell, these compounds can activate P2 receptors: P2X ionotropic receptors and G protein-coupled P2Y receptors. . Additionally, P2X7 receptor is an important member of the P2X family of ionotropic receptor as its activation opens a non-selective pore allowing the passage of molecules up to 900 Da. Eosinophils represent major effector cells in the allergic inflammatory response and they are, in fact, associated with several physiological and pathological processes. Here we investigate the expression of P2 receptors and roles of those receptors in murine eosinophils. In this context, our first step were to investigate the expression and functionality of the P2X receptors by patch clamping, our results suggest the presence of P2X1, P2X2 and P2X7. Next we evaluate by microfluorimetry the expression of P2Y receptors, our results based in the ranking order of potency suggests the presence of P2Y2, P2Y4, P2Y6 e P2Y11. Moreover, we confirmed our findings by immunofluorescence assays. We also did in vitro and in vivo migration assays to verify whether nucleotides could attract eosinophil. ATP increased migration of eosinophils, while suramin a P2 blocker abolished this effect in both in vitro, using trasnwell, and in vivo, using a model of rat allergic pleurisy. Next, we evaluated the putative role of pannexin-1 as the pore associated to the P2X7 receptor. We used hemichannels inhibitors in patch clamp and dye uptake experiments. The results indicate that they do not interfere with current generation or dye uptake after activation of P2X7R in rat and mouse macrophages. We have demonstrated that rat eosinophils express P2X and P2Y receptors by immunofluorescence. In addition, the activation of P2 receptors can increase migration of eosinophils in vitro and in vivo. Moreover, we demonstrated that specific inhibitors of pannexin-1 did not interfere with the dye uptake or current generated by the P2X7 activation. Our results showed that pannexin-1 is not the pore associated to the P2X7 receptor in macrophages.
APA, Harvard, Vancouver, ISO, and other styles
4

Kong, Qiongman. "Regulations and functions of P2Y₂ and P2X₇ nucleotide receptors in the central nervous system." Diss., Columbia, Mo. : University of Missouri-Columbia, 2007. http://hdl.handle.net/10355/4847.

Full text
Abstract:
Thesis (Ph.D.)--University of Missouri-Columbia, 2007.
The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on March 19, 2009) Vita. Includes bibliographical references.
APA, Harvard, Vancouver, ISO, and other styles
5

Vick, Jonathan. "The Contribution of Purinergic P2X and P2Y Receptors to the Excitability of Mouse Vomeronasal Sensory Neurons." ScholarWorks @ UVM, 2014. http://scholarworks.uvm.edu/graddis/283.

