@article{MTMT:33728557,
	title = {Urocortin stimulates the ERK1/2 signaling pathway and the proliferation of HeLa cells via CRF receptor 1},
	url = {https://m2.mtmt.hu/api/publication/33728557},
	author = {Balogh, Bálint and Vecsernyés, Mónika and Stayer-Harci, Alexandra and Berta, Gergely and Tarjányi, Oktávia and Sétáló, György (ifj.)},
	doi = {10.1002/2211-5463.13602},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	volume = {13},
	unique-id = {33728557},
	issn = {2211-5463},
	abstract = {Corticotropin-releasing factor (CRF) stimulates adrenocorticotropic hormone (ACTH) secretion from the pituitary gland and is an essential regulator of the hypothalamic-pituitary-adrenocortical axis. Isoforms of CRF receptor are known to mediate the effects of urocortin stress ligands on the regulation of stress responses, anxiety, and feeding behavior; however, urocortin stress ligands also influence cell proliferation. In view of the tumor-promoting capacity of prolonged stress, here we investigated (a) the effect of urocortin on cell proliferative signaling via extracellular signal-regulated kinase 1/2, (b) the expression and cellular distribution of the specific CRF receptor isoforms, and (c) the intracellular localization of phosphorylated ERK1/2 in HeLa cells. Stimulation of cell proliferation was observed in the presence of 10 nm urocortin. Our data also suggest that MAP kinase MEK, the transcription factors E2F-1 and p53, and PKB/Akt are involved in this process. These findings may have therapeutic relevance for the targeted treatment of various malignancies.},
	keywords = {cell proliferation; urocortin; HeLa; E2F-1; ERK1/2, MEK},
	year = {2023},
	eissn = {2211-5463},
	pages = {818-832}
}

@article{MTMT:32766373,
	title = {Prolonged treatment with the proteasome inhibitor MG-132 induces apoptosis in PC12 rat pheochromocytoma cells},
	url = {https://m2.mtmt.hu/api/publication/32766373},
	author = {Tarjányi, Oktávia and Haerer, Julian and Vecsernyés, Mónika and Berta, Gergely and Stayer-Harci, Alexandra and Balogh, Bálint and Borbásné Farkas, Kornélia and Boldizsár, Ferenc and Szeberényi, József and Sétáló, György (ifj.)},
	doi = {10.1038/s41598-022-09763-z},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {32766373},
	issn = {2045-2322},
	abstract = {Rat pheochromocytoma (PC12) cells were treated with the proteasome inhibitor MG-132 and morphological changes were recorded. Initially, neuronal differentiation was induced but after 24 h signs of morphological deterioration became apparent. We performed nuclear staining, flow cytometry and WST-1 assay then analyzed signal transduction pathways involving Akt, p38 MAPK (Mitogen-Activated Protein Kinase), JNK (c-Jun N-terminal Kinase), c-Jun and caspase-3. Stress signaling via p38, JNK and c-Jun was active even after 24 h of MG-132 treatment, while the survival-mediating Akt phosphorylation declined and the executor of apoptosis (caspase-3) was activated by that time and apoptosis was also observable. We examined subcellular localization of stress signaling components, applied kinase inhibitors and dominant negative H-Ras mutant-expressing PC12 cells in order to decipher connections of stress-mediating pathways. Our results are suggestive of that treatment with the proteasome inhibitor MG-132 has a biphasic nature in PC12 cells. Initially, it induces neuronal differentiation but prolonged treatments lead to apoptosis.},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Borbásné Farkas, Kornélia/0000-0002-5349-6527}
}

@article{MTMT:32709502,
	title = {Urocortin stimulates ERK1/2 phosphorylation and proliferation but reduces ATP production of MCF7 breast cancer cells},
	url = {https://m2.mtmt.hu/api/publication/32709502},
	author = {Balogh, Bálint and Vecsernyés, Mónika and Veres-Székely, Apor and Berta, Gergely and Stayer-Harci, Alexandra and Tarjányi, Oktávia and Sétáló, György (ifj.)},
	doi = {10.1016/j.mce.2022.111610},
	journal-iso = {MOL CELL ENDOCRINOL},
	journal = {MOLECULAR AND CELLULAR ENDOCRINOLOGY},
	volume = {547},
	unique-id = {32709502},
	issn = {0303-7207},
	year = {2022},
	eissn = {1872-8057},
	orcid-numbers = {Veres-Székely, Apor/0000-0002-6830-8779}
}

