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Dear Author, Please, Note That Changes Made to the HTML Content Dear Author, Please, note that changes made to the HTML content will be added to the article before publication, but are not reflected in this PDF. Note also that this file should not be used for submitting corrections. Our reference: TOXCON 4827 P-authorquery-v9 AUTHOR QUERY FORM Journal: TOXCON Please e-mail or fax your responses and any corrections to: E-mail: [email protected] Article Number: 4827 Fax: +31 2048 52789 Dear Author, Please check your proof carefully and mark all corrections at the appropriate place in the proof (e.g., by using on-screen annotation in the PDF file) or compile them in a separate list. Note: if you opt to annotate the file with software other than Adobe Reader then please also highlight the appropriate place in the PDF file. To ensure fast publication of your paper please return your corrections within 48 hours. 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TOXCON4827_grabs ■ 31 May 2014 ■ 1/1 Toxicon xxx (2014) 1 46 Contents lists available at ScienceDirect 47 48 Toxicon 49 50 51 journal homepage: www.elsevier.com/locate/toxicon 52 53 54 55 56 1 57 2 58 3 59 4 Highlights 60 5 61 6 fi ¼ ¼ Margatoxin inhibits Kv1.2 and Kv1.3 channels with low picomolar af nities (Kd 11.7 pM for Kv1.3 and Kd 6.4 pM for 62 7 Kv1.2). 63 8 Margatoxin is a non-selective blocker of Kv1.3. 64 9 Comprehensive assessment of the selectivity of MgTx for 14 ion channels included in the study. 65 10 MgTx (1 nM) does not inhibit hKv1.4-IR, hKv1.5, hKv1.6, hKv1.7, rKv2.1, Shaker-IR, hERG, hKCa1.1, hKCa3.1 and hNav1.5. 66 11 fi ¼ MgTx is a low af nity blocker of Kv1.1 (Kd 4.2 nM). 67 12 68 13 69 14 70 15 71 16 72 17 73 18 74 19 75 20 76 21 77 22 78 23 79 24 80 25 81 26 82 27 83 28 84 29 85 30 86 31 87 32 88 33 89 34 90 35 91 36 92 37 93 38 94 39 95 40 96 41 97 42 98 43 99 44 45 http://dx.doi.org/10.1016/j.toxicon.2014.05.002 0041-0101/© 2014 Elsevier Ltd. All rights reserved. þ Please cite this article in press as: Bartok, A., et al., Margatoxin is a non-selective inhibitor of human Kv1.3 K channels, Toxicon (2014), http://dx.doi.org/10.1016/j.toxicon.2014.05.002 TOXCON4827_proof ■ 31 May 2014 ■ 1/11 Toxicon xxx (2014) 1e11 51 Contents lists available at ScienceDirect 52 53 Toxicon 54 55 56 journal homepage: www.elsevier.com/locate/toxicon 57 58 59 60 þ 61 1 Margatoxin is a non-selective inhibitor of human Kv1.3 K 62 2 63 3 channels 64 4 65 5 a a b a c Q5 Adam Bartok , Agnes Toth , Sandor Somodi , Tibor G. Szanto , Peter Hajdu , 66 6 a, d, * a Gyorgy Panyi , Zoltan Varga 67 7 68 8 a Department of Biophysics and Cell Biology, University of Debrecen, Faculty of Medicine, 98 Nagyerdei krt., Debrecen 4032, Hungary b 69 9 Division of Metabolic Diseases, Department of Internal Medicine, University of Debrecen, 98 Nagyerdei krt., Debrecen 4032, Hungary c Department of Biophysics and Cell Biology, University of Debrecen, Faculty of Dentistry, 98 Nagyerdei krt., Debrecen 4032, Hungary 70 10 d MTA-DE Cell Biology and Signaling Research Group, 4032 Debrecen, Egyetem ter 1, Hungary 71 11 72 12 73 13 article info abstract 74 14 75 15 Article history: Margatoxin (MgTx), an alpha-KTx scorpion toxin, is considered a selective inhibitor of the 76 16 Received 11 March 2014 Kv1.3K þ channel. This peptide is widely used in ion channel research; however, a 77 17 Received in revised form 7 May 2014 comprehensive study of its selectivity with electrophysiological methods has not been Accepted 12 May 2014 78 18 published yet. The lack of selectivity might lead to undesired side effects upon therapeutic Available online xxxx 79 19 application or may lead to incorrect conclusion regarding the role of a particular ion 80 20 channel in a physiological or pathophysiological response either in vitro or in vivo. Keywords: 81 Using the patch-clamp technique we characterized the selectivity profile of MgTx using 21 Margatoxin L929 cells expressing mKv1.1 channels, human peripheral lymphocytes expressing Kv1.3 82 22 MgTx 83 23 Non-selective channels and transiently transfected tsA201 cells expressing hKv1.1, hKv1.2, hKv1.3, hKv1.4-IR, hKv1.5, hKv1.6, hKv1.7, rKv2.1, Shaker-IR, hERG, hKCa1.1, hKCa3.1 and hNav1.5 84 24 Kv1.3 Kv1.2 channels. MgTx is indeed a high affinity inhibitor of Kv1.3 (Kd ¼ 11.7 pM) but is not se- 85 25 lective, it inhibits the Kv1.2 channel with similar affinity (Kd ¼ 6.4 pM) and Kv1.1 in the 86 26 nanomolar range (Kd ¼ 4.2 nM). 