Full text
Abstract:
Olfaction, the sense of smell, allows animals to perceive the multitude of volatile and nonvolatile molecules present in the environment. In many mammals, such as mice and rats, there are four unique chemosensory organs including the (1) main olfactory epithelium (MOE), (2) septal organ, (3) Grüneberg ganglion, and (4) vomeronasal organ (VNO). While the VNO detects some general volatile odorants, it is further specialized for the detection of behaviorally relevant nonvolatile odorants or pheromones. In rodents, the VNO is encased within a bony capsule and located at the base of the nasal cavity. Odorants are detected by vomeronasal sensory neuron (VSN)s, bipolar neurons with a single axon that projects to the accessory olfactory bulb of the brain and a single dendrite capped with microvilli that project into the lumen of the VNO. In the MOE, purinergic signaling through adenosine 5'-triphosphate (ATP) gated ionotropic P2X and G-protein coupled P2Y receptors contributes a neuroprotective and neuroregenerative pathway. As virtually nothing was known about purinergic signaling in the VNO, I set out to characterize the (1) presence of the purinergic receptors and (2) ATP release pathways. In isolated VSNs, ATP elicited an increase in intracellular calcium ([Ca2+]I) and an inward current with similar potency. Adenosine and the P2Y receptor agonists adenosine 5'-diphosphate (ADP), uridine 5'-triphosphate (UTP), and uridine 5'-diphosphate (UDP) were ineffective. The increase in [Ca2+]I was dependent upon extracellular calcium and the inward current elicited by ATP was partially blocked by the P2X receptor antagonists pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate (PPADS) and 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP). When coapplied with the natural stimulus dilute urine, ATP increased the inward current above that elicited by either dilute urine or ATP alone. Furthermore, ADP hyperpolarized the voltage dependence of steady state inactivation of voltage activated sodium current (INa) in a subset of VSNs. The hyperpolarization in the voltage dependence of steady state inactivation elicited by ADP was blocked in the presence of suramin, a purinergic receptor antagonist, but similar to that produced by 1-oleoyl-2-acetyl-sn-glycerol (OAG), a membrane permeable protein kinase C (PKC) activator. Neither ATP nor ADP affected the voltage dependence of activation, fast inactivation, or time dependent recovery from inactivation. Interestingly, ADP reversibly increased spike frequency but did not change an action potential's amplitude, latency, halfwidth, or threshold voltage. Accordingly, we detected gene expression of the P2X1 and 3 as well as P2Y1, 2, and 6 receptors in the VNO and localized the P2Y1 and 2 receptors to isolated VSNs. Thus, excitability in VSNs can be enhanced by (1) ATP eliciting an inward current through P2X receptors and (2) ADP decreasing spike adaptation during persistent firing presumably through P2Y receptors. Moreover, one possible source of ATP may be from mechanical stimulation of the VNO that accompanies vasomotor pump activation.
APA, Harvard, Vancouver, ISO, and other styles
6

Chen, Xiaowei. "Involvement of purinergic P2X and P2Y2 receptors in urinary bladder sensation." Diss., University of Iowa, 2009. https://ir.uiowa.edu/etd/343.

Full text
Abstract:
Interstitial cystitis (IC)/painful bladder syndrome (PBS) is a functional visceral disorder characterized by increased bladder activity and chronic pelvic pain in the absence of a pathobiological condition. Enhanced sensory transduction of peripheral bladder afferents is hypothesized to contribute to the pain and mechanical hypersensitivity of IC/PBS patients. The aim of this thesis is to test the hypothesis that purinergic receptors, including ionotropic P2X and metabotropic P2Y, are important for sensory transmission in bladder afferent neurons and may be involved in bladder hypersensitivity after bladder tissue insults. Electrophysiological, single cell RT-PCR and immunohistochemistry techniques were performed in bladder afferent neurons from naïve and bladder inflamed mice to test the hypothesis. In Chapter 2, I characterized the distribution and function of P2X receptors in thoracolumbar (TL) and lumbosacral (LS) dorsal root ganglia (DRG) neurons innervating the urinary bladder, and found that LS and TL bladder neurons have differential purinergic signaling and distinct membrane electrical properties. In Chapter 3, I examined the sensitization of bladder afferent neurons and the plasticity of P2X receptor function in a mouse model of chemical induced bladder inflammation. P2X-mediated signals in LS and TL bladder neurons after bladder inflammation were enhanced compared with those in saline-treated controls, suggesting the importance of P2X in bladder hypersensitivity associated with cystitis. In Chapter 4, the modulation of P2Y on P2X function and the co-localization of P2Y and P2X were examined in bladder sensory neurons. It has been found that P2Y2 receptor enhances bladder sensory neuron excitability and facilitates the response of homomeric P2X2 receptor to the purinergic agonist (ATP). The present study provides evidence that LS and TL mouse bladder sensory neurons exhibit distinct P2X signaling, and the function of P2X receptors could be facilitated during bladder inflammation and modulated by activation of P2Y2 receptor, indicating an involvement of P2X and P2Y2 receptors as mechano- and chemosensors in bladder sensory transmission under normal conditions and in bladder hypersensitivity associated with inflammation.
APA, Harvard, Vancouver, ISO, and other styles
7

Dovlatova, Natalia. "Studies on placelet p2y receptors." Thesis, University of Nottingham, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.517665.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Hibell, Amanda Dawn. "Functional characteristics of P2X₇ receptors." Thesis, University of Cambridge, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621665.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Zheng, Wenxuan. "Properties of mammalian P2X₇ receptors." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/properties-of-mammalian-p2x7-receptors(1ff23f4a-47eb-4d06-b54c-bd7488c9700c).html.

