@article{MTMT:35083838,
	title = {Mild Hyperthermia-Induced Thermogenesis in the Endoplasmic Reticulum Defines Stress Response Mechanisms},
	url = {https://m2.mtmt.hu/api/publication/35083838},
	author = {Dukic, Barbara and Ruppert, Zsófia and Tóth, Erzsébet Melinda and Hunya, Ákos and Czibula, Ágnes and Bíró, Péter and Tiszlavicz, Ádám and Péter, Mária and Balogh, Gábor and Erdélyi, Miklós and Timinszky, Gyula and Vigh, László and Gombos, Imre and Török, Zsolt},
	doi = {10.3390/cells13131141},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {13},
	unique-id = {35083838},
	abstract = {Previous studies reported that a mild, non-protein-denaturing, fever-like temperature increase induced the unfolded protein response (UPR) in mammalian cells. Our dSTORM super-resolution microscopy experiments revealed that the master regulator of the UPR, the IRE1 (inositol-requiring enzyme 1) protein, is clustered as a result of UPR activation in a human osteosarcoma cell line (U2OS) upon mild heat stress. Using ER thermo yellow, a temperature-sensitive fluorescent probe targeted to the endoplasmic reticulum (ER), we detected significant intracellular thermogenesis in mouse embryonic fibroblast (MEF) cells. Temperatures reached at least 8 °C higher than the external environment (40 °C), resulting in exceptionally high ER temperatures similar to those previously described for mitochondria. Mild heat-induced thermogenesis in the ER of MEF cells was likely due to the uncoupling of the Ca2+/ATPase (SERCA) pump. The high ER temperatures initiated a pronounced cytosolic heat-shock response in MEF cells, which was significantly lower in U2OS cells in which both the ER thermogenesis and SERCA pump uncoupling were absent. Our results suggest that depending on intrinsic cellular properties, mild hyperthermia-induced intracellular thermogenesis defines the cellular response mechanism and determines the outcome of hyperthermic stress.},
	year = {2024},
	eissn = {2073-4409},
	orcid-numbers = {Hunya, Ákos/0000-0002-4547-9284; Czibula, Ágnes/0000-0003-4461-2773; Tiszlavicz, Ádám/0009-0008-4830-0594; Erdélyi, Miklós/0000-0002-9501-5752}
}

@article{MTMT:32849807,
	title = {Distinct Cellular Tools of Mild Hyperthermia-Induced Acquired Stress Tolerance in Chinese Hamster Ovary Cells.},
	url = {https://m2.mtmt.hu/api/publication/32849807},
	author = {Tiszlavicz, Ádám and Gombos, Imre and Péter, Mária and Hegedűs, Zoltán and Hunya, Ákos and Dukic, Barbara and Nagy, István and Peksel, Begüm and Balogh, Gábor and Horváth, Ibolya and Vigh, László and Török, Zsolt},
	doi = {10.3390/biomedicines10051172},
	journal-iso = {BIOMEDICINES},
	journal = {BIOMEDICINES},
	volume = {10},
	unique-id = {32849807},
	abstract = {Mild stress could help cells to survive more severe environmental or pathophysiological conditions. In the current study, we investigated the cellular mechanisms which contribute to the development of stress tolerance upon a prolonged (0-12 h) fever-like (40 °C) or a moderate (42.5 °C) hyperthermia in mammalian Chinese Hamster Ovary (CHO) cells. Our results indicate that mild heat triggers a distinct, dose-dependent remodeling of the cellular lipidome followed by the expression of heat shock proteins only at higher heat dosages. A significant elevation in the relative concentration of saturated membrane lipid species and specific lysophosphatidylinositol and sphingolipid species suggests prompt membrane microdomain reorganization and an overall membrane rigidification in response to the fluidizing heat in a time-dependent manner. RNAseq experiments reveal that mild heat initiates endoplasmic reticulum stress-related signaling cascades resulting in lipid rearrangement and ultimately in an elevated resistance against membrane fluidization by benzyl alcohol. To protect cells against lethal, protein-denaturing high temperatures, the classical heat shock protein response was required. The different layers of stress response elicited by different heat dosages highlight the capability of cells to utilize multiple tools to gain resistance against or to survive lethal stress conditions.},
	keywords = {MEMBRANE; STRESS; heat shock response; transcriptomics; LIPIDOMICS; Unfolded protein response; Chinese hamster ovary cells; acquired stress tolerance; membrane lipid metabolism},
	year = {2022},
	eissn = {2227-9059},
	orcid-numbers = {Hunya, Ákos/0000-0002-4547-9284}
}

