TY - JOUR AU - Dernovics, Áron AU - Seprényi, György AU - Rázga, Zsolt AU - Ayaydin, Ferhan AU - Veréb, Zoltán AU - Megyeri, Klára TI - Phenol-Soluble Modulin α3 Stimulates Autophagy in HaCaT Keratinocytes JF - BIOMEDICINES J2 - BIOMEDICINES VL - 11 PY - 2023 IS - 11 PG - 18 SN - 2227-9059 DO - 10.3390/biomedicines11113018 UR - https://m2.mtmt.hu/api/publication/34430365 ID - 34430365 N1 - Department of Medical Microbiology, Albert Szent-Györgyi Medical School, University of Szeged, Dóm tér 10., Szeged, H-6720, Hungary Department of Anatomy, Histology and Embryology, Albert Szent-Györgyi Medical School, University of Szeged, Kossuth L. sgt. 40, Szeged, H-6724, Hungary Department of Pathology, University of Szeged, Állomás u. 2, Szeged, H-6720, Hungary Hungarian Centre of Excellence for Molecular Medicine (HCEMM) Nonprofit Ltd., Római krt. 21., Szeged, H-6723, Hungary Laboratory of Cellular Imaging, Biological Research Centre, Eötvös Loránd Research Network, Temesvári krt. 62., Szeged, H-6726, Hungary Regenerative Medicine and Cellular Pharmacology Laboratory, Department of Dermatology and Allergology, University of Szeged, Korányi Fasor 6, Szeged, H-6720, Hungary University of Szeged, Szeged, Biobank, H-6720, Hungary Interdisciplinary Research Development and Innovation Center of Excellence, University of Szeged, Szeged, H-6720, Hungary Export Date: 12 December 2023 Correspondence Address: Megyeri, K.; Department of Medical Microbiology, Dóm tér 10., Hungary; email: megyeri.klara@med.u-szeged.hu LA - English DB - MTMT ER - TY - CONF AU - Apróné Török, Ibolya AU - Seprényi, György AU - Pór, Erzsébet AU - Emőke, Borbély AU - Titanilla, Szögi AU - Dobó, Endre TI - Post-diaminoenzidine treatments for double stainings : extension of sulfide-silver-gold internsification for light and fluorescent microscopy T2 - Magyar Anatómus Társaság 2022. évi konferenciája PY - 2022 SP - 60 PG - 1 UR - https://m2.mtmt.hu/api/publication/33570390 ID - 33570390 LA - English DB - MTMT ER - TY - JOUR AU - Al-Luhaibi, Zaid AU - Dernovics, Áron AU - Seprényi, György AU - Ayaydin, Ferhan AU - Boldogkői, Zsolt AU - Veréb, Zoltán AU - Megyeri, Klára TI - IL-36α and Lipopolysaccharide Cooperatively Induce Autophagy by Triggering Pro-Autophagic Biased Signaling JF - BIOMEDICINES J2 - BIOMEDICINES VL - 9 PY - 2021 IS - 11 PG - 16 SN - 2227-9059 DO - 10.3390/biomedicines9111541 UR - https://m2.mtmt.hu/api/publication/32470367 ID - 32470367 N1 - Funding Agency and Grant Number: Tempus Kozalapitvany (Stipendium Hungaricum scholarship) [SHE-03673-007/2016, 109162]; European UnionEuropean Commission [EFOP-3.6.1-16-2016-00008, 739593]; European Regional Development FundEuropean Commission; University of SzegedEuropean Commission [5514] Funding text: This research was funded by the Tempus Kozalapitvany (Stipendium Hungaricum scholarship) SHE-03673-007/2016, grant number 109162, and by the EFOP-3.6.1-16-2016-00008 project co-financed by the European Union and the European Regional Development Fund. The APC was funded by the University of Szeged Open Access Fund, grant number 5514, and the EFOP-3.6.1-16-2016-00008 project co-financed by the European Union and the European Regional Development Fund. Z.I.I.A. was funded by Tempus Kozalapitvany (Stipendium Hungaricum scholarship) SHE-03673-007/2016, grant number 109162. F.A. was funded by EU's Horizon 2020, grant number 739593. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Apróné Török, Ibolya AU - Seprényi, György AU - Pór, Erzsébet AU - Borbély, Emőke AU - Szögi, Titanilla AU - Dobó, Endre TI - Post-diaminobenzidine Treatments for Double Stainings. Extension of Sulfide-Silver-Gold Intensification for Light and Fluorescent Microscopy TS - Extension of Sulfide-Silver-Gold Intensification for Light and Fluorescent Microscopy JF - JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY J2 - J HISTOCHEM CYTOCHEM VL - 68 PY - 2020 IS - 8 SP - 571 EP - 582 PG - 12 SN - 0022-1554 DO - 10.1369/0022155420942213 UR - https://m2.mtmt.hu/api/publication/31439812 ID - 31439812 N1 - Department of Anatomy, Faculty of Medicine, University of Szeged, Szeged, Hungary Department of Medical Chemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary Export Date: 31 March 2021 CODEN: JHCYA Correspondence Address: Dobó, E.; Department of Anatomy, Hungary; email: dobo.endre@med.u-szeged.hu Chemicals/CAS: diaminobenzidine, 7411-49-6, 91-95-2; peroxidase, 9003-99-0; gold, 7440-57-5; 3,3'-Diaminobenzidine; Gold; Silver Compounds; silver sulfide Funding text 1: The author(s) disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: This study was supported by the Department of Anatomy, Faculty of Medicine, University of Szeged funds. Department of Anatomy, Faculty of Medicine, University of Szeged, Szeged, Hungary Department of Medical Chemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary Export Date: 14 April 2021 CODEN: JHCYA Correspondence Address: Dobó, E.; Department of Anatomy, Hungary; email: dobo.endre@med.u-szeged.hu Chemicals/CAS: diaminobenzidine, 7411-49-6, 91-95-2; peroxidase, 9003-99-0; gold, 7440-57-5; 3,3'-Diaminobenzidine; Gold; Silver Compounds; silver sulfide Funding text 1: The author(s) disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: This study was supported by the Department of Anatomy, Faculty of Medicine, University of Szeged funds. Department of Anatomy, Faculty of Medicine, University of Szeged, Szeged, Hungary Department of Medical Chemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary Export Date: 20 April 2021 CODEN: JHCYA Correspondence Address: Dobó, E.; Department of Anatomy, Hungary; email: dobo.endre@med.u-szeged.hu Chemicals/CAS: diaminobenzidine, 7411-49-6, 91-95-2; peroxidase, 9003-99-0; gold, 7440-57-5; 3,3'-Diaminobenzidine; Gold; Silver Compounds; silver sulfide Funding text 1: The author(s) disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: This study was supported by the Department of Anatomy, Faculty of Medicine, University of Szeged funds. Department of Anatomy, Faculty of Medicine, University of Szeged, Szeged, Hungary Department of Medical Chemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary Export Date: 23 April 2021 CODEN: JHCYA Correspondence Address: Dobó, E.; Department of Anatomy, Hungary; email: dobo.endre@med.u-szeged.hu Chemicals/CAS: diaminobenzidine, 7411-49-6, 91-95-2; peroxidase, 9003-99-0; gold, 7440-57-5; 3,3'-Diaminobenzidine; Gold; Silver Compounds; silver sulfide Funding text 1: The author(s) disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: This study was supported by the Department of Anatomy, Faculty of Medicine, University of Szeged funds. AB - 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: LA - English DB - MTMT ER - TY - GEN AU - Apróné Török, Ibolya AU - Seprényi, György AU - Borbély, Emőke AU - Szögi, Titanilla AU - Hegyi, Péter AU - Dobó, Endre TI - Peroxidáz alapú technika alkalmazása nukleáris és citoplazmatikus antigének egymás melletti kimutatására fény- és fluoreszcens mikroszkópiában PY - 2018 UR - https://m2.mtmt.hu/api/publication/30433688 ID - 30433688 N1 - [Poszter] LA - Hungarian DB - MTMT ER - TY - JOUR AU - Hoyk, Zsófia AU - Tóth, Erzsébet Melinda AU - Lénárt, Nikolett AU - Nagy, Dóra AU - Dukay, Brigitta AU - Csefová, Alexandra AU - Zvara, Ágnes AU - Seprényi, György AU - Kincses, András AU - Walter, Fruzsina AU - Veszelka, Szilvia AU - Vigh, Judit Piroska AU - Barabási, Beáta AU - Harazin, András AU - Kittel, Ágnes AU - Puskás, László AU - Penke, Botond AU - Vigh, László AU - Deli, Mária Anna AU - Sántha, Miklós TI - Cerebrovascular Pathology in Hypertriglyceridemic APOB-100 Transgenic Mice JF - FRONTIERS IN CELLULAR NEUROSCIENCE J2 - FRONT CELL NEUROSCI VL - 12 ET - 0 PY - 2018 PG - 17 SN - 1662-5102 DO - 10.3389/fncel.2018.00380 UR - https://m2.mtmt.hu/api/publication/30312141 ID - 30312141 N1 - These authors have contributed equally to this work: Zsófia Hoyk, Melinda E. Tóth. Funding text: This work was supported by funding from National Research, Development and Innovation Office, Hungary (GINOP2.3.2.