Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus

Toxicon

Volumn 54, Issue 4, 2009, Pages 379-389

  Papp, Ferenc ^a,b   Batista, Cesar V F ^c   Varga, Zoltan ^a   Herceg, Monika ^a   Román González, Sergio A ^c   Gaspar, Rezso ^a   Possani, Lourival D ^c   Panyi, Gyorgy ^a,b  

^a UNIVERSITY OF DEBRECEN   (Hungary)

^b UNIVERSITY OF DEBRECEN   (Hungary)

^c INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

Author keywords

Kv1.2; Kv1.3; Scorpion; Toxin

Indexed keywords

LYSINE; POTASSIUM CHANNEL KV1.2; POTASSIUM CHANNEL KV1.3; SCORPION VENOM; TST 26; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CHANNEL GATING; CONTROLLED STUDY; DRUG ANALYSIS; DRUG DETERMINATION; DRUG MECHANISM; DRUG PURIFICATION; DRUG STRUCTURE; ELECTROPHYSIOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; MASS SPECTROMETRY; PRIORITY JOURNAL; STEADY STATE;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CERCOPITHECUS AETHIOPS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COS CELLS; HUMANS; KINETICS; KV1.2 POTASSIUM CHANNEL; KV1.3 POTASSIUM CHANNEL; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PATCH-CLAMP TECHNIQUES; PEPTIDES; POTASSIUM CHANNEL BLOCKERS; PROTEIN STRUCTURE, TERTIARY; SCORPION VENOMS; SCORPIONS;

SCORPIONES; TITYUS SERRULATUS; TITYUS STIGMURUS;

EID: 67650473484     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2009.05.023     Document Type: Article

References (37)

