@article{MTMT:34797924,
	title = {Transient Receptor Potential Ankyrin 1 Ion Channel Is Expressed in Osteosarcoma and Its Activation Reduces Viability},
	url = {https://m2.mtmt.hu/api/publication/34797924},
	author = {Hudhud, Lina and Rozmer, Katalin and Kecskés, Angéla and Pohóczky, Krisztina and Bencze, Noémi and Buzás, Krisztina and Szőke, Éva and Helyes, Zsuzsanna},
	doi = {10.3390/ijms25073760},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34797924},
	issn = {1661-6596},
	abstract = {Osteosarcoma is a highly malignant, painful cancer with poor treatment opportunities and a bad prognosis. Transient receptor potential ankyrin 1 (TRPA1) and vanilloid 1 (TRPV1) receptors are non-selective cation channels that have been of great interest in cancer, as their expression is increased in some malignancies. In our study we aim to characterize the expression and functionality of the TRPA1 and TRPV1 channels in human and mouse osteosarcoma tissues and in a mouse cell line. TRPA1/Trpa1 and TRPV1/Trpv1 mRNA expressions were demonstrated by PCR gel electrophoresis and RNAscope in situ hybridization. The function of these channels was confirmed by their radioactive 45Ca2+ uptake in response to the TRPA1 agonist, Allyl-isothiocyanate (AITC), and TRPV1 agonist, capsaicin, in K7M2 cells. An ATP-based K2M7 cell viability luminescence assay was used to determine cell viability after AITC or capsaicin treatments. Both TRPA1/Trpa1 and TRPV1/Trpv1 were expressed similarly in human and mouse osteosarcoma tissues, while Trpa1 transcripts were more abundantly present in K7M2 cells. TRPA1 activation with 200 µM AITC induced a significant 45Ca2+ influx into K7M2 cells, and the antagonist attenuated this effect. In accordance with the lower Trpv1 expression, capsaicin induced a moderate 45Ca2+ uptake, which did not reach the level of statistical significance. Both AITC and capsaicin significantly reduced K7M2 cell viability, demonstrating EC50 values of 22 µM and 74 µM. The viability-decreasing effect of AITC was significantly but only partially antagonized by HC-030031, but the action of capsaicin was not affected by the TRPV1 antagonist capsazepine. We provide here the first data on the functional expression of the TRPA1 and TRPV1 ion channels in osteosarcoma, suggesting novel diagnostic and/or therapeutic perspectives.},
	keywords = {CAPSAICIN; TRPV1; Cell viability; mustard oil; TRPA1; Osteosarcoma; RNAscope in situ hybridization; radioactive 45Ca2+ uptake},
	year = {2024},
	eissn = {1422-0067},
	orcid-numbers = {Pohóczky, Krisztina/0000-0003-0385-5162; Buzás, Krisztina/0000-0001-8933-2033}
}

@article{MTMT:34766036,
	title = {Effects of Chrysin and Chrysin-7-sulfate on Ochratoxin A-Albumin Interactions and on the Plasma and Kidney Levels of the Mycotoxin in Rats},
	url = {https://m2.mtmt.hu/api/publication/34766036},
	author = {Poór, Miklós and Dombi, Ágnes and Fliszár-Nyúl, Eszter and Pedroni, Lorenzo and Dellafiora, Luca},
	doi = {10.1021/acsomega.4c01738},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {9},
	unique-id = {34766036},
	issn = {2470-1343},
	year = {2024},
	eissn = {2470-1343},
	pages = {17655-17666},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Dellafiora, Luca/0000-0002-1901-3317}
}

@article{MTMT:34719089,
	title = {The 2-aminoethyl diphenylborinate-based fluorescent method identifies quercetin and luteolin metabolites as substrates of Organic anion transporting polypeptides, OATP1B1 and OATP2B1},
	url = {https://m2.mtmt.hu/api/publication/34719089},
	author = {Kaci, Hana and Bakos, Éva and Needs, Paul W. and Kroon, Paul A. and Valentová, Kateřina and Poór, Miklós and Laczka, Csilla},
	doi = {10.1016/j.ejps.2024.106740},
	journal-iso = {EUR J PHARM SCI},
	journal = {EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES},
	unique-id = {34719089},
	issn = {0928-0987},
	abstract = {Organic anion transporting polypeptides (OATPs), OATP1B1 and OATP2B1 are membrane proteins mediating the cellular uptake of chemically diverse organic compounds. OATP1B1 is exclusively expressed in hepatocytes and plays a key role in hepatic detoxification. The ubiquitously expressed OATP2B1 promotes the intestinal absorption of orally administered drugs. Flavonoids are widely found in foods and beverages, and many of them can inhibit OATP function, resulting in food-drug interactions. In our previous work, we have shown that not only luteolin (LUT) and quercetin (Q), but also some of their metabolites can inhibit OATP1B1 and OATP2B1 activity. However, data about the potential direct transport of these flavonoids by OATPs have been incomplete. Hence, in the current study, we developed a simple, fluorescence-based method for the measurement of intracellular flavonoid levels. The method applies a cell-permeable small molecule (2-aminoethyl diphenylborinate, 2-APB), that, upon forming a complex with flavonoids, results in their fluorescence enhancement. This way the direct uptake of LUT and Q, and also their metabolites could be investigated both by confocal microscopy and in a fluorescence plate reader in living cells. With this approach we identified quercetin-3'-O-sulfate, luteolin-3'-O-glucuronide, luteolin-7-O-glucuronide and luteolin-3'-O-sulfate as substrates of both OATP1B1 and OATP2B1. Our results highlight that OATP1B1 and OATP2B1 can be key participants in the transmembrane movement of cell-permeable LUT and Q conjugates with otherwise low cell permeability. In addition, the novel method developed in this study can be a good completion to existing fluorescence-based assays to investigate OATP function.},
	year = {2024},
	eissn = {1879-0720}
}