Full text
Abstract:
To establish comprehensive pharmacology of P2X₇ receptors, membrane current recording, intracellular calcium transient recording and ethidium bromide uptake were carried out to examine several selective (A-740003, A- 438079) and non-selective (suramin) P2X₇ antagonists across mammalian P2X₇ receptors (human, mouse and rat). These P2X₇ receptors demonstrated species-dependent sensitivities to antagonists. In each species, A-740003 revealed variant IC50 values with different assays, indicating the assay- dependent pharmacology of P2X₇ receptors. Conventionally, pharmacology can be used to define a native current but not in the case of the human breast cancer cell line, Hs578T. It is found that P2X₇ was expressed at both mRNA and protein level. The ATP-evoked currents recorded from Hs578T cells were P2X₇-like with distinctive electrophysiological features. But the pharmacology profile of the currents did not fit with P2X₇ receptor. Further experiments are needed to either include or exclude the existence of functional P2X₇ receptors in Hs578T. Transmembrane domain 2 (TM2) is known as the pore-forming region for P2X receptors. TM2 of P2X₇ receptor was investigated with cysteine substitution scanning. The predicted α-helix structure of the TM2 segment was in good agreement with the results from the substituted cysteine accessibility method (SCAM). Thr336, Ser339, Tyr343, Phe344 and Thr348 were found important for both channel dilation and aqueous pore formation. Ser339 was further studied. Various substitutions at Ser339 were explored. The results suggest that the polarity of the side chain at Ser339 is essential for the channel dilation. Furthermore, disulfide bond formation was identified between S339C in the trimeric receptor, implying that the side chains of Ser339 might turn very close to each other during the channel opening and dilation.
APA, Harvard, Vancouver, ISO, and other styles
10

Liu, Jun. "Structural determinants of P2Y₂ receptor functions." Free to MU campus, others may purchase, 2003. http://wwwlib.umi.com/cr/mo/fullcit?p3100062.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "P2Z receptors"

1

Turner, John T., Gary A. Weisman, and Jeffrey S. Fedan, eds. The P2 Nucleotide Receptors. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-4612-1800-5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Brown, Julia. Pharmacological evaluation of novel ligands of P2Y receptors. Wolverhampton: University of Wolverhampton, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

White, Pamela J. The role of P2Y receptors in human vascular smooth muscle. Leicester: De Montfort University, 2005.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Rajagopal, Senthilkumar, and Murugavel Ponnusamy. Metabotropic GPCRs: TGR5 and P2Y Receptors in Health and Diseases. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1571-8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Pharmacology of purine and pyrimidine receptors. San Diego, CA: Elsevier, 2011.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Fairbairn, Ian Paul. Investigations of a novel mechanism of anti-tuberculous immunity mediated by purinergic (P2X[inferior seven]) receptors. Birmingham: University of Birmingham, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Yeung, Davy. Molecular and functional analysis of the purinergic P2X receptors in normal and dystrophic skeletal muscle: A thesis. Portsmouth: University of Portsmouth, School of Pharmacy and Biomedical Sciences, 2004.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Professor, Turner John T., Weisman Gary A, and Fedan Jeffrey S, eds. The P2 nucleotide receptors. Totowa, N.J: Humana Press, 1998.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Turner, John T. The P2 Nucleotide Receptors. Humana, 2012.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Nistri, Andrea, Geoffrey Burnstock, Baljit S. Khakh, and Rashid Giniatullin, eds. ATP-gated P2X receptors in health and disease. Frontiers SA Media, 2015. http://dx.doi.org/10.3389/978-2-88919-405-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "P2Z receptors"