@article{MTMT:31341681,
	title = {Alzheimer risk factors age and female sex induce cortical Aβ aggregation by raising extracellular zinc [Alzheimer risk factors age and female sex induce cortical A beta aggregation by raising extracellular zinc]},
	url = {https://m2.mtmt.hu/api/publication/31341681},
	author = {Datki, Zsolt László and Oláh, Zita and Jánosi-Mózes, Emese and Szegedi, Viktor and Kálmán, János and Hunya, Ákos and Fülöp, Lívia and Tamano, Haruna and Takeda, Atsushi and Adlard, Paul A. and Bush, Ashley I.},
	doi = {10.1038/s41380-020-0800-y},
	journal-iso = {MOL PSYCHIATR},
	journal = {MOLECULAR PSYCHIATRY},
	volume = {25},
	unique-id = {31341681},
	issn = {1359-4184},
	abstract = {Aging and female sex are the major risk factors for Alzheimer's disease and its associated brain amyloid-beta (A beta) neuropathology, but the mechanisms mediating these risk factors remain uncertain. Evidence indicates that A beta aggregation by Zn(2+)released from glutamatergic neurons contributes to amyloid neuropathology, so we tested whether aging and sex adversely influences this neurophysiology. Using acute hippocampal slices, we found that extracellular Zn2+-elevation induced by high K(+)stimulation was significantly greater with older (65 weeks vs 10 weeks old) rats, and was exaggerated in females. This was driven by slower reuptake of extracellular Zn2+, which could be recapitulated by mitochondrial intoxication. Zn2+:A beta aggregates were toxic to the slices, but A beta alone was not. Accordingly, high K(+)caused synthetic human A beta added to the slices to form soluble oligomers as detected by bis-ANS, attaching to neurons and inducing toxicity, with older slices being more vulnerable. Age-dependent energy failure impairing Zn(2+)reuptake, and a higher maximal capacity for Zn(2+)release by females, could contribute to age and sex being major risk factors for Alzheimer's disease.},
	year = {2020},
	eissn = {1476-5578},
	pages = {2728-2741},
	orcid-numbers = {Datki, Zsolt László/0000-0002-2537-4741; Oláh, Zita/0000-0002-6372-532X; Jánosi-Mózes, Emese/0000-0003-1532-289X; Szegedi, Viktor/0000-0003-4191-379X; Kálmán, János/0000-0001-5319-5639; Hunya, Ákos/0000-0002-4547-9284; Fülöp, Lívia/0000-0002-8010-0129}
}

@inproceedings{MTMT:31619291,
	title = {Dizájner drogok és metabolitjaik az igazságügyi gyakorlatban},
	url = {https://m2.mtmt.hu/api/publication/31619291},
	author = {Körmöczi, Tímea and Kovács, Orsolya and Sija, Éva and Hunya, Ákos and Samavati, Reza and Gáspár, Róbert and Institóris, László and Ilisz, István and Berkecz, Róbert},
	booktitle = {XLII. Kémiai Előadói Napok - Előadásösszefoglalók},
	unique-id = {31619291},
	year = {2019},
	pages = {73-77},
	orcid-numbers = {Körmöczi, Tímea/0000-0002-0973-2473; Hunya, Ákos/0000-0002-4547-9284; Gáspár, Róbert/0000-0002-1571-7579; Ilisz, István/0000-0001-8282-457X; Berkecz, Róbert/0000-0002-9076-2177}
}

@{MTMT:31619279,
	title = {Analysis of designer drugs and their metabolites in blood and urine samples},
	url = {https://m2.mtmt.hu/api/publication/31619279},
	author = {Körmöczi, Tímea and Kovács, Orsolya and Sija, Éva and Hunya, Ákos and Samavati, Reza and Gáspár, Róbert and Institóris, László and Ilisz, István and Berkecz, Róbert},
	booktitle = {Proceedings of the 25th International Symposium on Analytical and Environmental Problems},
	unique-id = {31619279},
	year = {2019},
	pages = {80-80},
	orcid-numbers = {Körmöczi, Tímea/0000-0002-0973-2473; Hunya, Ákos/0000-0002-4547-9284; Gáspár, Róbert/0000-0002-1571-7579; Ilisz, István/0000-0001-8282-457X; Berkecz, Róbert/0000-0002-9076-2177}
}

