@article{MTMT:33764688,
	title = {Synaptic Targets of Glycinergic Neurons in Laminae I–III of the Spinal Dorsal Horn},
	url = {https://m2.mtmt.hu/api/publication/33764688},
	author = {de Oliveira Miranda, Camila and Hegedűs, Krisztina and Kis, Nikoletta Gréta and Antal, Miklós},
	doi = {10.3390/ijms24086943},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33764688},
	issn = {1661-6596},
	abstract = {A great deal of evidence supports the inevitable importance of spinal glycinergic inhibition in the development of chronic pain conditions. However, it remains unclear how glycinergic neurons contribute to the formation of spinal neural circuits underlying pain-related information processing. Thus, we intended to explore the synaptic targets of spinal glycinergic neurons in the pain processing region (laminae I–III) of the spinal dorsal horn by combining transgenic technology with immunocytochemistry and in situ hybridization accompanied by light and electron microscopy. First, our results suggest that, in addition to neurons in laminae I–III, glycinergic neurons with cell bodies in lamina IV may contribute substantially to spinal pain processing. On the one hand, we show that glycine transporter 2 immunostained glycinergic axon terminals target almost all types of excitatory and inhibitory interneurons identified by their neuronal markers in laminae I–III. Thus, glycinergic postsynaptic inhibition, including glycinergic inhibition of inhibitory interneurons, must be a common functional mechanism of spinal pain processing. On the other hand, our results demonstrate that glycine transporter 2 containing axon terminals target only specific subsets of axon terminals in laminae I–III, including nonpeptidergic nociceptive C fibers binding IB4 and nonnociceptive myelinated A fibers immunoreactive for type 1 vesicular glutamate transporter, indicating that glycinergic presynaptic inhibition may be important for targeting functionally specific subpopulations of primary afferent inputs.},
	year = {2023},
	eissn = {1422-0067}
}

@article{MTMT:33682003,
	title = {Neuronal P2X4 receptor may contribute to peripheral inflammatory pain in rat spinal dorsal horn},
	url = {https://m2.mtmt.hu/api/publication/33682003},
	author = {Ducza, László and Gajtkó, Andrea and Hegedűs, Krisztina and Bakk, Erzsébet and Kis, Nikoletta Gréta and Gaál, Botond Ágoston and Takács, Roland Ádám and Szűcs, Péter and Matesz, Klára and Szentesiné Holló, Krisztina},
	doi = {10.3389/fnmol.2023.1115685},
	journal-iso = {FRONT MOL NEUROSCI},
	journal = {FRONTIERS IN MOLECULAR NEUROSCIENCE},
	volume = {16},
	unique-id = {33682003},
	issn = {1662-5099},
	abstract = {Abstract
		Intense inflammation may result in pain, which manifests as spinal central sensitisation. There is growing evidence that purinergic signaling plays a pivotal role in the orchestration of pain processing. Over the last decade the ionotropic P2X purino receptor 4 (P2X4) got into spotlight in neuropathic disorders, however its precise spinal expression was scantily characterised during inflammatory pain. Thus, we intended to analyse the receptor distribution within spinal dorsal horn and lumbar dorsal root ganglia (DRG) of rats suffering in inflammatory pain induced by complete Freund adjuvant (CFA).
		Methods
		CFA- induced peripheral inflammation was validated by mechanical and thermal behavioural tests. In order to ensure about the putative alteration of spinal P2X4 receptor gene expression qPCR reactions were designed, followed by immunoperoxidase and Western blot experiments to assess changes at a protein level. Colocalisation of P2X4 with neuronal and glial markers was investigated by double immunofluorescent labelings, which were subsequently analysed with IMARIS software. Transmission electronmicroscopy was applied to study the ultrastructural localisation of the receptor. Concurrently, in lumbar DRG cells similar methodology has been carried out to complete our observations.
		Results
		The figures of mechanical and thermal behavioural tests proved the establishment of CFA- induced inflammatory pain. We observed significant enhancement of P2X4 transcript level within the spinal dorsal horn three days upon CFA administration. Elevation of P2X4 immunoreactivity within Rexed lamina I-II of the spinal gray matter was synchronous with mRNA expression, and confirmed by protein blotting. According to IMARIS analysis the robust protein increase was mainly detected on primary afferent axontermini and GFAP-labelled astrocyte membrane compartments within the spinal dorsal horn, but not on postsynaptic dendrites was also validated ultrastructurally. Furthermore, lumbar DRG analysis demonstrated that peptidergic and non-peptidergic nociceptive subsets of ganglia cells were also abundantly positive for P2X4 receptor in CFA model.
		Conclusions
		Here we provide novel evidence about involvement of neuronal and glial P2X4 receptor in the establishment of inflammatory pain.},
	keywords = {Inflammatory pain, spinal dorsal horn, P2X4 receptor, Central sensitisation, primary afferents, glial cells, dorsal root ganglia},
	year = {2023},
	eissn = {1662-5099},
	orcid-numbers = {Gaál, Botond Ágoston/0000-0002-1739-2309; Szűcs, Péter/0000-0003-4635-6427}
}