@article{MTMT:30886434,
	title = {Prostaglandin E2, a postulated mediator of neurovascular coupling, at low concentrations dilates whereas at higher concentrations constricts human cerebral parenchymal arterioles},
	url = {https://m2.mtmt.hu/api/publication/30886434},
	author = {Czigler, András and Tóth, Luca and Szarka, Nikolett and Szilágyi, Krisztina and Kellermayer, Zoltán and Stayer-Harci, Alexandra and Vecsernyes, Monika and Ungvári, Zoltán István and Szolics, Alex and Koller, Ákos and Büki, András and Tóth, Péter József},
	doi = {10.1016/j.prostaglandins.2019.106389},
	journal-iso = {PROSTAG OTH LIPID M},
	journal = {PROSTAGLANDINS & OTHER LIPID MEDIATORS},
	volume = {146},
	unique-id = {30886434},
	issn = {1098-8823},
	abstract = {There is considerable controversy regarding the vasoactive action of prostaglandin E2 (PGE2). On the one hand, indirect evidence implicates that astrocytic release of PGE2 contributes to neurovascular coupling responses mediating functional hyperemia in the brain. On the other hand, overproduction of PGE2 was also reported to contribute to cerebral vasospasm associated with subarachnoid hemorrhage. The present study was conducted to resolve this controversy by determining the direct vasoactive effects of PGE2 in resistance-sized human cerebral parenchymal arterioles. To achieve this goal PGE2-induced isotonic vasomotor responses were assessed in parenchymal arterioles isolated from fronto-temporo-parietal cortical tissues surgically removed from patients and expression of PGE2 receptors were examined. In functionally intact parenchymal arterioles lower concentrations of PGE2 (from 10-8 to 10-6 mol/l) caused significant, endothelium-independent vasorelaxation, which was inhibited by the EP4 receptor blocker BGC201531. In contrast, higher concentrations of PGE2 evoked significant EP1-dependent vasoconstriction, which could not be reversed by the EP4 receptor agonist CAY10598. We also confirmed previous observations that PGE2 primarily evokes constriction in intracerebral arterioles isolated from R. norvegicus. Importantly, vascular mRNA and protein expression of vasodilator EP4 receptors was significantly higher than that of vasoconstrictor EP1 receptors in human cerebral arterioles. PGE2 at low concentrations dilates whereas at higher concentrations constricts human cerebral parenchymal arterioles. This bimodal vasomotor response is consistent with both the proposed vasodilator role of PGE2 during functional hyperemia and its putative role in cerebral vasospasm associated with subarachnoid hemorrhage in human patients.},
	keywords = {Cerebral ischemia; Neurovascular coupling; EP4; PGE(2); EP1},
	year = {2020},
	eissn = {2212-196X},
	orcid-numbers = {Ungvári, Zoltán István/0000-0002-6035-6039; Koller, Ákos/0000-0003-3256-8701}
}

@misc{MTMT:2952364,
	title = {Az urokortin2 jelátviteli kapcsolatainak vizsgálata PC12 sejtekben},
	url = {https://m2.mtmt.hu/api/publication/2952364},
	author = {Stayer-Harci, Alexandra and Balogh, Bálint and Berta, Gergely and Tarjányi, Oktávia and Vecsernyés, Mónika and Ábrahám, Hajnalka and Szeberényi, József and Sétáló, György (ifj.)},
	unique-id = {2952364},
	year = {2015}
}

@{MTMT:3322990,
	title = {A sejtek progresszív determinációja},
	url = {https://m2.mtmt.hu/api/publication/3322990},
	author = {Stayer-Harci, Alexandra and Mátics, Róbert and Varga, Dániel and Pollák, Edit and Varga, Máté},
	booktitle = {Fejlődésbiológia II},
	unique-id = {3322990},
	year = {2014},
	pages = {311-350},
	orcid-numbers = {Varga, Máté/0000-0003-4289-1705}
}

@{MTMT:3321697,
	title = {Indukció és determináció},
	url = {https://m2.mtmt.hu/api/publication/3321697},
	author = {Varga, Máté and Varga, Sándor and Szatmári, Dávid Zoltán and Gálosi, Rita and Stayer-Harci, Alexandra},
	booktitle = {Fejlődésbiológia II},
	unique-id = {3321697},
	year = {2014},
	pages = {351-398},
	orcid-numbers = {Varga, Máté/0000-0003-4289-1705}
}

@{MTMT:2729810,
	title = {A sejtek kommunikációja és kölcsönhatásai, jelátviteli folyamatok, jelátvitel és sejthalál},
	url = {https://m2.mtmt.hu/api/publication/2729810},
	author = {Schipp, Renáta and Stayer-Harci, Alexandra and Kiss, Katalin and Németh, Zoltán and Mátics, Róbert and Barna, János and Hoffmann, Gyula and Varga, Dániel and Varga, Máté and Varga, Judit},
	booktitle = {Fejlődésbiológia II},
	unique-id = {2729810},
	year = {2014},
	pages = {171-218},
	orcid-numbers = {Barna, János/0000-0002-9242-0939; Hoffmann, Gyula/0000-0002-2206-6997; Varga, Máté/0000-0003-4289-1705}
}