@article{MTMT:30431480,
	title = {The impact of dihydropyridine derivatives on the cerebral blood flow response to somatosensory stimulation and spreading depolarization},
	url = {https://m2.mtmt.hu/api/publication/30431480},
	author = {Szabó, Írisz and M.Tóth, Orsolya and Török, Zsolt and Varga, Dániel Péter and Menyhárt, Ákos and Frank, Rita and Hantosi, Dóra and Hunya, Ákos and Bari, Ferenc and Horváth, Ibolya and Vigh, László and Farkas, Eszter},
	doi = {10.1111/bph.14611},
	journal-iso = {BR J PHARMACOL},
	journal = {BRITISH JOURNAL OF PHARMACOLOGY},
	volume = {176},
	unique-id = {30431480},
	issn = {0007-1188},
	abstract = {A new class of heat shock protein co-inducer dihydropyridine derivatives devoid of calcium channel antagonist and vasodilator effects have been recently developed with the purpose to target neurodegeneration selectively. Here we set out to evaluate the action of one of these novel compounds LA1011 on neurovascular coupling in the ischemic rat cerebral cortex. As a reference, we applied nimodipine, a well-known calcium channel antagonist, vasodilator dihydropyridine compound.Rats (n=62) were treated with LA1011 or nimodipine, either by chronic, systemic (LA1011, 1 mg/kg b.w.), or acute, local administration (LA1011 and nimodipine, 100 μM). In the latter treatment group, global forebrain ischemia was induced in half of the animals by bilateral common carotid artery occlusion under isoflurane anesthesia. Functional hyperemia in the somatosensory cortex was created by mechanical stimulation of the contralateral whisker pad under alpha-chloralose anesthesia. Spreading depolarization (SD) events were elicited subsequently by 1 M KCl. Local field potential and cerebral blood flow (CBF) in the parietal somatosensory cortex were monitored by electrophysiology and laser Doppler flowmetry.LA1011 did not alter CBF, but intensified SD, presumably indicating the co-induction of heat shock proteins, and, perhaps an anti-inflammatory effect. Nimodipine attenuated evoked potentials and SD. In addition to the elevation of baseline CBF, nimodipine augmented hyperemia in response to both somatosensory stimulation and SD, particularly under ischemia. In conclusion, in contrast with CBF improvement achieved by nimodipine, LA1011 seems not to have discernible cerebrovascular effects, but may upregulate stress response.},
	year = {2019},
	eissn = {1476-5381},
	pages = {1222-1234},
	orcid-numbers = {Varga, Dániel Péter/0000-0001-5797-9334; Menyhárt, Ákos/0000-0002-1355-3208; Hunya, Ákos/0000-0002-4547-9284; Farkas, Eszter/0000-0002-8478-9664}
}

@article{MTMT:3310819,
	title = {Studies for improving a rat model of Alzheimer's disease: ICV administration of well-characterized β-amyloid 1-42 oligomers induce dysfunction in spatial memory},
	url = {https://m2.mtmt.hu/api/publication/3310819},
	author = {Kasza, Ágnes and Penke, Botond and Frank, Z and Bozsó, Zsolt and Szegedi, Viktor and Hunya, Ákos and Nemeth, K and Kozma, Gábor and Fülöp, Lívia},
	doi = {10.3390/molecules22112007},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {22},
	unique-id = {3310819},
	issn = {1420-3049},
	year = {2017},
	eissn = {1420-3049},
	orcid-numbers = {Penke, Botond/0000-0003-0938-0567; Bozsó, Zsolt/0000-0002-5713-3096; Szegedi, Viktor/0000-0003-4191-379X; Hunya, Ákos/0000-0002-4547-9284; Kozma, Gábor/0000-0003-2033-0720; Fülöp, Lívia/0000-0002-8010-0129}
}