87 27 Based on our comprehensive data MgTX has to be considered a non-selective Kv1.3 in- 88 28 fi hibitor, and thus, experiments aiming at elucidating the signi cance of Kv1.3 in in vitro or 89 29 in vivo physiological responses have to be carefully evaluated. 90 30 © 2014 Elsevier Ltd. All rights reserved. 91 31 92 32 93 33 94 34 95 35 1. Introduction 96 36 Non-standard abbreviations: rMgTx, recombinant margatoxin (Alomone 97 37 Labs, Jerusalem, Israel, cat. No.: RTM-325, Lot: MA103); sMgTx, synthetic margatoxin (Peptide Institute Inc. Osaka, Japan, cat. No.: 4290-s, Lot: Peptide toxins isolated from animal venoms are well 98 38 Q2 560914) known blockers of the pore of plasma membrane ion 99 39 channels thereby inhibiting cellular functions including 100 40 * Corresponding author. University of Debrecen, Faculty of Medicine, action potential generation, proliferation and differentia- 101 41 Department of Biophysics and Cell Biology, 98 Nagyerdei krt., Debrecen, tion (Jimenez-Vargas et al., 2012; Pedraza Escalona and 102 42 4032, Hungary. Tel.: þ36 52 412 623 (Dept. secretary), þ36 52 411 þ Possani, 2013; Rodriguez de la Vega and Possani, 2004, 103 43 600x65617 (through operator), 36 52 411 717x65617 (through auto- Q1 matic switchboard); fax: þ36 52 532 201. 2005). This property may allow the therapeutic applica- 104 44 E-mail addresses: [email protected] (A. Bartok), agi.toth@ tion of such molecules in various diseases such as asthma, 105 45 yahoo.com (A. Toth), [email protected] (S. Somodi), szantogt@ cardiac arrhythmia, hypertension and T-cell mediated 106 46 freemail.hu (T.G. Szanto), [email protected] (P. Hajdu), panyi@ autoimmune diseases (Bergeron and Bingham, 2012; 107 47 med.unideb.hu (G. Panyi), [email protected] (Z. Varga). Chandy et al., 2004; Jimenez-Vargas et al., 2012; Panyi 108 48 URL: http://biophys.med.unideb.hu/en/node/311 109 49 http://dx.doi.org/10.1016/j.toxicon.2014.05.002 110 50 0041-0101/© 2014 Elsevier Ltd. All rights reserved. 111 þ Please cite this article in press as: Bartok, A., et al., Margatoxin is a non-selective inhibitor of human Kv1.3 K channels, Toxicon (2014), http://dx.doi.org/10.1016/j.toxicon.2014.05.002 TOXCON4827_proof ■ 31 May 2014 ■ 2/11 2 A. Bartok et al. / Toxicon xxx (2014) 1e11 1 et al., 2006) or obesity and insulin resistance (Upadhyay labeled MgTx binding assays, observed potassium current 62 2 et al., 2013). block or other biological effects of the peptide may not be 63 þ 3 K channels play a key role in the regulation of the considered as a direct proof of Kv1.3 expression. (Arkett 64 4 membrane potential of excitable and non-excitable cells et al., 1994; Li et al., 2008; Saria et al., 1998). In addition, 65 5 (Abbott, 2006; Korn and Trapani, 2005; Varga et al., 2010, MgTx shares high sequence homology with other scorpion 66 þ 6 2011). Kv1.3 is a voltage-gated K channel, which is peptides that block both Kv1.3 and Kv1.2 channels with 67 7 expressed in a variety of cells and tissues e.g. in the central high affinity (Noxiustoxin, Css20) suggesting that MgTx 68 8 nervous system, pancreatic islets, lymphocytes, etc. may be a non-selective peptide as well. 69 9 (Gutman et al., 2005). Interestingly, Kv1.3 is the dominant We conducted electrophysiological measurements with 70 þ 10 voltage-gated K channel of human T-lymphocytes and its the patch-clamp technique in voltage-clamp mode to test 71 11 expression is sensitively regulated during terminal differ- the selectivity of MgTx.
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