An Arg307 To Gln Polymorphism Within The Atp-Binding Site Causes Loss Of Function Of The Human P2X7 Receptor.
Ben J. Gu,Ronald Sluyter,Kristen K. Skarratt,Anne N. Shemon,Lan-Phuong Dao-Ung,Stephen J. Fuller,Julian A. Barden,Alison L. Clarke,Steven Petrou,James S. Wiley +9 more
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TL;DR: A third polymorphism, which substitutes an uncharged glutamine for the highly positively charged Arg307 (R307Q), has been found in heterozygous dosage in 12 of 420 subjects studied and it is likely that this polymorphism abolishes the binding of ATP to the extracellular domain of P2X7.
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About: This article is published in Journal of Biological Chemistry. The article was published on 23 Jul 2004. and is currently open access. The article focuses on the topics: Wild type & Phospholipase D activity.
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Citations
Receptors for Purines and Pyrimidines
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TL;DR: In this review particular emphasis is placed on the discrepancy between the concentrations ofadenosine, ADP, and ATP in the purine receptors of UDP and UTP.
The P2X7 receptor: a key player in IL-1 processing and release.
Davide Ferrari,Cinzia Pizzirani,Elena Adinolfi,Roberto M. Lemoli,Antonio Curti,Marco Idzko,Elisabeth Panther,Francesco Di Virgilio +7 more
TL;DR: A deeper understanding of the mechanism by which the P2X7 receptor triggers IL-1 maturation and exteriorization may suggest novel avenues for the treatment of inflammatory diseases and provide a deeper insight in the fundamental mechanism of protease activation and cellular export of proteins lacking a leader sequence.
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The P2X7 Receptor in Infection and Inflammation
TL;DR: The central role played by the P2X7 receptor in promoting inflammation and driving innate and adaptive immunity is discussed, with an in‐depth knowledge of its structure and of the associated signal transduction mechanisms needed for an effective therapeutic development.
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The P2X7 Receptor Channel: Recent Developments and the Use of P2X7 Antagonists in Models of Disease
TL;DR: The cloning and characterization of human, rat, mouse, guinea pig, dog, and Rhesus macaque P2X7, as well as recent observations regarding the gating and permeability of P2x7, are discussed.
P2X 7 receptors in the nervous system
Beáta Sperlágh,E. Sylvester Vizi,Kerstin Wirkner,Peter Illes +3 more
- 01 Jan 2006
TL;DR: In this paper, the structural and pharmacological features of the P2X7 receptor, as well as its cell-type specific localization in the nervous system are reviewed. And the participation of P2x7 receptors in distinct neuronal, astroglial and microglial functions are described.
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References
Blockade of human P2X7 receptor function with a monoclonal antibody
G. Buell,I P Chessell,Anton D. Michel,G. Collo,M. Salazzo,S. Herren,Denise Gretener,Caroline B. A. Grahames,R. Kaur,M.H. Kosco-Vilbois,Patrick P.A. Humphrey +10 more
TL;DR: Preincubation of human monocytic THP-1 cells with the MoAb antagonized the ability of P2X 7 agonists to induce the release of interleukin-1β, and whole cell currents, elicited by the brief application of 2',3'-(4-benzoyl)-benZoyl-ATP in cells expressing human P2x 7, were reduced in amplitude by the presence of the Mo Ab.
226
Expression of P2X7 purinoceptors on human lymphocytes and monocytes: evidence for nonfunctional P2X7 receptors
TL;DR: Lymphocytes from normal subjects and patients with B-chronic lymphocytic leukemia (B-CLL) show functional responses to extracellular ATP characteristic of the P2X7 receptor (previously termed P2Z)....
225
Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor.
TL;DR: Results suggest that residues close to Ile67 contribute to the ATP-binding site, and introduction of negative charges into the receptor by mutagenesis at this position gave receptors in which the ATP concentration-response curve was right-shifted.
225
The role of positively charged amino acids in ATP recognition by human P2X1 receptors
TL;DR: Mutations at residues K68A and K309A reduced the potency of ATP by >1400-fold and prolonged the time course of the P2X1 receptor current but had no effect on suramin antagonism.
197
Adenosine Triphosphate–Induced Shedding of CD23 and L-Selectin (CD62L) From Lymphocytes Is Mediated by the Same Receptor but Different Metalloproteases
TL;DR: The data show that extracellular ATP induces shedding of L-selectin and CD23 from B-CLL lymphocytes by an action mediated by the P2Z/P2X7 receptor, however, different membrane metalloproteases seem to mediate the shedding of D-23 and L- selectin.
189
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