TY - CHAP AU - Jourdan, Tony AU - Degrace, Pascal AU - González-Mariscal, Isabel AU - Szanda, Gergő AU - Tam, Joseph TI - Endocannabinoids: the lipid effectors of metabolic regulation in health and disease T2 - Lipid Signaling and Metabolism PB - Academic Press CY - Cambridge, Massachusetts SN - 9780128194041 PY - 2020 SP - 297 EP - 320 PG - 24 DO - 10.1016/B978-0-12-819404-1.00015-4 UR - https://m2.mtmt.hu/api/publication/31634956 ID - 31634956 LA - English DB - MTMT ER - TY - CHAP AU - Spät, András AU - Szanda, Gergő ED - Groschner, K ED - Graier, W F ED - Romanin, C TI - Store-operated Ca2+ entry and mitochondria T2 - Store-operated Ca2+ entry (SOCE) pathways PB - Springer-Verlag Wien CY - Wien SN - 9783709109618 PY - 2012 SP - 177 EP - 192 PG - 16 UR - https://m2.mtmt.hu/api/publication/1901913 ID - 1901913 LA - English DB - MTMT ER - TY - JOUR AU - Spät, András AU - Fülöp, László AU - Szanda, Gergő TI - The role of mitochondrial Ca(2+) and NAD(P)H in the control of aldosterone secretion. JF - CELL CALCIUM J2 - CELL CALCIUM VL - 52 PY - 2012 IS - 1 SP - 64 EP - 72 PG - 9 SN - 0143-4160 DO - 10.1016/j.ceca.2012.01.009 UR - https://m2.mtmt.hu/api/publication/1892081 ID - 1892081 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Spät, András AU - Szanda, Gergő TI - Special features of mitochondrial Ca(2+) signalling in adrenal glomerulosa cells JF - PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY J2 - PFLUG ARCH EUR J PHY VL - 464 PY - 2012 IS - 1 SP - 43 EP - 50 PG - 8 SN - 0031-6768 DO - 10.1007/s00424-012-1086-y UR - https://m2.mtmt.hu/api/publication/1892080 ID - 1892080 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Balla, András AU - Tóth, Dániel AU - Soltész-Katona, Eszter AU - Szakadáti, Gyöngyi AU - Erdélyi, László Sándor AU - Várnai, Péter AU - Hunyady, László TI - Mapping of the localization of type I angiotensin receptor in membrane microdomains using bioluminescence resonance energy transfer-based sensors. JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 287 PY - 2012 IS - 12 SP - 9090 EP - 9099 PG - 10 SN - 0021-9258 DO - 10.1074/jbc.M111.293944 UR - https://m2.mtmt.hu/api/publication/1836577 ID - 1836577 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Ligeti, Erzsébet AU - Csépányi-Kömi, Roland AU - Hunyady, László TI - Physiological mechanisms of signal termination in biological systems JF - ACTA PHYSIOLOGICA J2 - ACTA PHYSIOL VL - 204 PY - 2012 IS - 4 SP - 469 EP - 478 PG - 10 SN - 1748-1708 DO - 10.1111/j.1748-1716.2012.02414.x UR - https://m2.mtmt.hu/api/publication/1820411 ID - 1820411 LA - English DB - MTMT ER - TY - JOUR AU - Gyombolai, Pál AU - Pap, Dorottya AU - Turu, Gábor AU - Catt, KJ AU - Bagdy, György AU - Hunyady, László TI - Regulation of endocannabinoid release by G proteins: A paracrine mechanism of G protein-coupled receptor action. JF - MOLECULAR AND CELLULAR ENDOCRINOLOGY J2 - MOL CELL ENDOCRINOL VL - 353 PY - 2012 IS - 1-2 SP - 29 EP - 36 PG - 8 SN - 0303-7207 DO - 10.1016/j.mce.2011.10.011 UR - https://m2.mtmt.hu/api/publication/1761606 ID - 1761606 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Szanda, Gergő AU - Rajki, Anikó AU - Spät, András TI - Control mechanisms of mitochondrial Ca(2+) uptake feed-forward modulation of aldosterone secretion JF - MOLECULAR AND CELLULAR ENDOCRINOLOGY J2 - MOL CELL ENDOCRINOL VL - 353 PY - 2012 IS - 1-2 SP - 101 EP - 108 PG - 8 SN - 0303-7207 DO - 10.1016/j.mce.2011.08.042 UR - https://m2.mtmt.hu/api/publication/1713000 ID - 1713000 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Chinopoulos, Christos AU - Ádám, Veronika TI - Modulation of the mitochondrial permeability transition by cyclophilin D: Moving closer to F(0)-F(1) ATP synthase? JF - MITOCHONDRION J2 - MITOCHONDRION VL - 12 PY - 2012 IS - 1 SP - 41 EP - 45 PG - 5 SN - 1567-7249 DO - 10.1016/j.mito.2011.04.007 UR - https://m2.mtmt.hu/api/publication/1616625 ID - 1616625 LA - English DB - MTMT ER - TY - JOUR AU - Fülöp, László AU - Szanda, Gergő AU - Enyedi, Balázs AU - Várnai, Péter AU - Spät, András TI - The Effect of OPA1 on Mitochondrial Ca Signaling JF - PLOS ONE J2 - PLOS ONE VL - 6 PY - 2011 IS - 9 PG - 11 SN - 1932-6203 DO - 10.1371/journal.pone.0025199 UR - https://m2.mtmt.hu/api/publication/1728974 ID - 1728974 N1 - Department of Physiology, Faculty of Medicine, Semmelweis University, Hungarian Academy of Sciences, Budapest, Hungary Laboratory of Neurobiochemistry and Molecular Physiology, Hungarian Academy of Sciences, Budapest, Hungary Cited By :45 Export Date: 10 November 2022 Correspondence Address: Spät, A.; Department of Physiology, Faculty of Medicine, , Budapest, Hungary; email: spat@eok.sote.hu Chemicals/CAS: RNA, 63231-63-0; calcium ion, 14127-61-8; guanosine triphosphatase, 9059-32-9; histamine, 51-45-6, 56-92-8, 93443-21-1; potassium ion, 24203-36-9; calcium, 14092-94-5, 7440-70-2; Antiporters; Calcium, 7440-70-2; GTP Phosphohydrolases, 3.6.1.-; OPA1 protein, human, 3.6.1.-; RNA, Small Interfering; Sodium-Calcium Exchanger AB - 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. LA - English DB - MTMT ER -