A novel thromboxane A2 receptor D304N variant that abrogates ligand binding in a patient with a bleeding diathesis

Blood

Volumn 115, Issue 2, 2010, Pages 363-369

  Mumford, Andrew D ^a   Dawood, Ban B ^b   Daly, Martina E ^c   Murden, Sherina L ^a   Williams, Michael D ^d   Protty, Majd B ^b   Spalton, Jennifer C ^b   Wheatley, Mark ^e   Mundell, Stuart J ^a   Watson, Steve P ^b  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^c UNIVERSITY OF SHEFFIELD   (United Kingdom)

^d BIRMINGHAM CHILDREN S HOSPITAL NHS FOUNDATION TRUST   (United Kingdom)

^e UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

15 HYDROXY 11ALPHA,9ALPHA EPOXYMETHANOPROSTA 5,13 DIENOIC ACID; 7 [3 [(4 PHENYLSEMICARBAZIDO)METHYL] 7 OXABICYCLO[2.2.1]HEPT 2 YL] 5 HEPTENOIC ACID; ADENOSINE TRIPHOSPHATE; ARACHIDONIC ACID; THROMBOXANE A2 RECEPTOR BLOCKING AGENT; CALCIUM; HYDRAZINE DERIVATIVE; LIGAND; THROMBOXANE A2 RECEPTOR; VASOCONSTRICTOR AGENT;

ADOLESCENT; ANIMAL CELL; ARTICLE; BLEEDING TENDENCY; CASE REPORT; CONTROLLED STUDY; DRUG RECEPTOR BINDING; GENE MUTATION; GENETIC VARIABILITY; HUMAN; IN VIVO STUDY; LIGAND BINDING; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; SUBSTITUTION REACTION; THROMBOCYTE AGGREGATION; THROMBOCYTE DYSFUNCTION; TREATMENT RESPONSE; AMINO ACID SUBSTITUTION; ANIMAL; BLEEDING DISORDER; CHO CELL; CLINICAL TRIAL; CRICETULUS; CYTOSOL; DRUG ANTAGONISM; FEMALE; GENE EXPRESSION; GENETICS; HAMSTER; METABOLISM; MISSENSE MUTATION; MULTICENTER STUDY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SECRETION; THROMBOCYTE;

15-HYDROXY-11 ALPHA,9 ALPHA-(EPOXYMETHANO)PROSTA-5,13-DIENOIC ACID; ADENOSINE TRIPHOSPHATE; ADOLESCENT; AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; ANIMALS; BLOOD PLATELETS; CALCIUM; CHO CELLS; CRICETINAE; CRICETULUS; CYTOSOL; FEMALE; GENE EXPRESSION; HEMORRHAGIC DISORDERS; HUMANS; HYDRAZINES; LIGANDS; MALE; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, THROMBOXANE A2, PROSTAGLANDIN H2; VASOCONSTRICTOR AGENTS;

EID: 75649106903     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2009-08-236976     Document Type: Article

References (30)