@article{MTMT:2376069,
	title = {The role of Src protein in the process formation of PC12 cells induced by the proteasome inhibitor MG-132.},
	url = {https://m2.mtmt.hu/api/publication/2376069},
	author = {Tarjányi, Oktávia and Berta, Gergely and Stayer-Harci, Alexandra and Bacsa, EB and Stark, B and Pap, Marianna and Szeberényi, József and Sétáló, György (ifj.)},
	doi = {10.1016/j.neuint.2013.07.008},
	journal-iso = {NEUROCHEM INT},
	journal = {NEUROCHEMISTRY INTERNATIONAL},
	volume = {63},
	unique-id = {2376069},
	issn = {0197-0186},
	abstract = {The PC12 (rat pheochromocytoma) cell line is a popular model system to study neuronal differentiation. Upon prolonged nerve growth factor (NGF) exposure these tumor cells stop to divide, become polygonal, grow projections and start to look and behave like sympathetic neurons. Differentiation of PC12 cells can also be induced by peptidyl-aldehyde proteasome inhibitors, such as Z-Leu-Leu-Leu-al (also known as MG-132) or via infection of the cells with Rous sarcoma virus. The signal transduction pathways underlying process formation, however, are still not fully understood. The liganded NGF receptor initiates a protein kinase cascade a member of which is Extracellular Signal-Regulated Kinase (ERK). Active ERK1/2 enzymes phosphorylate various cytoplasmic proteins and can also be translocated into the nucleus, where they regulate gene expression by activating key transcription factors. Using immunological methods we detected phosphorylation of TrkA, prolonged activation of Src, and ERK1/2 with nuclear translocation of the latter during MG-132-induced process formation of PC12 cells. Activated Src remained predominantly cytoplasmic. MG-132-induced sustained ERK1/2 activation, nuclear translocation and neuritogenesis required the intact function of Src since these phenomena were markedly reduced or failed upon chemical inhibition of Src tyrosine protein kinase activity.},
	year = {2013},
	eissn = {1872-9754},
	pages = {413-422}
}

@article{MTMT:2330540,
	title = {Partial rescue of geldanamycin-induced TrkA depletion by a proteasome inhibitor in PC12 cells.},
	url = {https://m2.mtmt.hu/api/publication/2330540},
	author = {Berta, Gergely and Stayer-Harci, Alexandra and Tarjányi, Oktávia and Vecsernyes, M and Balogh, András and Pap, Marianna and Szeberényi, József and Sétáló, György (ifj.)},
	doi = {10.1016/j.brainres.2013.05.015},
	journal-iso = {BRAIN RES},
	journal = {BRAIN RESEARCH},
	volume = {1520},
	unique-id = {2330540},
	issn = {0006-8993},
	abstract = {In this work we tried to identify mechanisms that could explain how chemical inhibition of heat-shock protein 90 reduces nerve growth factor signaling in rat pheochromocytoma PC12 cells. Geldanamycin is an antibiotic originally discovered based on its ability to bind heat-shock protein 90. This interaction can lead to the disruption of heat-shock protein 90-containing multimolecular complexes. It can also induce the inhibition or even degradation of partner proteins dissociated from the 90kDa chaperone and, eventually, can cause apoptosis, for instance, in PC12 cells. Before the onset of initial apoptotic events, however, a marked decrease in the activity of extracellular signal-regulated kinases ERK 1/2 and protein kinase B/Akt can be observed together with reduced expression of the high affinity nerve growth factor receptor, tropomyosine-related kinase, TrkA, in this cell type. The proteasome inhibitor MG-132 can effectively counteract the geldanamycin-induced reduction of TrkA expression and it can render TrkA and ERK1/2 phosphorylation but not that of protein kinase B/Akt by nerve growth factor again inducible. We have found altered intracellular distribution of TrkA in geldanamycin-treated and proteasome-inhibited PC12 cells that may, at least from the viewpoint of protein localization explain why nerve growth factor remains without effect on protein kinase B/Akt. The lack of protein kinase B/Akt stimulation by nerve growth factor in turn reveals why nerve growth factor treatment cannot save PC12 cells from geldanamycin-induced programmed cell death. Our observations can help to better understand the mechanism of action of geldanamycin, a compound with strong human therapeutical potential.},
	year = {2013},
	eissn = {1872-6240},
	pages = {70-79}
}