TY - JOUR AU - Oláh, Zoltán AU - Rédei, Dóra AU - Pecze, László AU - Vizler, Csaba AU - Jósvay, Katalin AU - Forgó, Péter AU - Winter, Zoltán AU - Dombi, György AU - Szakonyi, Gerda AU - Hohmann, Judit TI - Pellitorine, an extract of Tetradium daniellii, is an antagonist of the ion channel TRPV1 JF - PHYTOMEDICINE: INTERNATIONAL JOURNAL OF PHYTOTHERAPY AND PHYTOPHARMACOLOGY J2 - PHYTOMEDICINE VL - 34 PY - 2017 SP - 44 EP - 49 PG - 6 SN - 0944-7113 DO - 10.1016/j.phymed.2017.06.006 UR - https://m2.mtmt.hu/api/publication/3260664 ID - 3260664 LA - English DB - MTMT ER - TY - JOUR AU - Hetényi, Anasztázia AU - Németh, Lukács AU - Wéber, Edit AU - Szakonyi, Gerda AU - Winter, Zoltán AU - Jósvay, Katalin AU - Bartus, Éva AU - Oláh, Zoltán AU - Martinek, Tamás TI - Competitive inhibition of TRPV1 – calmodulin interaction by vanilloids JF - FEBS LETTERS J2 - FEBS LETT VL - 590 PY - 2016 IS - 16 SP - 2768 EP - 2775 PG - 8 SN - 0014-5793 DO - 10.1002/1873-3468.12267 UR - https://m2.mtmt.hu/api/publication/3087152 ID - 3087152 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet Program [LP-2011-009]; MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. [TP7-017]; Hungarian Research Foundation [OTKA K112442]; Richter Gedeon Talentum Alapitvany; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/ 2-11/1-2012-0001]\n Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet Program (LP-2011-009), MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. (TP7-017), the Hungarian Research Foundation (OTKA K112442) and Financial support from Richter Gedeon Talentum Alapitvany (Ph.D. Scholarship to E.B.). This research was supported by the European Union and the State of Hungary, cofinanced by the European Social Fund in the framework of TAMOP-4.2.4.A/ 2-11/1-2012-0001 'National Excellence Program'.\n Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet Program [LP-2011-009]; MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. [TP7-017]; Hungarian Research Foundation [OTKA K112442]; Richter Gedeon Talentum Alapitvany; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/ 2-11/1-2012-0001] Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet Program (LP-2011-009), MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. (TP7-017), the Hungarian Research Foundation (OTKA K112442) and Financial support from Richter Gedeon Talentum Alapitvany (Ph.D. Scholarship to E.B.). This research was supported by the European Union and the State of Hungary, cofinanced by the European Social Fund in the framework of TAMOP-4.2.4.A/ 2-11/1-2012-0001 'National Excellence Program'. AB - There is enormous interest toward vanilloid agonists of the pain receptor TRPV1 in analgesic therapy, but the mechanisms of their sensory neuron-blocking effects at high or repeated doses are still a matter of debate. Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1-calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin-protein interactions. These results draw attention to a previously unknown vanilloid target, which may contribute to the explanation of the paradoxical pain-modulating behavior of these important pharmacons. LA - English DB - MTMT ER - TY - JOUR AU - Jósvay, Katalin AU - Winter, Zoltán AU - Katona, Róbert László AU - Pecze, László AU - Marton, Annamária AU - Buhala, Andrea AU - Szakonyi, Gerda AU - Oláh, Zoltán AU - Vizler, Csaba TI - Besides neuro-imaging, the Thy1-YFP mouse could serve for visualizing experimental tumours, inflammation and wound-healing JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 4 PY - 2014 SP - 6776 PG - 7 SN - 2045-2322 DO - 10.1038/srep06776 UR - https://m2.mtmt.hu/api/publication/2763894 ID - 2763894 AB - The B6.Cg-Tg(Thy1-YFP)16Jrs/J transgenic mouse strain, widely used to study neuronal development and regeneration, expresses the yellow fluorescent protein (YFP) in the peripheral nerves and the central nervous system under the control of regulatory sequences of the Thy1 gene. The Thy1 (CD90) cell surface glycoprotein is present on many cell types besides neurons, and is known to be involved in cell adhesion, migration and signal transduction. We hypothesized that Thy1-activating conditions could probably activate the truncated Thy1 regulatory sequences used in the Thy1-YFP construct, resulting in YFP transgene expression outside