@article{MTMT:32707412,
	title = {The unique carnation stunt-associated pararetroviroid},
	url = {https://m2.mtmt.hu/api/publication/32707412},
	author = {Balázs, Ervin and Hegedűs, Krisztina and Divéki, Zoltán},
	doi = {10.1016/j.virusres.2022.198709},
	journal-iso = {VIRUS RES},
	journal = {VIRUS RESEARCH},
	volume = {312},
	unique-id = {32707412},
	issn = {0168-1702},
	year = {2022},
	eissn = {1872-7492},
	orcid-numbers = {Divéki, Zoltán/0000-0002-8695-2090}
}

@article{MTMT:32219371,
	title = {Morphological and neurochemical characterization of glycinergic neurons in laminae I-IV of the mouse spinal dorsal horn},
	url = {https://m2.mtmt.hu/api/publication/32219371},
	author = {de Oliveira Miranda, Camila and Hegedűs, Krisztina and Wildner, Hendrik and Zeilhofer, Hanns Ulrich and Antal, Miklós},
	doi = {10.1002/cne.25232},
	journal-iso = {J COMP NEUROL},
	journal = {JOURNAL OF COMPARATIVE NEUROLOGY},
	volume = {530},
	unique-id = {32219371},
	issn = {0021-9967},
	abstract = {A growing body of experimental evidence shows that glycinergic inhibition plays vital roles in spinal pain processing. In spite of this, however, our knowledge about the morphology, neurochemical characteristics, and synaptic relations of glycinergic neurons in the spinal dorsal horn is very limited. The lack of this knowledge makes our understanding about the specific contribution of glycinergic neurons to spinal pain processing quite vague. Here we investigated the morphology and neurochemical characteristics of glycinergic neurons in laminae I-IV of the spinal dorsal horn using a GlyT2::CreERT2-tdTomato transgenic mouse line. Confirming previous reports, we show that glycinergic neurons are sparsely distributed in laminae I-II, but their densities are much higher in lamina III and especially in lamina IV. First in the literature, we provide experimental evidence indicating that in addition to neurons in which glycine colocalizes with GABA, there are glycinergic neurons in laminae I-II that do not express GABA and can thus be referred to as glycine-only neurons. According to the shape and size of cell bodies and dendritic morphology, we divided the tdTomato-labeled glycinergic neurons into three and six morphological groups in laminae I-II and laminae III-IV, respectively. We also demonstrate that most of the glycinergic neurons co-express neuronal nitric oxide synthase, parvalbumin, the receptor tyrosine kinase RET, and the retinoic acid-related orphan nuclear receptor beta (ROR beta), but there might be others that need further neurochemical characterization. The present findings may foster our understanding about the contribution of glycinergic inhibition to spinal pain processing.},
	keywords = {immunohistochemistry; MOUSE; glycine transporter 2; spinal dorsal horn; Cell morphology; glycinergic neurons},
	year = {2022},
	eissn = {1096-9861},
	pages = {607-626},
	orcid-numbers = {Antal, Miklós/0000-0002-2457-7387}
}

