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anti-Human P2RX1 Antikörper:
anti-Mouse (Murine) P2RX1 Antikörper:
anti-Rat (Rattus) P2RX1 Antikörper:
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The pore-lining residues of P2X L340, A344 and A347 each have multiple packing sites that define the P2X ion channel pore configurations.
P2X1 receptors enhance platelet FcgammaRIIa receptor-evoked aggregation through an increase in [Ca(2+)]i downstream of the initial tyrosine phosphorylation events and early dense granule release
The importance of this movement was confirmed by demonstrating that substitution introducing positive charge present in the CRH of the hP2X1R causes PPADS sensitivity at the normally insensitive rat P2X4R. This study provides a template for developing P2XR subtype selectivity based on the differences among the mammalian subunits around the orthosteric P2XR-binding site and the CRH.
Healthy human eosinophils express functional P2X1 receptors whose activation leads to eosinophil alphaMbeta2 integrin-dependent adhesion. P2X1 responses are constitutively reduced in asthmatic compared with healthy eosinophils, probably as the result of an increase in extracellular nucleotide concentration.
the expression of P2X1 transcript and its splicing variant P2X1del in most human monocytes
These data suggest that vascular smooth muscle cells from human gastro-omental arteries express P2X1 and P2X4 receptor subunits
enhances platelet activation evoked by mild stimulants via the p38 signalling pathway
In conclusion, our results demonstrate for the first time that adenine nucleotides acting at P2X1 receptors inhibit the proliferation of human coronary smooth muscle cells via the induction of the early gene NR4A1.
With the development of leukemia, the expression of P2X7R increased in both bone marrow and spleen macrophages whereas expression of P2X1 Receptor increased in spleen macrophages.
Increased P2X1 receptor expression and ATP release may have contributed to the augmentation of contractile response induced by hypoxia-glucopenia and reoxygenation in he detrusor muscles.
Data indicate that MgATP2- activates P2X1 and P2X3, but not P2X2 and P2X4 receptors.
the contribution of the extracellular, transmembrane, and intracellular segments to recovery from desensitization
P2X(1) ion channels play a protective role in endotoxemia by negatively regulating systemic neutrophil activation, thereby limiting the oxidative response, coagulation, and organ damage.
These results suggest that conformational change in the P2X1 receptor is required for co-ordination of ATP action.
HSP90 inhibitors may be as effective as selective antagonists in regulating platelet P2X1 receptors, and their potential effects on hemostasis should be considered in clinical studies.
Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel
Studies indicate that P2X1, P2X2, and P2X4 receptors are detected in preglomerular microvessels.
the cytoskeleton plays an important role in P2X1 receptor regulation
Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating.
T-cell receptor stimulation results in the translocation of P2X1 and P2X4 receptors and pannexin-1 hemichannels to the immune synapse.
PMA-evoked Ca(2+)entry results from an NCX3-dependent dense granule secretion and subsequent P(2X1) receptor activation by secreted ATP, rather than activation of a novel NCCE pathway.
authors proposed a tentative intracellular signaling pathway of the acetylcholine-induced ciliary beat, in which the pannexin-1-purinergic P2X receptor unit may play a central role in ciliary beat regulation
Quite the reverse is seen in P2X1(-/-) mice, which had markedly lower cytokine levels and less coagulation activation compared to controls after exposure to uropathogenic Escherichia coli.
secretion of IL-22 in the regenerating liver is modulated by the ATP receptor, P2X1
Uridine adenosine tetraphosphate induced aortic contraction depends on activation of TX synthase and thromboxane A2 receptor, which partially requires the activation of P2X1R through an endothelium-dependent mechanism.
This study reveals a major role for the P2X1 receptor in LPS-induced lethal endotoxemia through its critical involvement in neutrophil emigration from venules.
NTPDase1 controls male fertility via the regulation of P2X1 activation.
The presence of the P2X1 receptor on both polymorphonuclear neutrophils and platelets is important for fibrin generation and thrombus formation in vivo.
Male contraception via simultaneous knockout of alpha1A-adrenoceptors and P2X1-purinoceptors in mice.
loss of Dicer may impair the expression of miRNAs that are capable of targeting P2x mRNAs.
The activity of P2X2/3 receptors in nodose ganglion neurons is involved in the transmission of myocardial ischemic nociceptive signal.
The P2X receptor phenotype in megakaryocytes and (by inference) platelets is due to expression of homomeric P2X1 receptors.
P2X(1) receptor-deficient mice establish the native P2X receptor and a P2Y6-like receptor in arteries.
Data suggest that the P2X1 receptor contributes to the formation of platelet thrombi, particularly in arteries in which shear forces are high.
P2X1 receptors have a role in renal microvascular autoregulatory behavior
altered function of P2X receptors may be an important contributor to pathogenic Ca2+ entry in dystrophic mouse muscle and may have implications for the pathogenesis of muscular dystrophies
analysis of a novel interaction between platelet P2X1 and thrombin receptors, with P2X1 functioning to amplify aggregation responses at low levels of thrombin receptor stimulation
The data support the hypothesis that jCaTs represent Ca(2+) that enters smooth muscle cells through P2X(1) receptors activated by neurally released ATP and this Ca(2+) is involved in the initial rapid component of the sympathetic neurogenic contraction.
The absence of a correlation between DE and neuroeffector calcium transient amplitudes suggests that the NCT amplitude is a poor measure of quantal size.
Thus an increased SR Ca(2+) content, occurring in the absence of cAMP accumulation or L-type Ca(2+) channel activation, is the principal mechanism by which cardiac P2X receptor mediates a stimulatory effect on cardiac myocyte contractility.
The authors show that porcine circovirus type 2 infection upregulated calcium/calmodulin-dependent protein kinase kinase-beta (CaMKKbeta) by increasing cytosolic Ca(2+) via inositol 1,4,5-trisphosphate receptor (IP3R).
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle, being responsible, for example, for sympathetic vasoconstriction in small arteries, arterioles and vas deferens. Mouse studies suggest that this receptor is essential for normal male reproductive function. It is possible that the development of selective antagonists for this receptor may provide an effective non-hormonal male contraceptive pill.
P2X purinoceptor 1
, ATP receptor
, P2X receptor, subunit 1
, P2X1 receptor
, purinergic receptor P2X1
, programmed cell death 3
, RP-2 protein