-15.2016-00060) and the Hungarian Basic Research Fund (OTKA NN111006). AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Megyeri, Klára AU - Orosz, László AU - Bolla, Beáta Szilvia AU - Erdei, Lilla AU - Rázga, Zsolt AU - Seprényi, György AU - Zsoldiné Urbán, Edit AU - Szabó, Kornélia Ágnes AU - Kemény, Lajos TI - Propionibacterium acnes induces autophagy in keratinocytes: involvement of multiple mechanisms JF - JOURNAL OF INVESTIGATIVE DERMATOLOGY J2 - J INVEST DERMATOL VL - 138 PY - 2018 IS - 4 SP - 750 EP - 759 PG - 10 SN - 0022-202X DO - 10.1016/j.jid.2017.11.018 UR - https://m2.mtmt.hu/api/publication/3300946 ID - 3300946 N1 - Funding Agency and Grant Number: OTKA [105369, GINOP-2.3.2-15-2016-00015, GINOP-2.2.1-15-2016-00007, GINOP-2.3.3-15-2016-00007, GINOP-2.3.3-15-2016-00012, EFOP-3.6.1-16-2016-00008] Funding text: This work was supported by research grants OTKA 105369, GINOP-2.3.2-15-2016-00015, GINOP-2.2.1-15-2016-00007, GINOP-2.3.3-15-2016-00007, GINOP-2.3.3-15-2016-00012, and EFOP-3.6.1-16-2016-00008. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Magyar, János AU - Horváth, Balázs AU - Vaczi, K AU - Hegyi, Bence AU - Gönczi, Mónika AU - Dienes, Beatrix AU - Kistamás, Kornél AU - Bányász, Tamás AU - Baczkó, István AU - Varró, András AU - Seprényi, György AU - Csernoch, László AU - Nánási, Péter Pál AU - Szentandrássy, Norbert TI - Calcium Activated Chloride Current in Mammalian Ventricular Myocytes JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 112 PY - 2017 IS - 3 SP - 36A EP - 36A PG - 1 SN - 0006-3495 DO - 10.1016/j.bpj.2016.11.227 UR - https://m2.mtmt.hu/api/publication/3280809 ID - 3280809 N1 - Supplement: 1 Meeting Abstract: 180-Plat LA - English DB - MTMT ER - TY - JOUR AU - Szentandrássy, Norbert AU - Hegyi, Bence AU - Horváth, Balázs AU - Vaczi, K AU - Gönczi, Mónika AU - Dienes, Beatrix AU - Kistamás, Kornél AU - Veress, Roland AU - Ruzsnavszky, Ferenc AU - Bányász, Tamás AU - Magyar, János AU - Baczkó, István AU - Varró, András AU - Seprényi, György AU - Csernoch, László AU - Nánási, Péter Pál TI - Recent advances in research of cardiac calcium-activated chloride channels JF - ACTA PHYSIOLOGICA J2 - ACTA PHYSIOL VL - 221 PY - 2017 IS - S713 SP - 22 EP - 22 PG - 1 SN - 1748-1708 UR - https://m2.mtmt.hu/api/publication/3280807 ID - 3280807 LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Balázs AU - Váczi, Krisztina AU - Hegyi, Bence AU - Gönczi, Mónika AU - Dienes, Beatrix AU - Kistamás, Kornél AU - Bányász, Tamás AU - Magyar, János AU - Baczkó, István AU - Varró, András AU - Seprényi, György AU - Csernoch, László AU - Nánási, Péter Pál AU - Szentandrássy, Norbert TI - Sarcolemmal Ca2+-entry through L-type Ca2+ channels controls the profile of Ca2+-activated Cl- current in canine ventricular myocytes. JF - JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY J2 - J MOL CELL CARDIOL VL - 97 PY - 2016 SP - 125 EP - 139 PG - 15 SN - 0022-2828 DO - 10.1016/j.yjmcc.2016.05.006 UR - https://m2.mtmt.hu/api/publication/3066993 ID - 3066993 N1 - Department of Physiology, Faculty of Medicine, University of Debrecen, Nagyerdei krt 98, P.O. Box 22, Debrecen, H-4012, Hungary Faculty of Pharmacy, University of Debrecen, Nagyerdei krt 98, P.O. Box 22, Debrecen, H-4012, Hungary MTA-DE Momentum, Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Nagyerdei krt 98, P.O. Box 22, Debrecen, H-4012, Hungary Division of Sport Physiology, Department of Physiology, Faculty of Medicine, University of Debrecen, Nagyerdei krt 98, P.O. Box 22, Debrecen, H-4012, Hungary Department of Pharmacology and Pharmacotherapy, Faculty of Medicine, University of Szeged, Dóm tér 12, P.O. Box 427, Szeged, H-6720, Hungary MTA-SZTE Research Group of Cardiovascular Pharmacology, Hungarian Academy of Sciences, Dóm tér 12, P.O. Box 427, Szeged, H-6720, Hungary Department of Medical Biology, Faculty of Medicine, University of Szeged, Somogyi Béla utca 4, P.O. Box 427, Szeged, H-6720, Hungary Department of Dental Physiology and Pharmacology, Faculty of Dentistry, University of Debrecen, Nagyerdei krt 98, P.O. Box 22, Debrecen, H-4012, Hungary Cited By :9 Export Date: 30 September 2019 CODEN: JMCDA Correspondence Address: Szentandrássy, N.; Department of Physiology, University of Debrecen, Nagyerdei krt 98, P.O. Box 22, Hungary; email: szentandrassy.norbert@med.unideb.hu Chemicals/CAS: calcium ion, 14127-61-8; Biomarkers; Calcium Channel Blockers; Calcium Channels, L-Type; Chloride Channels AB - 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. LA - English DB - MTMT ER -