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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 (show P2RX4 Proteins) receptor subunits
enhances platelet activation evoked by mild stimulants via the p38 (show CRK Proteins) 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 (show NR4A1 Proteins).
With the development of leukemia, the expression of P2X7R (show P2RX7 Proteins) 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 (show P2RX3 Proteins), but not P2X2 (show P2RX2 Proteins) and P2X4 (show P2RX4 Proteins) receptors.
These results suggest that conformational change in the P2X1 receptor is required for co-ordination of ATP action.
HSP90 (show HSP90 Proteins) 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
Uridine adenosine tetraphosphate induced aortic contraction depends on activation of TX synthase and thromboxane A2 receptor (show TBXA2R Proteins), which partially requires the activation of P2X1R through an endothelium-dependent mechanism.
This study reveals a major role for the P2X1 receptor in LPS (show TLR4 Proteins)-induced lethal endotoxemia through its critical involvement in neutrophil emigration from venules.
NTPDase1 (show ENTPD1 Proteins) 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 (show CACNA1A Proteins)-adrenoceptors and P2X1-purinoceptors in mice.
loss of Dicer (show DICER1 Proteins) may impair the expression of miRNAs that are capable of targeting P2x mRNAs.
The activity of P2X2 (show P2RX2 Proteins)/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 (show P2RY6 Proteins)-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.
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