Genetics of the P2X7 receptor and human disease

International Human Genome Consortium (2004) Finishing the euchromatic sequence of the human genome. Nature 431(7011):931–45

The International HapMap Consortium (2005) A haplotype map of the human genome. Nature 437(7063):1299–1320

Ford D, Easton DF, Stratton M, Narod S, Goldgar D, Devilee P et al (1998) Genetic heterogeneity and penetrance analysis of the BRCA1 and BRCA2 genes in breast cancer families. The Breast Cancer Linkage Consortium. Am J Hum Genet 62(3):676–689

Burn J, Chapman P, Delhanty J, Wood C, Lalloo F, Cachon-Gonzalez MB et al (1991) The UK Northern region genetic register for familial adenomatous polyposis coli: use of age of onset, congenital hypertrophy of the retinal pigment epithelium, and DNA markers in risk calculations. J Med Genet 28(5):289–296

The Wellcome Trust Case Control Consortium (2007) Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls. Nature 447(7145):661–678

Buell GN, Talabot F, Gos A, Lorenz J, Lai E, Morris MA et al (1998) Gene structure and chromosomal localization of the human P2X7 receptor. Receptors Channels 5(6):347–354

Gu BJ, Zhang W, Worthington RA, Sluyter R, Dao-Ung P, Petrou S et al (2001) A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7 receptor. J Biol Chem 276(14):11135–11142

Boldt W, Klapperstuck M, Buttner C, Sadtler S, Schmalzing G, Markwardt F (2003) Glu496Ala polymorphism of human P2X7 receptor does not affect its electrophysiological phenotype. Am J Physiol Cell Physiol 284(3):C749–C756

Wiley JS, Dao-Ung LP, Li C, Shemon AN, Gu BJ, Smart ML et al (2003) An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor. J Biol Chem 278(19):17108–17113

Smart ML, Gu B, Panchal RG, Wiley J, Cromer B, Williams DA et al (2003) P2X7 receptor cell surface expression and cytolytic pore formation are regulated by a distal C-terminal region. J Biol Chem 278(10):8853–8860

Gu BJ, Sluyter R, Skarratt KK, Shemon AN, Dao-Ung LP, Fuller SJ et al (2004) An Arg307 to Gln polymorphism within the ATP-binding site causes loss of function of the human P2X7 receptor. J Biol Chem 279(30):31287–31295

Skarratt KK, Fuller SJ, Sluyter R, Dao-Ung LP, Gu BJ, Wiley JS (2005) A 5′ intronic splice site polymorphism leads to a null allele of the P2X7 gene in 1–2% of the Caucasian population. FEBS Lett 579(12):2675–2678

Shemon AN, Sluyter R, Fernando SL, Clarke AL, Dao-Ung LP, Skarratt KK et al (2006) A Thr357 to Ser polymorphism in homozygous and compound heterozygous subjects causes absent or reduced P2X7 function and impairs ATP-induced mycobacterial killing by macrophages. J Biol Chem 281(4):2079–2086

Cabrini G, Falzoni S, Forchap SL, Pellegatti P, Balboni A, Agostini P et al (2005) A His-155 to Tyr polymorphism confers gain-of-function to the human P2X7 receptor of human leukemic lymphocytes. J Immunol 175(1):82–89

Denlinger LC, Coursin DB, Schell K, Angelini G, Green DN, Guadarrama AG et al (2006) Human P2X7 pore function predicts allele linkage disequilibrium. Clin Chem 52(6):995–1004

Barden N, Harvey M, Gagne B, Shink E, Tremblay M, Raymond C et al (2006) Analysis of single nucleotide polymorphisms in genes in the chromosome 12Q24.31 region points to P2RX7 as a susceptibility gene to bipolar affective disorder. Am J Med Genet B Neuropsychiatr Genet 141B(4):374–382

Lucae S, Salyakina D, Barden N, Harvey M, Gagne B, Labbe M et al (2006) P2RX7, a gene coding for a purinergic ligand-gated ion channel, is associated with major depressive disorder. Hum Mol Genet 15(16):2438–2445

McQuillin A, Bass NJ, Choudhury K, Puri V, Kosmin M, Lawrence J, et al (2008) Case–ontrol studies show that a non-conservative amino-acid change from a glutamine to arginine in the P2RX7 purinergic receptor protein is associated with both bipolar- and unipolar-affective disorders. Mol Psychiatry. doi: 1038/mp.2008.6

Saunders BM, Fernando SL, Sluyter R, Britton WJ, Wiley JS (2003) A loss-of-function polymorphism in the human P2X7 receptor abolishes ATP-mediated killing of mycobacteria. J Immunol 171(10):5442–5446

Fairbairn IP, Stober CB, Kumararatne DS, Lammas DA (2001) ATP-mediated killing of intracellular mycobacteria by macrophages is a P2X(7)-dependent process inducing bacterial death by phagosome–lysosome fusion. J Immunol 167(6):3300–3307

Kusner DJ, Adams J (2000) ATP-induced killing of virulent Mycobacterium tuberculosis within human macrophages requires phospholipase D. J Immunol 164(1):379–388

Fernando SL, Saunders BM, Sluyter R, Skarratt KK, Goldberg H, Marks GB et al (2007) A polymorphism in the P2X7 gene increases susceptibility to extrapulmonary tuberculosis. Am J Respir Crit Care Med 175(4):360–366

Lammas DA, Stober C, Harvey CJ, Kendrick N, Panchalingam S, Kumararatne DS (1997) ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors. Immunity 7(3):433–444

Nino-Moreno P, Portales-Perez D, Hernandez-Castro B, Portales-Cervantes L, Flores-Meraz V, Baranda L et al (2007) P2X7 and NRAMP1/SLC11 A1 gene polymorphisms in Mexican mestizo patients with pulmonary tuberculosis. Clin Exp Immunol 148(3):469–477

Coutinho-Silva R, Stahl L, Raymond MN, Jungas T, Verbeke P, Burnstock G et al (2003) Inhibition of chlamydial infectious activity due to P2X7R-dependent phospholipase D activation. Immunity 19(3):403–412

Coutinho-Silva R, Perfettini JL, Persechini PM, Dautry-Varsat A, Ojcius DM (2001) Modulation of P2Z/P2X(7) receptor activity in macrophages infected with Chlamydia psittaci. Am J Physiol Cell Physiol 280(1):C81–C89

Panupinthu N, Rogers JT, Zhao L, Solano-Flores LP, Possmayer F, Sims SM et al (2008) P2X7 receptors on osteoblasts couple to production of lysophosphatidic acid: a signaling axis promoting osteogenesis. J Cell Biol 181(5):859–871

Ohlendorff SD, Tofteng CL, Jensen JE, Petersen S, Civitelli R, Fenger M et al (2007) Single nucleotide polymorphisms in the P2X7 gene are associated to fracture risk and to effect of estrogen treatment. Pharmacogenet Genomics 17(7):555–567