1

Chessell, I. P., A. D. Michel, and P. P. A. Humphrey. "P2X Receptors." In Purinergic and Pyrimidinergic Signalling I, 47–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-09604-8_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Evans, Richard J., Annmarie Surprenant, and R. Alan North. "P2X Receptors." In The P2 Nucleotide Receptors, 43–61. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-4612-1800-5_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Rajagopal, Senthilkumar, and Murugavel Ponnusamy. "P2Y Receptor." In Metabotropic GPCRs: TGR5 and P2Y Receptors in Health and Diseases, 39–55. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1571-8_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Hennies, Hagen-Heinrich, Corinna Maul, and Bernd Sundermann. "P2 Receptors." In Analgesics, 487–96. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527605614.ch11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Horstkorte, Rüdiger, Bettina Büttner, Kaya Bork, Navdeep Sahota, Sarah Sabir, Laura O’Regan, Joelle Blot, et al. "Nucleotide Receptor P2x." In Encyclopedia of Signaling Molecules, 1275–87. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_50.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Horstkorte, Rüdiger, Bettina Büttner, Kaya Bork, Navdeep Sahota, Sarah Sabir, Laura O’Regan, Joelle Blot, et al. "Nucleotide Receptor P2Y." In Encyclopedia of Signaling Molecules, 1287–92. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_198.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Pendergast, William, and Richard Evans. "P2Y Receptor Agonists." In New Drugs for Asthma, Allergy and COPD, 165–68. Basel: KARGER, 2001. http://dx.doi.org/10.1159/000062142.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Communi, Didier, Bernard Robaye, and Jean-Marie Boeynaems. "Nucleotide Receptor P2Y." In Encyclopedia of Signaling Molecules, 3629–36. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_198.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Shen, Jian-Bing, Bruce T. Liang, and Florentina Soto. "Nucleotide Receptor P2x." In Encyclopedia of Signaling Molecules, 3616–29. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_50.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Kawate, Toshimitsu. "P2X Receptor Activation." In Advances in Experimental Medicine and Biology, 55–69. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/5584_2017_55.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "P2Z receptors"

1

Gonzales, Silvia D., Chong Wang, Amaris A. Genemaras, and C. Y. Charles Huang. "Novel Measuring System of ATP-Induced Transmembrane Potential Change of Nucleus Pulposus Cells." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80539.

Full text
Abstract:
Low back pain is a serious concern in industrialized societies that affects millions of people around the world [1]. It can be attributed to several spine disorders; intervertebral disc (IVD) degeneration being one of the most common causes [2]. IVDs are the largest avascular tissue in the body and are composed of two differentiated anatomical structures: the nucleus pulposus (NP) and the annulus fibrosus (AF). The ability to withstand compressive loads due to weight and bending is provided by the swelling of the NP structure, while the ability to resist tensile forces during bending and twisting is provided by the AF fibers [3]. The biomechanical functions of NP and AF rely on their extracellular matrix (ECM) structure and composition. Previous studies have demonstrated that static and dynamic compressive loading alters ATP production, which may have an effect on ECM synthesis [2]. In addition, dynamic loading has shown an increase in ATP release from NP cells, which may contribute to endplate calcification and therefore to IVD degeneration [2, 4]. When tissue is damaged, ATP, which is found in millimolar concentrations in all cells, leaks or is released into the extracellular milieu [5, 6]. Extracellular ATP is a powerful signaling molecule that can regulate cell metabolism, survival, and growth [7]. However, IVD cell response to ATP has not been investigated. The receptors involved in transducing responses to ATP are found in many tissues throughout the body and are responsible for different kinds of intercellular communication. ATP receptor subtypes are ligand-gated ion channels (P2X) and G-protein coupled receptors (P2Y). P2X receptors show calcium permeability while P2Y receptors mediate calcium release from intracellular stores in response to ATP [6]. Direct ATP application to the cell has been reported to cause a change in membrane conductance in a variety of tissues [8]. The voltage sensitive dye di-8-ANEPPS allows for a noninvasive method of measuring fluorescence changes of the cell membrane, which are proportional to variations of the transmembrane potential [8]. Therefore, the objectives of this study were (1) to develop a novel transmembrane potential measuring system using di-8-ANEPPS dye and (2) to investigate the response of NP cells to ATP by measuring the change in transmembrane potential.
APA, Harvard, Vancouver, ISO, and other styles
2

Gordon, J. L. "ADENINE NUCLEOTIDES AND THEREGULATION OF VASCULAR TONE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643719.