@article{MTMT:32474149,
	title = {NLRP2 Is Overexpressed in Spinal Astrocytes at the Peak of Mechanical Pain Sensitivity during Complete Freund Adjuvant-Induced Persistent Pain},
	url = {https://m2.mtmt.hu/api/publication/32474149},
	author = {Ducza, László and Szűcs, Péter and Hegedűs, Krisztina and Bakk, Erzsébet and Gajtkó, Andrea and Wéber, Ildikó and Szentesiné Holló, Krisztina},
	doi = {10.3390/ijms222111408},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32474149},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Szűcs, Péter/0000-0003-4635-6427}
}

@article{MTMT:31294506,
	title = {Cysteine specific bioconjugation with benzyl isothiocyanates},
	url = {https://m2.mtmt.hu/api/publication/31294506},
	author = {Petri, László and Szijj, Péter A. and Kelemen, Ádám and Imre, Timea and Gömöry, Ágnes and Lee, Maximillian T. W. and Hegedűs, Krisztina and Ábrányi-Balogh, Péter and Chudasama, Vijay and Keserű, György Miklós},
	doi = {10.1039/D0RA02934C},
	journal-iso = {RSC ADV},
	journal = {RSC ADVANCES},
	volume = {10},
	unique-id = {31294506},
	issn = {2046-2069},
	year = {2020},
	eissn = {2046-2069},
	pages = {14928-14936},
	orcid-numbers = {Gömöry, Ágnes/0000-0001-5216-0135}
}

@article{MTMT:3364574,
	title = {Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.},
	url = {https://m2.mtmt.hu/api/publication/3364574},
	author = {Takáts, Szabolcs and Glatz, Gábor and Szenci, Győző and Boda, Attila and Horváth V., Gábor and Hegedűs, Krisztina and Kovács, Attila Lajos and Juhász, Gábor},
	doi = {10.1371/journal.pgen.1007359},
	journal-iso = {PLOS GENET},
	journal = {PLOS GENETICS},
	volume = {14},
	unique-id = {3364574},
	issn = {1553-7390},
	abstract = {The autophagosomal SNARE Syntaxin17 (Syx17) forms a complex with Snap29 and Vamp7/8 to promote autophagosome-lysosome fusion via multiple interactions with the tethering complex HOPS. Here we demonstrate that, unexpectedly, one more SNARE (Ykt6) is also required for autophagosome clearance in Drosophila. We find that loss of Ykt6 leads to large-scale accumulation of autophagosomes that are unable to fuse with lysosomes to form autolysosomes. Of note, loss of Syx5, the partner of Ykt6 in ER-Golgi trafficking does not prevent autolysosome formation, pointing to a more direct role of Ykt6 in fusion. Indeed, Ykt6 localizes to lysosomes and autolysosomes, and forms a SNARE complex with Syx17 and Snap29. Interestingly, Ykt6 can be outcompeted from this SNARE complex by Vamp7, and we demonstrate that overexpression of Vamp7 rescues the fusion defect of ykt6 loss of function cells. Finally, a point mutant form with an RQ amino acid change in the zero ionic layer of Ykt6 protein that is thought to be important for fusion-competent SNARE complex assembly retains normal autophagic activity and restores full viability in mutant animals, unlike palmitoylation or farnesylation site mutant Ykt6 forms. As Ykt6 and Vamp7 are both required for autophagosome-lysosome fusion and are mutually exclusive subunits in a Syx17-Snap29 complex, these data suggest that Vamp7 is directly involved in membrane fusion and Ykt6 acts as a non-conventional, regulatory SNARE in this process.},
	year = {2018},
	eissn = {1553-7404},
	orcid-numbers = {Takáts, Szabolcs/0000-0003-2139-7740; Szenci, Győző/0000-0003-0359-6869; Boda, Attila/0000-0003-1811-8595; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:3287984,
	title = {Molecular mechanisms of developmentally programmed crinophagy in Drosophila.},
	url = {https://m2.mtmt.hu/api/publication/3287984},
	author = {Csizmadia, Tamás and Lőrincz, Péter and Hegedűs, Krisztina and Szeplaki, S and Lőw, Péter and Juhász, Gábor},
	doi = {10.1083/jcb.201702145},
	journal-iso = {J CELL BIOL},
	journal = {JOURNAL OF CELL BIOLOGY},
	volume = {217},
	unique-id = {3287984},
	issn = {0021-9525},
	abstract = {At the onset of metamorphosis, Drosophila salivary gland cells undergo a burst of glue granule secretion to attach the forming pupa to a solid surface. Here, we show that excess granules evading exocytosis are degraded via direct fusion with lysosomes, a secretory granule-specific autophagic process known as crinophagy. We find that the tethering complex HOPS (homotypic fusion and protein sorting); the small GTPases Rab2, Rab7, and its effector, PLEKHM1; and a SNAP receptor complex consisting of Syntaxin 13, Snap29, and Vamp7 are all required for the fusion of secretory granules with lysosomes. Proper glue degradation within lysosomes also requires the Uvrag-containing Vps34 lipid kinase complex and the v-ATPase proton pump, whereas Atg genes involved in macroautophagy are dispensable for crinophagy. Our work establishes the molecular mechanism of developmentally programmed crinophagy in Drosophila and paves the way for analyzing this process in metazoans.},
	year = {2018},
	eissn = {1540-8140},
	pages = {361-374},
	orcid-numbers = {Csizmadia, Tamás/0000-0002-2098-9165; Lőrincz, Péter/0000-0001-7374-667X; Lőw, Péter/0000-0003-2450-7087; Juhász, Gábor/0000-0001-8548-8874}
}