@article{MTMT:3099240,
	title = {Dihydropyridine Derivatives Modulate Heat Shock Responses and have a Neuroprotective Effect in a Transgenic Mouse Model of Alzheimer's Disease},
	url = {https://m2.mtmt.hu/api/publication/3099240},
	author = {Kasza, Ágnes and Hunya, Ákos and Frank, Z and Fülöp, Ferenc and Török, Zsolt and Balogh, Gábor and Sántha, Miklós and Bálind, Árpád and Bernáth, S and Blundell, KLIM and Prodromou, C and Horváth, Ibolya and Zeiler, H-J and Hooper, PL and Vigh, László and Penke, Botond},
	doi = {10.3233/JAD-150860},
	journal-iso = {J ALZHEIMERS DIS},
	journal = {JOURNAL OF ALZHEIMER'S DISEASE},
	volume = {53},
	unique-id = {3099240},
	issn = {1387-2877},
	abstract = {Heat shock proteins (Hsps) have chaperone activity and play a pivotal role in the homeostasis of proteins by preventing misfolding, by clearing aggregated and damaged proteins from cells, and by maintaining proteins in an active state. Alzheimer's disease (AD) is thought to be caused by amyloid-β peptide that triggers tau hyperphosphorylation, which is neurotoxic. Although proteostasis capacity declines with age and facilitates the manifestation of neurodegenerative diseases such as AD, the upregulation of chaperones improves prognosis. Our research goal is to identify potent Hsp co-inducers that enhance protein homeostasis for the treatment of AD, especially 1,4-dihydropyridine derivatives optimized for their ability to modulate cellular stress responses. Based on favorable toxicological data and Hsp co-inducing activity, LA1011 was selected for the in vivo analysis of its neuroprotective effect in the APPxPS1 mouse model of AD. Here, we report that 6 months of LA1011 administration effectively improved the spatial learning and memory functions in wild type mice and eliminated neurodegeneration in double mutant mice. Furthermore, Hsp co-inducer therapy preserves the number of neurons, increases dendritic spine density, and reduces tau pathology and amyloid plaque formation in transgenic AD mice. In conclusion, the Hsp co-inducer LA1011 is neuroprotective and therefore is a potential pharmaceutical candidate for the therapy of neurodegenerative diseases, particularly AD. © 2016 - IOS Press and the authors. All rights reserved.},
	keywords = {Alzheimer's disease; neuroprotection; HEAT-SHOCK PROTEINS; Dihydropyridines; Hsp co-induction},
	year = {2016},
	eissn = {1875-8908},
	pages = {557-571},
	orcid-numbers = {Hunya, Ákos/0000-0002-4547-9284; Fülöp, Ferenc/0000-0003-1066-5287; Penke, Botond/0000-0003-0938-0567}
}

@article{MTMT:2990307,
	title = {Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe.},
	url = {https://m2.mtmt.hu/api/publication/2990307},
	author = {Glatz, Attila and Pilbat, Ana Maria and Nemeth, GL and Kontár, Katalin and Jósvay, Katalin and Hunya, Ákos and Udvardy, Andor and Gombos, Imre and Péter, Mária and Balogh, Gábor and Horváth, Ibolya and Vigh, László and Török, Zsolt},
	doi = {10.1007/s12192-015-0662-4},
	journal-iso = {CELL STRESS CHAPERON},
	journal = {CELL STRESS & CHAPERONES},
	volume = {21},
	unique-id = {2990307},
	issn = {1355-8145},
	abstract = {Changes in the levels of three structurally and functionally different important thermoprotectant molecules, namely small heat shock proteins (sHsps), trehalose, and lipids, have been investigated upon heat shock in Schizosaccharomyces pombe. Both alpha-crystallin-type sHsps (Hsp15.8 and Hsp16) were induced after prolonged high-temperature treatment but with different kinetic profiles. The shsp null mutants display a weak, but significant, heat sensitivity indicating their importance in the thermal stress management. The heat induction of sHsps is different in wild type and in highly heat-sensitive trehalose-deficient (tps1Delta) cells; however, trehalose level did not show significant alteration in shsp mutants. The altered timing of trehalose accumulation and induction of sHsps suggest that the disaccharide might provide protection at the early stage of the heat stress while elevated amount of sHsps are required at the later phase. The cellular lipid compositions of two different temperature-adapted wild-type S. pombe cells are also altered according to the rule of homeoviscous adaptation, indicating their crucial role in adapting to the environmental temperature changes. Both Hsp15.8 and Hsp16 are able to bind to different lipids isolated from S. pombe, whose interaction might provide a powerful protection against heat-induced damages of the membranes. Our data suggest that all the three investigated thermoprotectant macromolecules play a pivotal role during the thermal stress management in the fission yeast.},
	year = {2016},
	eissn = {1466-1268},
	pages = {327-338},
	orcid-numbers = {Hunya, Ákos/0000-0002-4547-9284}
}

@mastersthesis{MTMT:2856341,
	title = {Physiological factors could enhance amyloid-beta toxicity},
	url = {https://m2.mtmt.hu/api/publication/2856341},
	author = {Hunya, Ákos},
	doi = {10.14232/phd.1674},
	publisher = {SZTE},
	unique-id = {2856341},
	year = {2013},
	orcid-numbers = {Hunya, Ákos/0000-0002-4547-9284}
}