Full text
Abstract:
ATP, although known mainly as an intracellular energy source, is also capable of acting extracellularly as a vasoactive agent of great potency, at concentrations around lμM or less. ADP is approximately equipotent with ATP in its actions on extracellular receptors in the vasculature.ATP and ADP can arise extracellularly through release from the cytoplasm of cellsexposed to damaging stimuli or by degranulation of platelets. The concentration of the nucleotides in the cytoplasm of most cells (including vascular endothelial and smooth muscle cells) is more than ImM, and the concentration in the dense storage granules of platelets approaches 1M. Thus, there is potential for very high localised concentrations of ATP and ADP in the plasma following platelet degranulation or damageto cells of the vessel well. Release from vascular endothelial and smooth muscle cells can occur with no loss of cell viability or leakage of cytoplasmic proteins.The vasoactivity of ATP and ADP is mediated via P2 purinoceptors. Vasodilation can be induced through the release of EDRF from endothelial cells or through stimulation of PGI2 production (PGI2 is a vasodilator in many, althoughnot all, arterial beds). Purinoceptor-mediated prostacyclin production can be stimulated from perfused vascular beds (e.g. theheart andthe lung), from isolated blood vessels or from cultured endothelial cells.In some blood vessels, purinoceptor-mediated vasoconstriction can be induced by direct actionon the vascular smooth muscle cells. The receptors responsible are sub-classified as P2X (which induce vasoconstriction) and P2Y (whichinduce vasodilation). The P2Y purinoceptor that mediates EDRF production is very similar to that which is responsible for PGI2 production, although there are some intriguing differences inthe potency of ATP analogs at stimulating these two responses, even on the same cells. The intracellular mechanisms responsible have not yet been fully elucidated, but it appears that elevation of intracellular calcium is likely to play a causal role.Adenosine, which is the product of ATP and ADP metabolism by nucleotidases, can also induce vasodilation in many blood vessels, acting via P1] purinoceptors on the smooth muscle cells, but its potency is often less than that of ATP and ADP.The fate of adenine nucleotides released into the plasma is determined by ectonucleotidases on the luminal surface of the endothelial cells, not by enzymes in the blood itself (the half-life of ATP in samples of blood or plasma is many minutes, while in the microcirculation the half-life isless than one second). Endothelial ectonucleotidases have been detected in several vascular beds, and many of their characteristics are now known. These enzymes are distinct entities from the P2 purinoceptors on endothelium, as shown by the marked differences in potency of several ATP analogs as P2 receptor stimulants and as substrates for the nucleotidases.In summary, vascular endothelial and smooth muscle cells respond to extracellularATP and ADP, and can also metabolise thesenucleotides extracellularly by ectonucleotidases. In addition, ATP and ADP can be selectively released from the cells of the vessel wall and from activated platelets. Thus, the endothelial pericellular environment can be the site of complex interactions by which vascular tone is regulated through the release, actions and metabolism ofextracellular nucleotides.
APA, Harvard, Vancouver, ISO, and other styles
3

Wang, Chong, Silvia D. Gonzales, Weiyong Gu, and C. Y. Charles Huang. "Accumulation of Extracellular ATP in Porcine Nucleus Pulposus." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80671.