@CONFERENCE{MTMT:3363929,
	title = {Developmentally programmed secretory granule degradation in the Drosophila late larval and early pupal salivary gland cells},
	url = {https://m2.mtmt.hu/api/publication/3363929},
	author = {Csizmadia, Tamás and Lőrincz, Péter and Hegedűs, Krisztina and Széplaki, Szilvia and Lőw, Péter and Juhász, Gábor},
	booktitle = {EDRC 2017},
	unique-id = {3363929},
	year = {2017},
	orcid-numbers = {Csizmadia, Tamás/0000-0002-2098-9165; Lőrincz, Péter/0000-0001-7374-667X; Lőw, Péter/0000-0003-2450-7087; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:3278744,
	title = {Drosophila Atg16 promotes enteroendocrine cell differentiation via regulation of intestinal Slit/Robo signaling.},
	url = {https://m2.mtmt.hu/api/publication/3278744},
	author = {Nagy, Péter and Szatmári, Zsuzsanna and Sándor, Gyöngyvér Orsolya and Lippai, Mónika and Hegedűs, Krisztina and Juhász, Gábor},
	doi = {10.1242/dev.147033},
	journal-iso = {DEVELOPMENT},
	journal = {DEVELOPMENT},
	volume = {144},
	unique-id = {3278744},
	issn = {0950-1991},
	abstract = {Genetic variations of Atg16L1, Slit and Rab19 predispose to the development of inflammatory bowel disease (IBD), but the relationship of these mutations is unclear. Here we show that in Drosophila guts lacking the WD40 domain of Atg16, pre-enteroendocrine cells (pre-EEs) accumulate that fail to differentiate into properly functioning secretory EEs. Mechanistically, loss of Atg16 or its binding partner Rab19 impairs Slit production, which normally inhibits EE generation by activating Robo signaling in stem cells. Importantly, loss of Atg16 or decreased Slit/Robo signaling trigger an intestinal inflammatory response. Surprisingly, analysis of Rab19 and domain-specific Atg16 mutants indicates that their stem cell niche regulatory function is independent of autophagy. Our study reveals how mutations in these different genes may contribute to IBD.},
	year = {2017},
	eissn = {1477-9129},
	pages = {3990-4001},
	orcid-numbers = {Nagy, Péter/0000-0002-5053-0646; Sándor, Gyöngyvér Orsolya/0000-0002-0838-2838; Lippai, Mónika/0000-0002-7307-4233; Juhász, Gábor/0000-0001-8548-8874}
}