@article{MTMT:34424543,
	title = {The Epigenetics of Neuropathic Pain: A Systematic Update},
	url = {https://m2.mtmt.hu/api/publication/34424543},
	author = {Pethő, Gábor and Kántás, Boglárka and Horváth, Ádám and Pintér, Erika},
	doi = {10.3390/ijms242417143},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34424543},
	issn = {1661-6596},
	abstract = {Epigenetics deals with alterations to the gene expression that occur without change in the nucleotide sequence in the DNA. Various covalent modifications of the DNA and/or the surrounding histone proteins have been revealed, including DNA methylation, histone acetylation, and methylation, which can either stimulate or inhibit protein expression at the transcriptional level. In the past decade, an exponentially increasing amount of data has been published on the association between epigenetic changes and the pathomechanism of pain, including its most challenging form, neuropathic pain. Epigenetic regulation of the chromatin by writer, reader, and eraser proteins has been revealed for diverse protein targets involved in the pathomechanism of neuropathic pain. They include receptors, ion channels, transporters, enzymes, cytokines, chemokines, growth factors, inflammasome proteins, etc. Most work has been invested in clarifying the epigenetic downregulation of mu opioid receptors and various K+ channels, two types of structures mediating neuronal inhibition. Conversely, epigenetic upregulation has been revealed for glutamate receptors, growth factors, and lymphokines involved in neuronal excitation. All these data cannot only help better understand the development of neuropathic pain but outline epigenetic writers, readers, and erasers whose pharmacological inhibition may represent a novel option in the treatment of pain.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Pintér, Erika/0000-0001-9898-632X}
}

@article{MTMT:34213742,
	title = {In vitro testing of host-targeting small molecule antiviral matriptase/TMPRSS2 inhibitors in 2D and 3D cell-based assays},
	url = {https://m2.mtmt.hu/api/publication/34213742},
	author = {van Eijk, Nicholas and Schmacke, Luna C. and Steinmetzer, Torsten and Pilgram, Oliver and Poór, Miklós and Pásztiné Gere, Erzsébet},
	doi = {10.1016/j.biopha.2023.115761},
	journal-iso = {BIOMED PHARMACOTHER},
	journal = {BIOMEDICINE & PHARMACOTHERAPY},
	volume = {168},
	unique-id = {34213742},
	issn = {0753-3322},
	year = {2023},
	eissn = {1950-6007},
	orcid-numbers = {van Eijk, Nicholas/0009-0007-6795-0798}
}

@article{MTMT:34212259,
	title = {Expression and function of the Transient Receptor Vanilloid 1 and Ankyrin 1 ion channels in endometriosis cell line},
	url = {https://m2.mtmt.hu/api/publication/34212259},
	author = {Toth, Norbert and Hogden, Marthe Gjerstad and Szoke, Eva and Helyes, Zsuzsanna and Pohóczky, Krisztina},
	journal-iso = {BR J PHARMACOL},
	journal = {BRITISH JOURNAL OF PHARMACOLOGY},
	volume = {180},
	unique-id = {34212259},
	issn = {0007-1188},
	year = {2023},
	eissn = {1476-5381},
	pages = {766-767},
	orcid-numbers = {Pohóczky, Krisztina/0000-0003-0385-5162}
}