Full text
Abstract:
There are many reasons for people to miss work; one of the leading contributors is low back pain (LBP), which is believed to affect 80% of the population at some point during their lifetime. Suffering from back pain is the chief complaint of 5% of people who visit the doctor in the US [1]. The total medical cost related to low back pain in the US exceeds 100 billion dollars every year [2]. The cause of LBP is still unclear. However, recent studies revealed that intervertebral disc (IVD) degeneration is closely related to LBP [3]. IVD transfers loads and allows the spine to move through torsion, bending or compression [4–6]. There are two main anatomic regions in IVD: nucleus pulposus (NP) and annulus fibrosis (AF). The loss of notochordal cells in the NP region has been associated with the initiation of disc degeneration [7]. Our recent studies demonstrated that the adenosine triphosphate (ATP) production of notochordal NP cells was much higher than that of the AF cells while mechanical loading promoted ATP release from IVD cells [8]. Extracellular ATP (eATP) is a powerful signaling molecule that can mediate a wide variety of biological responses, such as cell metabolism, survival, and growth by binding to the purinergic receptors: G protein coupled receptor (P2Y) or ligand-gated ionotropic receptor (P2X) [9]. In addition, eATP is often rapidly hydrolyzed by several families of ectonucleotidases [10–12]. The by-products of eATP hydrolysis include inorganic pyrophosphate (PPi) and phosphate (Pi) which are closely related to mineral crystal formation and tissue calcification [12–15]. PPi and Pi released from eATP hydrolysis may contribute to endplate calcification which has been associated with disc degeneration. However, eATP accumulation in the IVD has not been studied yet. Therefore, the objective of this study was to investigate the accumulative level of eATP in the NP region of porcine IVD using a novel optical ATP sensor.
APA, Harvard, Vancouver, ISO, and other styles
4

Vanhoutte, Paul M. "PLATELETS, ENDOTHELIUM AND VASOSPASM." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643722.

Full text
Abstract:
The endothelium can secrete both relaxing and contracting substances. One of the most powerful stimuli to the release of the former are thrombin and aggregating platelets. This contributes to the protective role of the endothelium against inappropriate intraluminal platelet aggregation and coagulation in blood vessels with an intact intima. Thrombin-induced, endothelium-dependent relaxations have been obtained in isolated arteries of different species, including humans. Endothelium-dependent relaxations can be evoked by autologous platelets in isolated blood vessels of the dog, pig and rat; they can be obtained in canine coronary arteries with human platelets. The major platelet-products involved in these endothelium-dependent relaxations are 5-hydroxytryptamine (serotonin) and the adenine nucleotides. Although platelet-activating factor (PAF) can evoke endothelium-dependent relaxation it only does so at concentrations much higher than those occurring under physiological conditions; since the relaxations are not prevented by PAF-antagonists, they are non-specific in nature.The receptor mediating the endothelium-dependent relaxations to serotonin released from the aggregating platelets can be subtyped as a S1~(5HT1) serotonergic receptor;those mediating the response to the adenine nucleotides as P2y-purinergic receptors. In the absence of the endothelium aggregating platelets cause contractions of vascular smooth muscle; these are mediated by a mixture of S1-like and S2~serotoner-gic receptors in coronary arteriesof the dog, and by S2-serotonergic receptors in those of the pig. Thus, in the porcine coronary artery, the S2-serotonergic antagonist ketanserin markedly enhances the platelet-induced endothelium-dependent relaxation. After previous (four weeks) injury, the regenerated endothelium of the porcine coronary artery loses the ability to respond to serotonin,and is unable to prevent the constrictionsevoked by aggregating platelets. The endothelium-dependent relaxations of porcine coronary arteries evoked by aggregating platelets are potentiated by chronic treatmentof the donor animals with cod liver oil. These studies emphasize the protective roleof the endothelial cells against the vasoconstriction (vasospasm) induced by aggregating platelets. This role is depressed after previous injury, and can be facilitatedby dietary adj ustments.
APA, Harvard, Vancouver, ISO, and other styles
5

Cristalli, Gloria, Diego Dal Ben, Catia Lambertucci, Floriana R. Portino, Sara Taffi, Sauro Vittori, and Rosaria Volpini. "Synthesis of new P2 receptor ligands." In XIIIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2005. http://dx.doi.org/10.1135/css200507087.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Bau, I.-Jiuan, and Gou-Jen Wang. "A Highly Sensitive Electrochemical Impedimetric Nanobiosensor for Dust Mite Antigen Der p2 Detection." In ASME 2011 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/detc2011-47123.