the nervous system. We demonstrated that the stroma of subcutaneous tumours induced by the injection of 4T1 or MC26 carcinoma cells into BALB/c(Thy1-YFP) mice, carrying the same construct, indeed expressed the YFP transgene. In the tumour mass, the yellow-green fluorescent stromal cells were clearly distinguishable from 4T1 carcinoma cells stably transfected with red fluorescent protein. Local inflammation induced by subcutaneous injection of complete Freund's adjuvant, as well as the experimental wound-healing milieu, also triggered YFP fluorescence in both the BALB/c(Thy1-YFP) and B6.Cg-Tg(Thy1-YFP)16Jrs/J mice, pointing to eventual overlapping pathways of wound-healing, inflammation and tumour growth. LA - English DB - MTMT ER - TY - THES AU - Winter, Zoltán TI - Investigation of the transient receptor potential vanilloid 1 (TRPV1) ion channel PB - Szegedi Tudományegyetem (SZTE) PY - 2013 SP - 58 DO - 10.14232/phd.1885 UR - https://m2.mtmt.hu/api/publication/2852024 ID - 2852024 N1 - 3. Témavezető: Oláh Zoltán (biokémia) LA - English DB - MTMT ER - TY - JOUR AU - Winter, Zoltán AU - Buhala, Andrea AU - Ötvös, Ferenc AU - Jósvay, Katalin AU - Vizler, Csaba AU - Dombi, György AU - Szakonyi, Gerda AU - Oláh, Zoltán TI - Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel – an overview of the current mutational data JF - MOLECULAR PAIN J2 - MOL PAIN VL - 9 PY - 2013 IS - 1 PG - 29 SN - 1744-8069 DO - 10.1186/1744-8069-9-30 UR - https://m2.mtmt.hu/api/publication/2341377 ID - 2341377 LA - English DB - MTMT ER - TY - JOUR AU - Pecze, László AU - Winter, Zoltán AU - Jósvay, Katalin AU - Ötvös, Ferenc AU - Kolozsi, Csongor AU - Vizler, Csaba AU - Budai, D AU - Letoha, Tamás AU - Dombi, György AU - Szakonyi, Gerda AU - Oláh, Zoltán TI - Divalent Heavy Metal Cations Block the TRPV1 Ca2+ Channel JF - BIOLOGICAL TRACE ELEMENT RESEARCH J2 - BIOL TRACE ELEM RES VL - 151 PY - 2013 IS - 3 SP - 451 EP - 461 PG - 11 SN - 0163-4984 DO - 10.1007/s12011-012-9570-y UR - https://m2.mtmt.hu/api/publication/2192154 ID - 2192154 N1 - Received: 4 May 2012 / Accepted: 3 December 2012 AB - Transient receptor potential vanilloid 1 (TRPV1) is a non- selective cation channel involved in pain sensation and in a wide range of non-pain-related physiological and pathological conditions. The aim of the present study was to explore the effects of selected heavy metal cations on the function of TRPV1. The cations ranked in the following sequence of pore- blocking activity: Co(2+) [half-maximal inhibitory concentration (IC(50)) = 13 muM] > Cd(2+) (IC(50) = 38 muM) > Ni(2+) (IC(50) = 62 muM) > Cu(2+) (IC(50) = 200 muM). Zn(2+) proved to be a weak (IC(50) = 27 muM) and only partial inhibitor of the channel function, whereas Mg(2+), Mn(2+) and La(3+) did not exhibit any substantial effect. Co(2+), the most potent channel blocker, was able not only to compete with Ca(2+) but also to pass with it through the open channel of TRPV1. In response to heat activation or vanilloid treatment, Co(2+) accumulation was verified in TRPV1-transfected cell lines and in the TRPV1+ dorsal root ganglion neurons. The inhibitory effect was also demonstrated in vivo. Co(2+) applied together with vanilloid agonists attenuated the nocifensive eye wipe response in mice. Different rat TRPV1 pore point mutants (Y627W, N628W, D646N and E651W) were created that can validate the binding site of previously used channel blockers in agonist-evoked (45)Ca(2+) influx assays in cells expressing TRPV1. The IC(50) of Co(2+) on these point mutants were determined to be reasonably comparable to those on the wild type, which suggests that divalent cations passing through the TRPV1 channel use the same negatively charged amino acids as Ca(2+). LA - English DB - MTMT ER - TY - JOUR AU - Pecze, László AU - Pelsőczi, Péter AU - Kecskés, Miklós AU - Winter, Zoltán AU - Papp, András AU - Kaszas, K AU - Letoha, Tamás AU - Vizler, Csaba AU - Oláh, Zoltán TI - Resiniferatoxin mediated ablation of TRPV1+ neurons removes TRPA1 as well JF - CANADIAN JOURNAL OF NEUROLOGICAL SCIENCES / JOURNAL CANADIEN DES SCIENCES NEUROLOGIQUES J2 - CAN J NEUROL SCI VL - 36 PY - 2009 IS - 2 SP - 234 EP - 241 PG - 8 SN - 0317-1671 DO - 10.1017/S0317167100006600 UR - https://m2.mtmt.hu/api/publication/1918262 ID - 1918262 LA - English DB - MTMT ER -