@article{MTMT:34430365,
	title = {Phenol-Soluble Modulin α3 Stimulates Autophagy in HaCaT Keratinocytes},
	url = {https://m2.mtmt.hu/api/publication/34430365},
	author = {Dernovics, Áron and Seprényi, György and Rázga, Zsolt and Ayaydin, Ferhan and Veréb, Zoltán and Megyeri, Klára},
	doi = {10.3390/biomedicines11113018},
	journal-iso = {BIOMEDICINES},
	journal = {BIOMEDICINES},
	volume = {11},
	unique-id = {34430365},
	year = {2023},
	eissn = {2227-9059},
	orcid-numbers = {Rázga, Zsolt/0000-0003-4717-8482; Veréb, Zoltán/0000-0002-9518-2155}
}

@CONFERENCE{MTMT:33570390,
	title = {Post-diaminoenzidine treatments for double stainings : extension of sulfide-silver-gold internsification for light and fluorescent microscopy},
	url = {https://m2.mtmt.hu/api/publication/33570390},
	author = {Apróné Török, Ibolya and Seprényi, György and Pór, Erzsébet and Emőke, Borbély and Szögi, Titanilla and Dobó, Endre},
	booktitle = {Magyar Anatómus Társaság 2022. évi konferenciája},
	unique-id = {33570390},
	year = {2022},
	pages = {60-61},
	orcid-numbers = {Apróné Török, Ibolya/0000-0002-2441-8925; Szögi, Titanilla/0000-0002-9854-7340}
}

@article{MTMT:32470367,
	title = {IL-36α and Lipopolysaccharide Cooperatively Induce Autophagy by Triggering Pro-Autophagic Biased Signaling},
	url = {https://m2.mtmt.hu/api/publication/32470367},
	author = {Al-Luhaibi, Zaid and Dernovics, Áron and Seprényi, György and Ayaydin, Ferhan and Boldogkői, Zsolt and Veréb, Zoltán and Megyeri, Klára},
	doi = {10.3390/biomedicines9111541},
	journal-iso = {BIOMEDICINES},
	journal = {BIOMEDICINES},
	volume = {9},
	unique-id = {32470367},
	abstract = {Autophagy is an intracellular catabolic process that controls infections both directly and indirectly via its multifaceted effects on the innate and adaptive immune responses. It has been reported that LPS stimulates this cellular process, whereas the effect of IL-36 alpha on autophagy remains largely unknown. We therefore investigated how IL-36 alpha modulates the endogenous and LPS-induced autophagy in THP-1 cells. The levels of LC3B-II and autophagic flux were determined by Western blotting. The intracellular localization of LC3B was measured by immunofluorescence assay. The activation levels of signaling pathways implicated in autophagy regulation were evaluated by using a phosphokinase array. Our results showed that combined IL-36 alpha and LPS treatment cooperatively increased the levels of LC3B-II and Beclin-1, stimulated the autophagic flux, facilitated intracellular redistribution of LC3B, and increased the average number of autophagosomes per cell. The IL36 alpha/LPS combined treatment increased phosphorylation of STAT5a/b, had minimal effect on the Akt/PRAS40/mTOR pathway, and reduced the levels of phospho-Yes, phospho-FAK, and phospho-WNK1. Thus, this cytokine/PAMP combination triggers pro-autophagic biased signaling by several mechanisms and thus cooperatively stimulates the autophagic cascade. An increased autophagic activity of innate immune cells simultaneously exposed to IL-36 alpha and LPS may play an important role in the pathogenesis of Gram-negative bacterial infections.},
	year = {2021},
	eissn = {2227-9059},
	orcid-numbers = {Boldogkői, Zsolt/0000-0003-1184-7293}
}