Full text
Abstract:
The group 2 allergen, Der p2, has been reported to activate innate toll-like receptors (TLRs) on respiratory epithelial cells and thus aggravate respiratory diseases. In this study, a high sensitive nanobiosensor based on a 3D sensing element that has uniformly deposited gold nanoparticles for the detection of the dust mite antigen Der p2 is proposed. The barrier layer of an anodic aluminum oxide (AAO) film is used as the template in this highly sensitive nanobiosensor fabricated with a reducing agent and stabilizer-free method. Electrochemical deposition is utilized to synthesize uniformly distributed gold nanoparticles on the surface of the barrier layer. The size and the distribution density of the nanoparticles can be well controlled by the potential applied during electrochemical deposition. Following this procedure, monoclonal antibodies were immobilized against the dust mite antigen Der p2 by the gold nanoparticles through the 11-MUA (11-mercaptoundecanoic acid), EDC (1-Ethyl-3-(3-dimethyl-aminopropyl)-carbodiimide)/NHS (N-hydroxysuccinimide) self-assembled monolayer approach. The proposed nanobiosensor was successfully used to examine the Der p2 down to a concentration of 1pg/mL through the electrochemical impedance spectroscopy analysis. The high sensitivity of the proposed 3D nanobiosensor can be attributed to the high intensity and uniformity of the Au nanoparticles on the sensor. The proposed nanobiosensor would be useful for the fast detection of rare molecules in a solution.
APA, Harvard, Vancouver, ISO, and other styles
7

Pascual, T., YS Tsai, M. Martín, A. Lluch, J. Cortes, A. Llombart, P. Conte, et al. "Abstract P2-08-06: Standardized nCounter-based determination of estrogen receptor (ER), progesterone receptor (PR) and HER2 receptor status in breast cancer." In Abstracts: 2018 San Antonio Breast Cancer Symposium; December 4-8, 2018; San Antonio, Texas. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-p2-08-06.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Redfern, A., P. Lau, A. White, S. Hoon, M. Bulsara, and A. Long. "Abstract P2-12-02: Cochrane review of capecitabine for hormone receptor positive versus hormone receptor negative breast cancer." In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p2-12-02.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Nicholson, RI, HO Habashy, JM Gee, P. Finlay, L. Farrow, B. Jasani, P. Barrett-Lee, JF Robertson, and IO Ellis. "Abstract P2-06-19: Transferrin Receptor (CD71) Identifies Poor Response to Tamoxifen in Oestrogen Receptor Positive Breast Cancer Patients." In Abstracts: Thirty-Third Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 8‐12, 2010; San Antonio, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/0008-5472.sabcs10-p2-06-19.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Hennigs, Jan K., Nicole Lüneburg, Annett Stage, Hans J. Baumann, Rainer Kiefmann, Rainer H. Böger, and Hans Klose. "P2 Receptor Mediated Ca2+ Signaling In Human Pulmonary Artery Endothelial Cells." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1947.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "P2Z receptors"

1

Balk, Steven P. Tamoxifen Dependent Interaction Between in Estrogen Receptor and a Novel p21 Activated Kinase. Fort Belvoir, VA: Defense Technical Information Center, June 2004. http://dx.doi.org/10.21236/ada435363.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Balk, Steven P. Tamoxifen Dependent Interaction Between the Estrogen Receptor and a Novel P21 Activated Kinase. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada424652.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Sun, Zijie. Interaction Between a Novel p21 Activated Kinase (PAK6) and Androgen Receptor in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2005. http://dx.doi.org/10.21236/ada438427.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Sun, Zijie. Interaction Between a Novel p21 Activated Kinase (PAK6) and Androgen Receptor in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2003. http://dx.doi.org/10.21236/ada415338.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Sun, Zijie. Interaction Between a Novel p21 Activated Kinase (PAK6) and Androgen Receptor in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2004. http://dx.doi.org/10.21236/ada423821.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'P2Z receptors' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography