@{MTMT:31634956,
	title = {Endocannabinoids: the lipid effectors of metabolic regulation in health and disease},
	url = {https://m2.mtmt.hu/api/publication/31634956},
	author = {Jourdan, Tony and Degrace, Pascal and González-Mariscal, Isabel and Szanda, Gergő and Tam, Joseph},
	booktitle = {Lipid Signaling and Metabolism},
	doi = {10.1016/B978-0-12-819404-1.00015-4},
	unique-id = {31634956},
	year = {2020},
	pages = {297-320},
	orcid-numbers = {Szanda, Gergő/0000-0002-1308-7593}
}

@{MTMT:1901913,
	title = {Store-operated Ca2+ entry and mitochondria},
	url = {https://m2.mtmt.hu/api/publication/1901913},
	author = {Spät, András and Szanda, Gergő},
	booktitle = {Store-operated Ca2+ entry (SOCE) pathways},
	unique-id = {1901913},
	year = {2012},
	pages = {177-192},
	orcid-numbers = {Spät, András/0000-0001-8013-5631; Szanda, Gergő/0000-0002-1308-7593}
}

@article{MTMT:1892081,
	title = {The role of mitochondrial Ca(2+) and NAD(P)H in the control of aldosterone secretion.},
	url = {https://m2.mtmt.hu/api/publication/1892081},
	author = {Spät, András and Fülöp, László and Szanda, Gergő},
	doi = {10.1016/j.ceca.2012.01.009},
	journal-iso = {CELL CALCIUM},
	journal = {CELL CALCIUM},
	volume = {52},
	unique-id = {1892081},
	issn = {0143-4160},
	abstract = {The mineralocorticoid hormone aldosterone is synthesized in the zona glomerulosa of the adrenal cortex. Glomerulosa cells respond to the physiological stimuli, elevated extracellular [K(+)] and angiotensin II, with an intracellular Ca(2+) signal. Cytosolic Ca(2+) facilitates the transport of the steroid-precursor cholesterol to mitochondria and, after a few hours, it also induces the transcription of aldosterone synthase. Therefore, the cytosolic Ca(2+) signal is regarded as the most important short and long-term mediator of aldosterone secretion. However, cytosolic Ca(2+) is also taken up by mitochondria and, in turn, the mitochondrial Ca(2+) response activates mitochondrial dehydrogenases resulting in stimulation of respiration and increase in reduced pyridine nucleotides. Since both cholesterol side-chain cleavage and all of the hydroxylation steps of steroid synthesis require NADPH as a cofactor, the importance of cytosolic Ca(2+) - mitochondrial Ca(2+) coupling and of appropriate NADPH supply in respect to hormone production can be assumed. However, the importance of the mitochondrial factors has been neglected so far. Here, after summarizing earlier findings we provide new results obtained through modifying mitochondrial Ca(2+) uptake by knocking down p38 MAPK or OPA1 and overexpressing S100G, supporting the notion that mitochondrial Ca(2+) and reduced pyridine nucleotides are facilitating factors for both basal and stimulated steroid production.},
	year = {2012},
	eissn = {1532-1991},
	pages = {64-72},
	orcid-numbers = {Spät, András/0000-0001-8013-5631; Szanda, Gergő/0000-0002-1308-7593}
}

@article{MTMT:1892080,
	title = {Special features of mitochondrial Ca(2+) signalling in adrenal glomerulosa cells},
	url = {https://m2.mtmt.hu/api/publication/1892080},
	author = {Spät, András and Szanda, Gergő},
	doi = {10.1007/s00424-012-1086-y},
	journal-iso = {PFLUG ARCH EUR J PHY},
	journal = {PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY},
	volume = {464},
	unique-id = {1892080},
	issn = {0031-6768},
	abstract = {Aldosterone, secreted by adrenal glomerulosa cells, allows the adaptation of the vertebrate organism to a wide range of physiological and pathological stimuli including acute haemodynamic challenges and long-term changes in dietary sodium and potassium intake. Most of the extracellular signals are mediated by cytosolic Ca(2+) signal deriving from Ca(2+) release, store-operated and/or voltage-gated Ca(2+) influx. Mitochondria in glomerulosa cells play a fundamental role in generating and modulating the final biological response. These organelles not only house several enzymes of aldosterone biosynthesis but also-in a Ca(2+)-dependent manner-provide NADPH for the function of these enzymes. Moreover, mitochondria, constituting a high portion of cytoplasmic volume and displaying a uniquely low-threshold Ca(2+) sequestering ability, shape and thus modulate the decoding of the complex cytosolic Ca(2+) response. The unusual features of mitochondrial Ca(2+) signalling that permit such an integrative function in adrenal glomerulosa cells are hereby described.},
	year = {2012},
	eissn = {1432-2013},
	pages = {43-50},
	orcid-numbers = {Spät, András/0000-0001-8013-5631; Szanda, Gergő/0000-0002-1308-7593}
}

@article{MTMT:1836577,
	title = {Mapping of the localization of type I angiotensin receptor in membrane microdomains using bioluminescence resonance energy transfer-based sensors.},
	url = {https://m2.mtmt.hu/api/publication/1836577},
	author = {Balla, András and Tóth, Dániel and Soltész-Katona, Eszter and Szakadáti, Gyöngyi and Erdélyi, László Sándor and Várnai, Péter and Hunyady, László},
	doi = {10.1074/jbc.M111.293944},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {287},
	unique-id = {1836577},
	issn = {0021-9258},
	abstract = {Initiation and termination of signaling of the type I angiotensin receptor (AT1-R) can lead to dynamic changes in its localization in plasma membrane microdomains. Several markers were recently developed to investigate membrane microdomains. Here, we used several YFP-labeled fusion constructs (i.e. raft-, or non-raft plasma membrane markers) to analyze the agonist-induced changes in compartmentalization of AT1-R, including internalization or lateral movement between plasma membrane compartments in response to stimulation using bioluminescence resonance energy transfer (BRET) measurements. Our data demonstrate that angiotensin II (AngII) stimulus changes the microdomain localization of wild type or mutated (DRY/AAY or TSTS/A) AT1-Rs co-expressed with the fluorescent probes in HEK293 cells. The comparison of the trafficking of AT1-R upon AngII stimulus to those of [Sar1,Ile8]-AngII or [Sar1,Ile4,Ile8]-AngII stimulus revealed different type of changes depending on the nature of the ligand. The observed changes in receptor compartmentalization of the AT1-R are strikingly different from those of 5HT-2C and EGF receptors, which demonstrate the usefulness of the BRET-based measurements in the investigation of receptor trafficking in the plasma membrane in living cell experiments.},
	year = {2012},
	eissn = {1083-351X},
	pages = {9090-9099},
	orcid-numbers = {Balla, András/0000-0002-6450-2793; Tóth, Dániel/0000-0001-6670-3348; Soltész-Katona, Eszter/0000-0002-9054-740X; Szakadáti, Gyöngyi/0000-0002-9739-424X; Várnai, Péter/0000-0002-7777-806X; Hunyady, László/0000-0002-8438-7251}
}

@article{MTMT:1820411,
	title = {Physiological mechanisms of signal termination in biological systems},
	url = {https://m2.mtmt.hu/api/publication/1820411},
	author = {Ligeti, Erzsébet and Csépányi-Kömi, Roland and Hunyady, László},
	doi = {10.1111/j.1748-1716.2012.02414.x},
	journal-iso = {ACTA PHYSIOL},
	journal = {ACTA PHYSIOLOGICA},
	volume = {204},
	unique-id = {1820411},
	issn = {1748-1708},
	year = {2012},
	eissn = {1748-1716},
	pages = {469-478},
	orcid-numbers = {Ligeti, Erzsébet/0000-0001-6374-729X; Csépányi-Kömi, Roland/0000-0001-6825-7142; Hunyady, László/0000-0002-8438-7251}
}

@article{MTMT:1761606,
	title = {Regulation of endocannabinoid release by G proteins: A paracrine mechanism of G protein-coupled receptor action.},
	url = {https://m2.mtmt.hu/api/publication/1761606},
	author = {Gyombolai, Pál and Pap, Dorottya and Turu, Gábor and Catt, KJ and Bagdy, György and Hunyady, László},
	doi = {10.1016/j.mce.2011.10.011},
	journal-iso = {MOL CELL ENDOCRINOL},
	journal = {MOLECULAR AND CELLULAR ENDOCRINOLOGY},
	volume = {353},
	unique-id = {1761606},
	issn = {0303-7207},
	abstract = {In the past years, the relationship between the endocannabinoid system (ECS) and other hormonal and neuromodulatory systems has been intensively studied. G protein-coupled receptors (GPCRs) can stimulate endocannabinoid (eCB) production via activation of G(q/11) proteins and, in some cases, G(s) proteins. In this review, we summarize the pathways through which GPCR activation can trigger eCB release, as well as the best known examples of this process throughout the body tissues. Angiotensin II-induced activation of AT(1) receptors, similar to other G(q/11)-coupled receptors, can lead to the formation of 2-arachidonoylglycerol (2-AG), an important eCB. The importance of eCB formation in angiotensin II action is supported by the finding that the hypertensive effect of angiotensin II, injected directly into the hypothalamic paraventricular nucleus of anaesthetized rats, can be abolished by AM251, an inverse agonist of CB(1) cannabinoid receptors (CB(1)Rs). We conclude that activation of the ECS should be considered as a general consequence of the stimulation of G(q/11)-coupled receptors, and may mediate some of the physiological effects of GPCRs.},
	year = {2012},
	eissn = {1872-8057},
	pages = {29-36},
	orcid-numbers = {Turu, Gábor/0000-0002-4421-3812; Bagdy, György/0000-0001-8141-3410; Hunyady, László/0000-0002-8438-7251}
}

@article{MTMT:1713000,
	title = {Control mechanisms of mitochondrial Ca(2+) uptake feed-forward modulation of aldosterone secretion},
	url = {https://m2.mtmt.hu/api/publication/1713000},
	author = {Szanda, Gergő and Rajki, Anikó and Spät, András},
	doi = {10.1016/j.mce.2011.08.042},
	journal-iso = {MOL CELL ENDOCRINOL},
	journal = {MOLECULAR AND CELLULAR ENDOCRINOLOGY},
	volume = {353},
	unique-id = {1713000},
	issn = {0303-7207},
	abstract = {Mitochondrial Ca(2+) signal activates metabolism by boosting pyridine nucleotide reduction and ATP synthesis or, if Ca(2+) sequestration is supraphysiological, may even lead to apoptosis. Although the molecular background of mitochondrial Ca(2+) uptake has recently been elucidated, the regulation of Ca(2+) handling is still not properly clarified. In human adrenocortical H295R cells we found a regulatory mechanism involving p38 MAPK and novel-type PKC isoforms. Upon stimulation with angiotensin II (AII) these kinases are activated typically prior to the release of Ca(2+) and - most probably by reducing the Ca(2+) permeation through the outer mitochondrial membrane - attenuate mitochondrial Ca(2+) uptake in a feed-forward manner. The biologic significance of the kinase-mediated reduction of mitochondrial Ca(2+) signal is also reflected by the attenuation of AII-mediated aldosterone secretion. As another feed-forward mechanism, we found in HEK-293T and H295R cells that Ca(2+) signal evoked either by IP(3) or by voltage-gated influx is accompanied by a concomitant cytosolic Mg(2+) signal. In permeabilized HEK-293T cells Mg(2+) was found to be a potent inhibitor of mitochondrial Ca(2+) uptake in the physiologic [Mg(2+)] and [Ca(2+)] range. Thus, these inhibitory mechanisms may serve not only as protection against mitochondrial Ca(2+) overload and subsequent apoptosis but also have the potential to substantially alter physiological responses.},
	year = {2012},
	eissn = {1872-8057},
	pages = {101-108},
	orcid-numbers = {Szanda, Gergő/0000-0002-1308-7593; Spät, András/0000-0001-8013-5631}
}

@article{MTMT:1616625,
	title = {Modulation of the mitochondrial permeability transition by cyclophilin D: Moving closer to F(0)-F(1) ATP synthase?},
	url = {https://m2.mtmt.hu/api/publication/1616625},
	author = {Chinopoulos, Christos and Ádám, Veronika},
	doi = {10.1016/j.mito.2011.04.007},
	journal-iso = {MITOCHONDRION},
	journal = {MITOCHONDRION},
	volume = {12},
	unique-id = {1616625},
	issn = {1567-7249},
	year = {2012},
	eissn = {1872-8278},
	pages = {41-45},
	orcid-numbers = {Chinopoulos, Christos/0000-0003-0183-4149; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1728974,
	title = {The Effect of OPA1 on Mitochondrial Ca Signaling},
	url = {https://m2.mtmt.hu/api/publication/1728974},
	author = {Fülöp, László and Szanda, Gergő and Enyedi, Balázs and Várnai, Péter and Spät, András},
	doi = {10.1371/journal.pone.0025199},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {6},
	unique-id = {1728974},
	issn = {1932-6203},
	abstract = {The dynamin-related GTPase protein OPA1, localized in the intermembrane space and tethered to the inner membrane of mitochondria, participates in the fusion of these organelles. Its mutation is the most prevalent cause of Autosomal Dominant Optic Atrophy. OPA1 controls the diameter of the junctions between the boundary part of the inner membrane and the membrane of cristae and reduces the diffusibility of cytochrome c through these junctions. We postulated that if significant Ca(2+) uptake into the matrix occurs from the lumen of the cristae, reduced expression of OPA1 would increase the access of Ca(2+) to the transporters in the crista membrane and thus would enhance Ca(2+) uptake. In intact H295R adrenocortical and HeLa cells cytosolic Ca(2+) signals evoked with K(+) and histamine, respectively, were transferred into the mitochondria. The rate and amplitude of mitochondrial [Ca(2+)] rise (followed with confocal laser scanning microscopy and FRET measurements with fluorescent wide-field microscopy) were increased after knockdown of OPA1, as compared with cells transfected with control RNA or mitofusin1 siRNA. Ca(2+) uptake was enhanced despite reduced mitochondrial membrane potential. In permeabilized cells the rate of Ca(2+) uptake by depolarized mitochondria was also increased in OPA1-silenced cells. The participation of Na(+)/Ca(2+) and Ca(2+)/H(+) antiporters in this transport process is indicated by pharmacological data. Altogether, our observations reveal the significance of OPA1 in the control of mitochondrial Ca(2+) metabolism.},
	year = {2011},
	eissn = {1932-6203},
	orcid-numbers = {Szanda, Gergő/0000-0002-1308-7593; Enyedi, Balázs/0000-0001-5713-3785; Várnai, Péter/0000-0002-7777-806X; Spät, András/0000-0001-8013-5631}
}