@article{MTMT:31439812,
	title = {Post-diaminobenzidine Treatments for Double Stainings. Extension of Sulfide-Silver-Gold Intensification for Light and Fluorescent Microscopy},
	url = {https://m2.mtmt.hu/api/publication/31439812},
	author = {Apróné Török, Ibolya and Seprényi, György and Pór, Erzsébet and Borbély, Emőke and Szögi, Titanilla and Dobó, Endre},
	doi = {10.1369/0022155420942213},
	journal-iso = {J HISTOCHEM CYTOCHEM},
	journal = {JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY},
	volume = {68},
	unique-id = {31439812},
	issn = {0022-1554},
	abstract = {Double staining protocols using the most popular immunoperoxidase techniques may raise difficulties. The two ordinary detection systems may cross-talk, when the primary antibodies are derived from phylogenetically closely related animals. A color shift of the 3,3 '-diaminobenzidine (DAB) polymer may occur during the second development, resulting in poor distinction between the two kinds of deposits. A post-DAB technique, sulfide-silver-gold intensification, was fine tuned to eliminate these difficulties, which may be especially suitable for colocalization of cell nuclei and perikarya of the same cells. The revised method was probed in combination with a subsequent other immunoperoxidase step or fluorochrome-tagged reagents. The nuclear antigens (BrdU, c-Fos, and Prox-1) were first visualized with DAB polymer, which were then treated with SSGI, turning the deposit black. Thereafter, cytoplasmic antigens (doublecortin, neuronal nuclei, and calbindin) were detected with either another immunoperoxidase using DAB again or immunofluorescence labeling. In both approaches, the immunopositive nuclei and cytoplasmic sites could be easily distinguished even at low magnifications. Different shielding or eluting posttreatments were compared for consecutive acetylcholinesterase histochemistry terminated with DAB development and immunohistochemistry in the same sections. In conclusion, we recommend post-DAB treatments that abolish interactions between detection systems and allow clear distinction between the two signals under various conditions:},
	keywords = {immunohistochemistry; immunofluorescence; silver enhancement; DAB; Double staining; Diisopropyl fluorophosphate; acetylcholinesterase histochemistry},
	year = {2020},
	eissn = {1551-5044},
	pages = {571-582},
	orcid-numbers = {Apróné Török, Ibolya/0000-0002-2441-8925; Szögi, Titanilla/0000-0002-9854-7340}
}

@misc{MTMT:30433688,
	title = {Peroxidáz alapú technika alkalmazása nukleáris és citoplazmatikus antigének egymás melletti kimutatására fény- és fluoreszcens mikroszkópiában},
	url = {https://m2.mtmt.hu/api/publication/30433688},
	author = {Apróné Török, Ibolya and Seprényi, György and Borbély, Emőke and Szögi, Titanilla and Hegyi, Péter and Dobó, Endre},
	unique-id = {30433688},
	year = {2018},
	orcid-numbers = {Apróné Török, Ibolya/0000-0002-2441-8925; Szögi, Titanilla/0000-0002-9854-7340}
}

@article{MTMT:30312141,
	title = {Cerebrovascular Pathology in Hypertriglyceridemic APOB-100 Transgenic Mice},
	url = {https://m2.mtmt.hu/api/publication/30312141},
	author = {Hoyk, Zsófia and Tóth, Erzsébet Melinda and Lénárt, Nikolett and Nagy, Dóra and Dukay, Brigitta and Csefová, Alexandra and Zvara, Ágnes and Seprényi, György and Kincses, András and Walter, Fruzsina and Veszelka, Szilvia and Vigh, Judit Piroska and Barabási, Beáta and Harazin, András and Kittel, Ágnes and Puskás, László and Penke, Botond and Vigh, László and Deli, Mária Anna and Sántha, Miklós},
	doi = {10.3389/fncel.2018.00380},
	journal-iso = {FRONT CELL NEUROSCI},
	journal = {FRONTIERS IN CELLULAR NEUROSCIENCE},
	volume = {12},
	unique-id = {30312141},
	issn = {1662-5102},
	abstract = {Hypertriglyceridemia is not only a serious risk factor in the development of cardiovascular diseases, but it is linked to neurodegeneration, too. Previously, we generated transgenic mice overexpressing the human APOB-100 protein, a mouse model of human atherosclerosis. In this model we observed high plasma levels of triglycerides, oxidative stress, tau hyperphosphorylation, synaptic dysfunction, cognitive impairment, increased neural apoptosis and neurodegeneration. Neurovascular dysfunction is recognized as a key factor in the development of neurodegenerative diseases, but the cellular and molecular events linking cerebrovascular pathology and neurodegeneration are not fully understood. Our aim was to study cerebrovascular changes in APOB-100 transgenic mice. We described the kinetics of the development of chronic hypertriglyceridemia in the transgenic animals. Increased blood-brain barrier permeability was found in the hippocampus of APOB-100 transgenic mice which was accompanied by structural changes. Using transmission electron microscopy, we detected changes in the brain capillary endothelial tight junction structure and edematous swelling of astrocyte endfeet. In brain microvessels isolated from APOB-100 transgenic animals increased Lox-1, Aqp4, and decreased Meox-2, Mfsd2a, Abcb1a, Lrp2, Glut-1, Nos2, Nos3, Vim, and in transgenic brains reduced Cdh2 and Gfap-σ gene expressions were measured using quantitative real-time PCR. We confirmed the decreased P-glycoprotein (ABCB1) and vimentin expression related to the neurovascular unit by immunostaining in transgenic brain sections using confocal microscopy. We conclude that in chronic hypertriglyceridemic APOB-100 transgenic mice both functional and morphological cerebrovascular pathology can be observed, and this animal model could be a useful tool to study the link between cerebrovascular pathology and neurodegeneration.},
	keywords = {P-GLYCOPROTEIN; Blood-Brain Barrier; HYPERTRIGLYCERIDEMIA; tight junction; astroglia; Apolipoprotein B-100; Brain endothelial cell; cerebrovascular pathology},
	year = {2018},
	eissn = {1662-5102},
	orcid-numbers = {Lénárt, Nikolett/0000-0002-7456-949X; Walter, Fruzsina/0000-0001-8145-2823; Harazin, András/0000-0002-0904-5606; Penke, Botond/0000-0003-0938-0567; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:3300946,
	title = {Propionibacterium acnes induces autophagy in keratinocytes: involvement of multiple mechanisms},
	url = {https://m2.mtmt.hu/api/publication/3300946},
	author = {Megyeri, Klára and Orosz, László and Bolla, Beáta Szilvia and Erdei, Lilla and Rázga, Zsolt and Seprényi, György and Zsoldiné Urbán, Edit and Szabó, Kornélia Ágnes and Kemény, Lajos},
	doi = {10.1016/j.jid.2017.11.018},
	journal-iso = {J INVEST DERMATOL},
	journal = {JOURNAL OF INVESTIGATIVE DERMATOLOGY},
	volume = {138},
	unique-id = {3300946},
	issn = {0022-202X},
	abstract = {Propionibacterium acnes is a dominant member of the cutaneous microbiota. Herein, we evaluate the effects of different P. acnes strains and propionic acid on autophagy in keratinocytes. Our results showed that P. acnes strain 889 altered the architecture of the mitochondrial network, elevated the levels of LC3B-II, Beclin-1 and phospho-AMPKalpha, stimulated autophagic flux, facilitated intracellular redistribution of LC3B, increased average number of autophagosomes per cell, and enhanced development of acidic vesicular organelles in the HPV-KER cell line. Propionic acid increased the level of phospho-AMPKalpha, enhanced lipidation of LC3B, stimulated autophagic flux, as well as facilitated translocation of LC3B into autophagosomes in HPV-KER cells. P. acnes strains 889, 6609 and heat-killed strain 889 also stimulated autophagosome formation in primary keratinocytes to varying degrees. These results indicate that cell wall components and secreted propionic acid metabolite of P. acnes evoke mitochondrial damage successively, thereby trigger AMPK-associated activation of autophagy, which in turn facilitates the removal of dysfunctional mitochondria and promotes survival of keratinocytes. Thus, we suggest that low-level colonization of hair follicles with non-invasive P. acnes strains, by triggering a local increase in autophagic activity, might exert a profound effect on several physiological processes responsible for the maintenance of skin tissue homeostasis.},
	year = {2018},
	eissn = {1523-1747},
	pages = {750-759},
	orcid-numbers = {Erdei, Lilla/0000-0001-8129-2364; Rázga, Zsolt/0000-0003-4717-8482; Zsoldiné Urbán, Edit/0000-0002-9602-7552; Szabó, Kornélia Ágnes/0000-0002-6231-3251; Kemény, Lajos/0000-0002-2119-9501}
}

@article{MTMT:3280809,
	title = {Calcium Activated Chloride Current in Mammalian Ventricular Myocytes},
	url = {https://m2.mtmt.hu/api/publication/3280809},
	author = {Magyar, János and Horváth, Balázs and Vaczi, K and Hegyi, Bence and Gönczi, Mónika and Dienes, Beatrix and Kistamás, Kornél and Bányász, Tamás and Baczkó, István and Varró, András and Seprényi, György and Csernoch, László and Nánási, Péter Pál and Szentandrássy, Norbert},
	doi = {10.1016/j.bpj.2016.11.227},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {112},
	unique-id = {3280809},
	issn = {0006-3495},
	year = {2017},
	eissn = {1542-0086},
	pages = {36A-36A},
	orcid-numbers = {Horváth, Balázs/0000-0003-2562-8446; Baczkó, István/0000-0002-9588-0797; Varró, András/0000-0003-0745-3603; Szentandrássy, Norbert/0000-0003-0197-9567}
}