@article{MTMT:34153929,
	title = {Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites.},
	url = {https://m2.mtmt.hu/api/publication/34153929},
	author = {Balázs, Orsolya and Dombi, Ágnes and Zsidó, Balázs Zoltán and Hetényi, Csaba and Valentová, Kateřina and Vida, Róbert György and Poór, Miklós},
	doi = {10.1016/j.biopha.2023.115548},
	journal-iso = {BIOMED PHARMACOTHER},
	journal = {BIOMEDICINE & PHARMACOTHERAPY},
	volume = {167},
	unique-id = {34153929},
	issn = {0753-3322},
	abstract = {Luteolin, naringenin, myricetin, and ampelopsin are abundant flavonoids in nature, and several dietary supplements also contain them at very high doses. After the peroral intake, flavonoids go through extensive presystemic biotransformation; therefore, typically their sulfate/glucuronic acid conjugates reach high concentrations in the circulation. Xanthine oxidase (XO) enzyme is involved in uric acid production, and it also takes part in the elimination of certain drugs (e.g., 6-mercaptopurine). The inhibitory effects of flavonoid aglycones on XO have been widely studied; however, only limited data are available regarding their sulfate and glucuronic acid conjugates. In this study, we examined the impacts of luteolin, naringenin, myricetin, ampelopsin, and their sulfate/glucuronide derivatives on XO-catalyzed xanthine and 6-mercaptopurine oxidations employing in vitro enzyme incubation assays and molecular modeling studies. Our major results/conclusions are the following: (1) Sulfate metabolites were stronger while glucuronic acid derivatives were weaker inhibitors of XO compared to the parent flavonoids. (2) Naringenin, ampelopsin, and their metabolites were weak inhibitors of the enzyme. (3) Luteolin, myricetin, and their sulfates were highly potent inhibitors of XO, and the glucuronides of luteolin showed moderate inhibitory impacts. (4) Conjugated metabolites of luteolin and myricetin can be involved in the inhibitory effects of these flavonoids on XO enzyme.},
	keywords = {xanthine oxidase; myricetin; luteolin; naringenin; ampelopsin; Flavonoid conjugates},
	year = {2023},
	eissn = {1950-6007},
	orcid-numbers = {Vida, Róbert György/0000-0003-1176-0251}
}

@article{MTMT:34067941,
	title = {Synthesis and in vitro photodynamic activity of aza-BODIPY-based photosensitizers},
	url = {https://m2.mtmt.hu/api/publication/34067941},
	author = {Hlogyik, Tamás and Laczkó-Rigó, Réka and Bakos, Éva and Poór, Miklós and Kele, Zoltán and Laczka, Csilla and Mernyák, Erzsébet},
	doi = {10.1039/d3ob00699a},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {21},
	unique-id = {34067941},
	issn = {1477-0520},
	abstract = {Aza-BODIPY dyes have recently come to attention owing to their excellent chemical and photophysical properties. In particular, their absorption and emission maxima can efficiently be shifted to the red or even to the NIR spectral region. On this basis, aza-BODIPY derivatives are widely investigated as fluorescent probes or phototherapeutic agents. Here we report the synthesis of a set of novel aza-BODIPY derivatives as potential photosensitizers for use in photodynamic therapy. Triazolyl derivatives were obtained via Cu(I)-catalyzed azide-alkyne cycloaddition as the key step. In vitro photodynamic activities of the newly synthesized compounds were evaluated on the A431 human epidermoid carcinoma cell line. Structural differences influenced the light-induced toxicity of the test compounds markedly. Compared to the initial tetraphenyl aza-BODIPY derivative, the compound bearing two hydrophilic triethylene glycol side chains showed substantial, more than 250-fold, photodynamic activity with no dark toxicity. Our newly synthesized aza-BODIPY derivative, acting in the nanomolar range, might serve as a promising candidate for the design of more active and selective photosensitizers.},
	year = {2023},
	eissn = {1477-0539},
	pages = {6018-6027},
	orcid-numbers = {Kele, Zoltán/0000-0002-4401-0302; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:33777591,
	title = {Interaction of Fumonisin B1, N-Palmitoyl-Fumonisin B1, 5-O-Palmitoyl-Fumonisin B1, and Fumonisin B4 Mycotoxins with Human Serum Albumin and Their Toxic Impacts on Zebrafish Embryos},
	url = {https://m2.mtmt.hu/api/publication/33777591},
	author = {Csenki, Zsolt Imre and Bartók, Tibor and Bock, Illés and Horváth, Levente and Lemli, Beáta and Zsidó, Balázs Zoltán and Angeli, Cserne and Hetényi, Csaba and Szabó, István and Urbányi, Béla and Kovács, Melinda and Poór, Miklós},
	doi = {10.3390/biom13050755},
	journal-iso = {BIOMOLECULES},
	journal = {BIOMOLECULES},
	volume = {13},
	unique-id = {33777591},
	issn = {2218-273X},
	keywords = {human serum albumin; Fumonisin B1; ZEBRAFISH EMBRYOS; N-palmitoyl-fumonisin B; 5-O-palmitoyl-fumonisin B1; fumonisin B4},
	year = {2023},
	eissn = {2218-273X},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337; Szabó, István/0000-0002-3954-799X; Kovács, Melinda/0000-0001-5988-3934}
}

@article{MTMT:33722503,
	title = {Probing the Interactions of 31 Mycotoxins with Xanthine Oxidase: Alternariol, Alternariol-3-Sulfate, and α-Zearalenol Are Allosteric Inhibitors of the Enzyme},
	url = {https://m2.mtmt.hu/api/publication/33722503},
	author = {Balázs, Orsolya and Dombi, Ágnes and Zsidó, Balázs Zoltán and Hetényi, Csaba and Vida, Róbert György and Poór, Miklós},
	doi = {10.3390/toxins15040250},
	journal-iso = {TOXINS},
	journal = {TOXINS},
	volume = {15},
	unique-id = {33722503},
	issn = {2072-6651},
	year = {2023},
	eissn = {2072-6651},
	orcid-numbers = {Vida, Róbert György/0000-0003-1176-0251}
}