ArticleJournal of immunology (Baltimore, Md. : 1950)2009
Differential regulation of P2X7 receptor activation by extracellular nicotinamide adenine dinucleotide and ecto-ADP-ribosyltransferases in murine macrophages and T cells.
Article in Journal of immunology (Baltimore, Md. : 1950), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- Methodological guidelines for P2X receptor assays and data interpretation.Cell death & disease · 2026Review
- Purinergic and extracellular vesicle signaling in alcohol-induced blood-brain barrier breakdown and neuroimmune activation.Brain, behavior, and immunity · 2025Review
- Cross-kingdom mechanisms of trained immunity in plant systemic acquired resistance.Nature plants · 2025Review
- The Multifaceted Role of P2X7R in Microglia and Astrocytes.Neurochemical research · 2025Review
- Purine-based infochemicals and immunometabolites: a comparative review of emerging signaling pathways in plants and animals.FEMS microbiology reviews · 2025Review
- P2 X 7 receptor is a critical regulator of extracellular ATP-induced profibrotic genes expression in rat kidney: implication of transforming growth factor-β/Smad signaling pathway.Purinergic signalling · 2024Article
- Ischemic Tolerance Induced by Glial Cells.Neurochemical research · 2022Review
- P2X7 Receptors in Astrocytes: A Switch for Ischemic Tolerance.Molecules (Basel, Switzerland) · 2022Review
- NADTrends in immunology · 2022Review
- Abacavir Increases Purinergic P2X7 Receptor Activation by ATP: Does a Pro-inflammatory Synergism Underlie Its Cardiovascular Toxicity?Frontiers in pharmacology · 2021Article
- Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor.International journal of molecular sciences · 2020Review
- The P2X7 Receptor as Regulator of T Cell Development and Function.Frontiers in immunology · 2020Article
- Hobit- and Blimp-1-driven CD4Nature immunology · 2019Article
- Astrocytes and Microglia Are Resistant to NADFrontiers in molecular neuroscience · 2019Article
- ATP Evokes CaJournal of immunology (Baltimore, Md. : 1950) · 2018Article
- P2RX7 Purinoceptor as a Therapeutic Target-The Second Coming?Frontiers in chemistry · 2018Review
- Ecto-ADP-ribosyltransferase ARTC2.1 functionally modulates FcγR1 and FcγR2B on murine microglia.Scientific reports · 2017Article
- A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide ineLife · 2017Article
- Nucleoside Reverse Transcriptase Inhibitors Suppress Laser-Induced Choroidal Neovascularization in Mice.Investigative ophthalmology & visual science · 2015Article
- P2X7 on Mouse T Cells: One Channel, Many Functions.Frontiers in immunology · 2015Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Extracellular NAD induces the ATP-independent activation of the ionotropic P2X(7) purinergic receptor (P2X(7)R) in murine T lymphocytes via a novel covalent pathway involving ADP-ribosylation of arginine residues on the P2X(7)R ectodomain. This modification is catalyzed by ART2.2, a GPI-anchored ADP-ribosyltransferase (ART) that is constitutively expressed in murine T cells. We previously reported that ART2.1, a related ecto-ART, is up-regulated in inflammatory murine macrophages that constitutively express P2X(7)R. Thus, we tested the hypothesis that extracellular NAD acts via ART2.1 to regulate P2X(7)R function in murine macrophages. Coexpression of the cloned murine P2X(7)R with ART2.1 or ART2.2 in HEK293 cells verified that P2X(7)R is an equivalent substrate for ADP-ribosylation by either ART2.1 or ART2.2. However, in contrast with T cells, the stimulation of macrophages or HEK293 cells with NAD alone did not activate the P2X(7)R. Rather, NAD potentiated ATP-dependent P2X(7)R activation as indicated by a left shift in the ATP dose-response relationship. Thus, extracellular NAD regulates the P2X(7)R in both macrophages and T cells but via distinct mechanisms. Although ADP-ribosylation is sufficient to gate a P2X(7)R channel opening in T cells, this P2X(7)R modification in macrophages does not gate the channel but decreases the threshold for gating in response to ATP binding. These findings indicate that extracellular NAD and ATP can act synergistically to regulate P2X(7)R signaling in murine macrophages and also suggest that the cellular context in which P2X(7)R signaling occurs differs between myeloid and lymphoid leukocytes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.