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Plant responses to extracellular nucleotides: Cellular processes and biological effects

Integration of P2Y receptor-activated signal transduction pathways in G protein-dependent signalling networks

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Increased 5-HT$_{3}$-mediated signalling in pelvic afferent neurons from mice deficient in P2X$_{2}$ and/or P2X$_{3}$ receptor subunits

Upregulation of P2Y2 receptors by retinoids in normal human epidermal keratinocytes

Stimulation of an α1-adrenergic receptor downregulates ecto-5′ nucleotidase activity on the apical membrane of RPE cells

P2X$_{5}$ and P2X$_{7}$ receptors in human warts and CIN-612 organotypic raft cultures of human papillomavirus infected keratinocytes

Adenosine 5′-triphosphate and its relationship with other mediators that activate pelvic nerve afferent neurons in the rat colorectum

Kinetics of ATP release following compression injury of a peripheral nerve trunk

Signaling pathways downstream of P2 receptors in human neutrophils

Excitatory effect of ATP on rat area postrema neurons

Characterization of human and rodent native and recombinant adenosine A$_{2B}$ receptors by radioligand binding studies

Purinergic Signalling : Volume 2, Issue 2, June 2006

Purinergic Signalling : Volume 2, Issue 1, May 2006

Purinergic Signalling : Volume 1

Signaling pathways downstream of P2 receptors in human neutrophils

Content Provider	Springer Nature Link
Author	Meshki, John Tuluc, Florin Bredetean, Ovidiu Garcia, Analia Kunapuli, Satya P.
Copyright Year	2006
Abstract	Extracellular nucleotides stimulate human neutrophils by activating the purinergic P2Y$_{2}$ receptor. However, it is not completely understood which types of G proteins are activated downstream of this P2 receptor subtype. We investigated the G-protein coupling to P2Y$_{2}$ receptors and several subsequent signaling events. Treatment of neutrophils with pertussis toxin (PTX), a Gi protein inhibitor, caused only ∼75% loss of nucleotide-induced Ca$^{2+}$ mobilization indicating that nucleotides cause Ca$^{2+}$ mobilization both through Gi-dependent and Gi-independent pathways. However, the PLC inhibitor U73122 almost completely inhibited Ca$^{2+}$ mobilization in both nucleotide- and fMLP-stimulated neutrophils, strongly supporting the view that both the PTX-sensitive and the PTX-insensitive mechanism of Ca$^{2+}$ increase require activation of PLC. We investigated the dependence of ERK phosphorylation on the Gi pathway. Treatment of neutrophils with PTX caused almost complete inhibition of ERK phosphorylation in nucleotide or fMLP activated neutrophils. U73122 caused inhibition of nucleotide- or fMLP-stimulated ERK phosphorylation, suggesting that although pertussis toxin-insensitive pathways cause measurable Ca$^{2+}$ mobilization, they are not sufficient for causing ERK phosphorylation. Since PLC activation leads to intracellular Ca$^{2+}$ increase and PKC activation, we investigated if these intracellular events are necessary for ERK phosphorylation. Exposure of cells to the Ca$^{2+}$ chelator BAPTA had no effect on nucleotide- or fMLP-induced ERK phosphorylation. However, the PKC inhibitor GF109203X was able to almost completely inhibit nucleotide- or fMLP-induced ERK phosphorylation. We conclude that the P2Y$_{2}$ receptor can cause Ca$^{2+}$ mobilization through a PTX-insensitive but PLC-dependent pathway and ERK phosphorylation is highly dependent on activation of the Gi proteins.
Starting Page	537
Ending Page	544
Page Count	8
File Format	PDF
ISSN	15739538
Journal	Purinergic Signalling
Volume Number	2
Issue Number	3
e-ISSN	15739546
Language	English
Publisher	Springer Netherlands
Publisher Date	2006-06-20
Publisher Institution	International Purine Club
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	ATP calcium fMLP G protein mitogen-activated protein kinases P2 receptor reactive oxygen species UTP Biomedicine general Pharmacology/Toxicology Human Physiology Neurosciences Cancer Research
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Cellular and Molecular Neuroscience

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