@article{MTMT:3280807,
	title = {Recent advances in research of cardiac calcium-activated chloride channels},
	url = {https://m2.mtmt.hu/api/publication/3280807},
	author = {Szentandrássy, Norbert and Hegyi, Bence and Horváth, Balázs and Vaczi, K and Gönczi, Mónika and Dienes, Beatrix and Kistamás, Kornél and Veress, Roland and Ruzsnavszky, Ferenc and Bányász, Tamás and Magyar, János and Baczkó, István and Varró, András and Seprényi, György and Csernoch, László and Nánási, Péter Pál},
	journal-iso = {ACTA PHYSIOL},
	journal = {ACTA PHYSIOLOGICA},
	volume = {221},
	unique-id = {3280807},
	issn = {1748-1708},
	year = {2017},
	eissn = {1748-1716},
	pages = {22-22},
	orcid-numbers = {Szentandrássy, Norbert/0000-0003-0197-9567; Horváth, Balázs/0000-0003-2562-8446; Baczkó, István/0000-0002-9588-0797; Varró, András/0000-0003-0745-3603}
}

@article{MTMT:3066993,
	title = {Sarcolemmal Ca2+-entry through L-type Ca2+ channels controls the profile of Ca2+-activated Cl- current in canine ventricular myocytes.},
	url = {https://m2.mtmt.hu/api/publication/3066993},
	author = {Horváth, Balázs and Váczi, Krisztina and Hegyi, Bence and Gönczi, Mónika and Dienes, Beatrix and Kistamás, Kornél and Bányász, Tamás and Magyar, János and Baczkó, István and Varró, András and Seprényi, György and Csernoch, László and Nánási, Péter Pál and Szentandrássy, Norbert},
	doi = {10.1016/j.yjmcc.2016.05.006},
	journal-iso = {J MOL CELL CARDIOL},
	journal = {JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY},
	volume = {97},
	unique-id = {3066993},
	issn = {0022-2828},
	abstract = {Ca2+-activated Cl- current (ICl(Ca)) mediated by TMEM16A and/or Bestrophin-3 may contribute to cardiac arrhythmias. The true profile of ICl(Ca) during an actual ventricular action potential (AP), however, is poorly understood. We aimed to study the profile of ICl(Ca) systematically under physiological conditions (normal Ca2+ cycling and AP voltage-clamp) as well as in conditions designed to change [Ca2+]i. The expression of TMEM16A and/or Bestrophin-3 in canine and human left ventricular myocytes was examined. The possible spatial distribution of these proteins and their co-localization with Cav1.2 was also studied. The profile of ICl(Ca), identified as a 9-anthracene carboxylic acid-sensitive current under AP voltage-clamp conditions, contained an early fast outward and a late inward component, overlapping early and terminal repolarizations, respectively. Both components were moderately reduced by ryanodine, while fully abolished by BAPTA, but not EGTA. [Ca2+]i was monitored using Fura-2-AM. Setting [Ca2+]i to the systolic level measured in the bulk cytoplasm (1.1muM) decreased ICl(Ca), while application of Bay K8644, isoproterenol, and faster stimulation rates increased the amplitude of ICl(Ca). Ca2+-entry through L-type Ca2+ channels was essential for activation of ICl(Ca). TMEM16A and Bestrophin-3 showed strong co-localization with one another and also with Cav1.2 channels, when assessed using immunolabeling and confocal microscopy in both canine myocytes and human ventricular myocardium. Activation of ICl(Ca) in canine ventricular cells requires Ca2+-entry through neighboring L-type Ca2+ channels and is only augmented by SR Ca2+-release. Substantial activation of ICl(Ca) requires high Ca2+ in the dyadic clefts which can be effectively buffered by BAPTA, but not EGTA.},
	year = {2016},
	eissn = {1095-8584},
	pages = {125-139},
	orcid-numbers = {Horváth, Balázs/0000-0003-2562-8446; Baczkó, István/0000-0002-9588-0797; Varró, András/0000-0003-0745-3603; Szentandrássy, Norbert/0000-0003-0197-9567}
}