1. + channel revealed by the NMR-derived structures of scorpion toxins. Neuron 15 (1995) 1169-1181
2. Avdonin V., Tang X.D., and Hoshi T. Stimulatory action of internal protons on Slo1 BK channels. Biophys. J. 84 (2003) 2969-2980
3. Bagdany M., Batista C.V., Valdez-Cruz N.A., Somodi S., Rodriguez de la Vega R.C., Licea A.F., Varga Z., Gaspar R., Possani L.D., and Panyi G. Anuroctoxin, a new scorpion toxin of the alpha-KTx 6 subfamily, is highly selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes. Mol. Pharmacol. 67 (2005) 1034-1044
4. Barona J., Batista C.V., Zamudio F.Z., Gomez-Lagunas F., Wanke E., Otero R., and Possani L.D. Proteomic Analysis of the Venom and Characterization of Toxins Specific for Na+ - and K+ -Channels From the Colombian Scorpion Tityus Pachyurus. Biochim. Biophys. Acta 1764 (2006) 76-84
5. Batista C.V., del Pozo L., Zamudio F.Z., Contreras S., Becerril B., Wanke E., and Possani L.D. Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and the role of prolines on mass spectrometry analysis of toxins. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 803 (2004) 55-66
6. Batista C.V., Gomez-Lagunas F., Rodríguez de la Vega R.C., Hajdu P., Panyi G., Gaspar R., and Possani L.D. Two novel toxins From the Amazonian scorpion Tityus cambridgei that block Kv1.3 and shaker B K(+)-channels with distinctly different affinities. Biochim. Biophys. Acta 1601 (2002) 123-131
7. Batista C.V., Roman-Gonzalez S.A., Salas-Castillo S.P., Zamudio F.Z., Gomez-Lagunas F., and Possani L.D. Proteomic analysis of the venom from the scorpion Tityus stigmurus: biochemical and physiological comparison with other Tityus species. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 146 (2007) 147-157
8. + Channel. Science 271 (1996) 653-656
9. Beeton C., Wulff H., Standifer N.E., Azam P., Mullen K.M., Pennington M.W., Kolski-Andreaco A., Wei E., Grino A., Counts D.R., Wang P.H., Leehealey C.J., Andrews S., Sankaranarayanan A., Homerick D., Roeck W.W., Tehranzadeh J., Stanhope K.L., Zimin P., Havel P.J., Griffey S., Knaus H.G., Nepom G.T., Gutman G.A., Calabresi P.A., and Chandy K.G. Kv1.3 channels are a therapeutic target for T Cell-mediated autoimmune diseases. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 17414-17419
10. + channels. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 5092-5095
11. Corzo G., Papp F., Varga Z., Barraza O., Espino-Solis P.G., Rodriguez de la Vega R.C., Gaspar R., Panyi G., and Possani L.D. A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venom of the scorpion Centruroides suffusus suffusus. Biochem. Pharmacol. 76 (2008) 1142-1154
12. + channel blocking toxin from Tityus discrepans scorpion venom. FEBS Lett. 456 (1999) 146-148
13. Dauplais M., Lecoq A., Song J., Cotton J., Jamin N., Gilquin B., Roumestand C., Vita C., de Medeiros C.L., Rowan E.G., Harvey A.L., and Menez A. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272 (1997) 4302-4309
14. Deutsch C., Krause D., and Lee S.C. Voltage-gated potassium conductance in human T lymphocytes stimulated with phorbol ester. J. Physiol. (Lond.) 372 (1986) 405-423
15. Diego-Garcia E., Batista C.V., Garcia-Gomez B.I., Lucas S., Candido D.M., Gomez-Lagunas F., and Possani L.D. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. Toxicon 45 (2005) 273-283
16. + channel: peptide and channel residues mediating molecular recognition. Neuron 12 (1994) 1377-1388
17. + channel. Biophys. J. 65 (1993) 1613-1619
18. + channels in human T lymphocytes. Biophys. J. 55 (1989) 203-206
19. + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol. Pharmacol. 45 (1994) 1227-1234
20. Gutman G.A., Chandy K.G., Grissmer S., Lazdunski M., McKinnon D., Pardo L.A., Robertson G.A., Rudy B., Sanguinetti M.C., Stuhmer W., and Wang X. International union of pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. Pharmacol. Rev. 57 (2005) 473-508
21. Hopkins W.F. Toxin and subunit specificity of blocking affinity of three peptide toxins for heteromultimeric, voltage-gated potassium channels expressed in Xenopus oocytes. J. Pharmacol. Exp. Ther. 285 (1998) 1051-1060
22. Kalman K., Pennington M.W., Lanigan M.D., Nguyen A., Rauer H., Mahnir V., Paschetto K., Kem W.R., Grissmer S., Gutman G.A., Christian E.P., Cahalan M.D., Norton R.S., and Chandy K.G. ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem 273 (1998) 32697-32707
23. Lange A., Giller K., Hornig S., Martin-Eauclaire M.F., Pongs O., Becker S., and Baldus M. Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR. Nature 440 (2006) 959-962
24. Legros C., Oughuideni R., Darbon H., Rochat H., Bougis P.E., and Martin-Eauclaire M.F. Characterization of a new peptide from Tityus serrulatus scorpion venom which is a ligand of the apamin-binding site. FEBS Lett. 390 (1996) 81-84
25. Marom S., and Levitan I.B. State-dependent inactivation of the Kv3 potassium channel. Biophys. J. 67 (1994) 579-589
26. + channels of T cells. Toxicon 46 (2005) 418-429
27. + channel blockers: novel tools to inhibit T cell activation leading to specific immunosuppression. Curr. Pharm. Des. 12 (2006) 2199-2220
28. Peter M., Hajdu P., Varga Z., Damjanovich S., Possani L.D., Panyi G., and Gaspar R. Blockage of human T lymphocyte Kv1.3 channels by Pi1, a novel class of scorpion toxin. Biochem. Biophys. Res. Commun. 278 (2000) 34-37
29. Péter M., Varga Z., Hajdú P., Gaspar Jr. R., Damjanovich S., Horjales E., Possani L.D., and Panyi G. Effects of toxins Pi2 and Pi3 on human T lymphocyte Kv1.3 channels: the role of Glu7 and Lys24. J. Membr. Biol. 179 (2001) 13-25
30. Rodrigues A.R., Arantes E.C., Monje F., Stuhmer W., and Varanda W.A. Tityustoxin-K(alpha) blockade of the voltage-gated potassium channel Kv1.3. Br. J. Pharmacol. 139 (2003) 1180-1186
31. +-channels. Toxicon 43 (2004) 865-875
32. Starkus J.G., Kuschel L., Rayner M.D., and Heinemann S.H. Ion conduction through C-type inactivated shaker channels. J. Gen. Physiol. 110 (1997) 539-550
33. + channels. Neuron 18 (1997) 675-682
34. Tytgat J., Chandy K.G., Garcia M.L., Gutman G.A., Martin-Eauclaire M.F., van der Walt J.J., and Possani L.D. A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies. Trends Pharmacol. Sci. 20 (1999) 444-447
35. Visan V., Fajloun Z., Sabatier J.M., and Grissmer S. Mapping of maurotoxin binding sites on HKv1.2, HKv1.3, and HIKCa1 channels. Mol. Pharmacol. 66 (2004) 1103-1112
36. + channel. Mol. Pharmacol. 44 (1993) 430-436
37. + channel in effector memory T cells as new target for MS. J. Clin. Invest. 111 (2003) 1703-1713