1. Montuschi P, Barnes PJ, Roberts LJ 2nd. Isoprostanes: markers and mediators of oxidative stress. FASEB J. 2004;18(15):1791-1800.
2. Raychowdhury MK, Yukawa M, Collins LJ, McGrail SH, Kent KC, Ware JA. Alternative splicing produces a divergent cytoplasmic tail in the human endothelial thromboxane A2 receptor. J Biol Chem. 1994;269(30):19256-19261.
3. Nakahata N. Thromboxane A2: physiology/pathophysiology, cellular signal transduction and pharmacology. Pharmacol Ther. 2008;118(1):18-35.
4. Huang JS, Ramamurthy SK, Lin X, Le Breton GC. Cell signalling through thromboxane A2 receptors. Cell Signal. 2004;16(5):521-533.
5. Habib A, FitzGerald GA, Maclouf J. Phosphorylation of the thromboxane receptor alpha, the predominant isoform expressed in human platelets. J Biol Chem. 1999;274(5):2645-2651.
6. Kinsella BT, O'Mahony DJ, Fitzgerald GA. The human thromboxane A2 receptor alpha isoform (TP alpha) functionally couples to the G proteins Gq and G11 in vivo and is activated by the isoprostane 8-epi prostaglandin F2 alpha. J Pharmacol Exp Ther. 1997;281(2):957-964.
7. Offermanns S, Laugwitz KL, Spicher K, Schultz G. G proteins of the G12 family are activated via thromboxane A2 and thrombin receptors in human platelets. Proc Natl Acad Sci U S A. 1994;91(2):504-508.
8. Smyth SS, Woulfe DS, Weitz JI, et al. G-protein-coupled receptors as signaling targets for antiplatelet therapy. Arterioscler Thromb Vasc Biol. 2009;29:449-457.
9. Vilahur G, Casani L, Badimon L. A thromboxane A2/prostaglandin H2 receptor antagonist (S18886) shows high antithrombotic efficacy in an experimental model of stent-induced thrombosis. Thromb Haemost. 2007;98(3):662-669.
10. Turek JW, Halmos T, Sullivan NL, Antonakis K, Le Breton GC. Mapping of a ligand-binding site for the human thromboxane A2 receptor protein. J Biol Chem. 2002;277(19):16791-16797.
11. Khasawneh FT, Huang JS, Turek JW, Le Breton GC. Differential mapping of the amino acids mediating agonist and antagonist coordination with the human thromboxane A2 receptor protein. J Biol Chem. 2006;281(37):26951-26965.
12. Capra V, Veltri A, Foglia C, et al. Mutational analysis of the highly conserved ERY motif of the thromboxane A2 receptor: alternative role in G protein-coupled receptor signaling. Mol Pharmacol. 2004;66(4):880-889.
13. Geng L, Wu J, So SP, Huang G, Ruan KH. Structural and functional characterization of the first intracellular loop of human thromboxane A2 receptor. Arch Biochem Biophys. 2004;423(2):253-265.
14. Hirata T, Kakizuka A, Ushikubi F, Fuse I, Okuma M, Narumiya S. Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly inherited bleeding disorder. J Clin Invest. 1994;94(4):1662-1667.
15. Higuchi W, Fuse I, Hattori A, Aizawa Y. Mutations of the platelet thromboxane A2 (TXA2) receptor in patients characterized by the absence of TXA2-induced platelet aggregation despite normal TXA2 binding activity. Thromb Haemost. 1999;82(5):1528-1531.
16. Dawood BB, Wilde J, Watson SP. Reference curves for aggregation and ATP secretion to aid diagnose of platelet-based bleeding disorders: effect of inhibition of ADP and thromboxane A(2) pathways. Platelets. 2007;18(5):329-345.
17. Mundell SJ, Jones ML, Hardy AR, et al. Distinct roles for protein kinase C isoforms in regulating platelet purinergic receptor function. Mol Pharmacol. 2006;70(3):1132-1142.
18. Hardy AR, Conley PB, Luo J, Benovic JL, Poole AW, Mundell SJ. P2Y1 and P2Y12 receptors for ADP desensitize by distinct kinase-dependent mechanisms. Blood. 2005;105(9):3552-3560.
19. Mundell SJ, Benovic JL, Kelly E. A dominant negative mutant of the G protein-coupled receptor kinase 2 selectively attenuates adenosine A2 receptor desensitization. Mol Pharmacol. 1997;51(6):991-998.
20. Grynkiewicz G, Poenie M, Tsien RY. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J Biol Chem. 1985;260(6):3440- 3450.
21. Hayward CP, Pai M, Liu Y, et al. Diagnostic utility of light transmission platelet aggregometry: results from a prospective study of individuals referred for bleeding disorder assessments. J Thromb Haemost. 2009;7(4):676-684.
22. Cattaneo M, Hayward CP, Moffat KA, Pugliano MT, Liu Y, Michelson AD. Results of a worldwide survey on the assessment of platelet function by light transmission aggregometry: a report from the platelet physiology subcommittee of the SSC of the ISTH. J Thromb Haemost. 2009;7(6):1029.
23. Fuse I, Mito M, Hattori A, et al. Defective signal transduction induced by thromboxane A2 in a patient with a mild bleeding disorder: impaired phospholipase C activation despite normal phospholipase A2 activation. Blood. 1993;81(4):994-1000.
24. Ushikubi F, Okuma M, Kanaji K, et al. Hemorrhagic thrombocytopathy with platelet thromboxane A2 receptor abnormality: defective signal transduction with normal binding activity. Thromb Haemost. 1987;57(2):158-164.
25. Quiroga T, Goycoolea M, Panes O, et al. High prevalence of bleeders of unknown cause among patients with inherited mucocutaneous bleeding. A prospective study of 280 patients and 299 controls. Haematologica. 2007;92(3):357-365.
26. Li J, Edwards PC, Burghammer M, Villa C, Schertler GF. Structure of bovine rhodopsin in a trigonal crystal form. J Mol Biol. 2004;343(5):1409-1438.
27. Pardo L, Deupi X, Dolker N, Lopez-Rodriguez ML, Campillo M. The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors. Chem Biochem. 2007;8(1):19-24.
28. Rosenbaum DM, Rasmussen SG, Kobilka BK. The structure and function of G-protein-coupled receptors. Nature. 2009;459(7254):356-363.
29. Mirzadegan T, Benko G, Filipek S, Palczewski K. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry. 2003;42(10):2759-2767.
30. Zhou W, Flanagan C, Ballesteros JA, et al. A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor. Mol Pharmacol. 1994;45(2):165-170.