TY - CHAP AU - Sőti, Csaba ED - Mandl, József ED - Csala, Miklós TI - Az öregedés T2 - Orvosi patobiokémia PB - Medicina Könyvkiadó Zrt. CY - Budapest SN - 9789632267821 PY - 2023 SP - 405 EP - 419 PG - 15 UR - https://m2.mtmt.hu/api/publication/34715613 ID - 34715613 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Hajdú, Gábor AU - Somogyvári, Milán AU - Csermely, Péter AU - Sőti, Csaba TI - Lysosome-related organelles promote stress and immune responses in C. elegans JF - COMMUNICATIONS BIOLOGY J2 - COMMUN BIOL VL - 6 PY - 2023 IS - 1 PG - 17 SN - 2399-3642 DO - 10.1038/s42003-023-05246-7 UR - https://m2.mtmt.hu/api/publication/34144416 ID - 34144416 AB - Lysosome-related organelles (LROs) play diverse roles and their dysfunction causes immunodeficiency. However, their primordial functions remain unclear. Here, we report that C. elegans LROs (gut granules) promote organismal defenses against various stresses. We find that toxic benzaldehyde exposure induces LRO autofluorescence, stimulates the expression of LRO-specific genes and enhances LRO transport capacity as well as increases tolerance to benzaldehyde, heat and oxidative stresses, while these responses are impaired in glo-1 /Rab32 and pgp- 2 ABC transporter LRO biogenesis mutants. Benzaldehyde upregulates glo-1 - and pgp-2- dependent expression of heat shock, detoxification and antimicrobial effector genes, which requires daf-16 /FOXO and/or pmk-1 /p38MAPK. Finally, benzaldehyde preconditioning increases resistance against Pseudomonas aeruginosa PA14 in a glo-1 - and pgp-2 -dependent manner, and PA14 infection leads to the deposition of fluorescent metabolites in LROs and induction of LRO genes. Our study suggests that LROs may play a role in systemic responses to stresses and in pathogen resistance. LA - English DB - MTMT ER - TY - JOUR AU - Varga, Attila AU - Nguyen, Minh Tu AU - Pénzes, Kinga AU - Bátai, Bence AU - Gyulavári, Pál AU - Gurbi, Bianka AU - Murányi, József AU - Csermely, Péter AU - Csala, Miklós AU - Vántus, Tibor AU - Sőti, Csaba TI - Protein Kinase D3 (PKD3) Requires Hsp90 for Stability and Promotion of Prostate Cancer Cell Migration JF - CELLS J2 - CELLS-BASEL VL - 12 PY - 2023 IS - 2 PG - 15 SN - 2073-4409 DO - 10.3390/cells12020212 UR - https://m2.mtmt.hu/api/publication/33541689 ID - 33541689 N1 - Department of Molecular Biology, Semmelweis University, Budapest, 1094, Hungary MTA-SE Pathobiochemistry Research Group, Semmelweis University, Budapest, 1094, Hungary Institute of Medical Microbiology, Semmelweis University, Budapest, 1089, Hungary HCEMM-SU Molecular Oncohematology Research Group, Department of Pathology and Experimental Cancer Research, Semmelweis University, Budapest, 1085, Hungary IQVIA Hungary, Budapest, 1117, Hungary Cited By :2 Export Date: 19 January 2024 Correspondence Address: Varga, A.; Department of Molecular Biology, Hungary; email: varga.attila@med.semmelweis-univ.hu Correspondence Address: Sőti, C.; Department of Molecular Biology, Hungary; email: soti.csaba@med.semmelweis-univ.hu AB - Prostate cancer metastasis is a significant cause of mortality in men. PKD3 facilitates tumor growth and metastasis, however, its regulation is largely unclear. The Hsp90 chaperone stabilizes an array of signaling client proteins, thus is an enabler of the malignant phenotype. Here, using different prostate cancer cell lines, we report that Hsp90 ensures PKD3 conformational stability and function to promote cancer cell migration. We found that pharmacological inhibition of either PKDs or Hsp90 dose-dependently abrogated the migration of DU145 and PC3 metastatic prostate cancer cells. Hsp90 inhibition by ganetespib caused a dose-dependent depletion of PKD2, PKD3, and Akt, which are all involved in metastasis formation. Proximity ligation assay and immunoprecipitation experiments demonstrated a physical interaction between Hsp90 and PKD3. Inhibition of the chaperone–client interaction induced misfolding and proteasomal degradation of PKD3. PKD3 siRNA combined with ganetespib treatment demonstrated a specific involvement of PKD3 in DU145 and PC3 cell migration, which was entirely dependent on Hsp90. Finally, ectopic expression of PKD3 enhanced migration of non-metastatic LNCaP cells in an Hsp90-dependent manner. Altogether, our findings identify PKD3 as an Hsp90 client and uncover a potential mechanism of Hsp90 in prostate cancer metastasis. The molecular interaction revealed here may regulate other biological and pathological functions. LA - English DB - MTMT ER - TY - JOUR AU - Somogyvári, Milán AU - Khatatneh, Saba AU - Sőti, Csaba TI - Hsp90: From Cellular to Organismal Proteostasis JF - CELLS J2 - CELLS-BASEL VL - 11 PY - 2022 IS - 16 PG - 20 SN - 2073-4409 DO - 10.3390/cells11162479 UR - https://m2.mtmt.hu/api/publication/33061712 ID - 33061712 N1 - Export Date: 14 November 2022 Correspondence Address: Somogyvári, M.; Department of Molecular Biology, Hungary; email: somogyvari.milan@med.semmelweis-univ.hu Correspondence Address: Sőti, C.; Department of Molecular Biology, Hungary; email: soti.csaba@med.semmelweis-univ.hu AB - Assuring a healthy proteome is indispensable for survival and organismal health. Proteome disbalance and the loss of the proteostasis buffer are hallmarks of various diseases. The essential molecular chaperone Hsp90 is a regulator of the heat shock response via HSF1 and a stabilizer of a plethora of signaling proteins. In this review, we summarize the role of Hsp90 in the cellular and organismal regulation of proteome maintenance. LA - English DB - MTMT ER - TY - JOUR AU - Griñán-Ferré, Christian AU - Bellver-Sanchis, Aina AU - Izquierdo, Vanessa AU - Corpas, Rubén AU - Roig-Soriano, Joan AU - Chillón, Miguel AU - Andres-Lacueva, Cristina AU - Somogyvári, Milán AU - Sőti, Csaba AU - Sanfeliu, C AU - Mercè, Pallàs TI - The pleiotropic neuroprotective effects of resveratrol in cognitive decline and Alzheimer’s disease pathology: from antioxidant to epigenetic therapy. JF - AGEING RESEARCH REVIEWS J2 - AGEING RES REV VL - 67 PY - 2021 PG - 24 SN - 1568-1637 DO - 10.1016/j.arr.2021.101271 UR - https://m2.mtmt.hu/api/publication/31847732 ID - 31847732 N1 - Funding Agency and Grant Number: Ministerio de Economia, Industria y Competitividad (Agencia Estatal de Investigacion, AEI); Fondo Europeo de Desarrollo Regional (MINECO-FEDER) [PID2019-106285RB, PCIN-2015-229]; Generalitat de CatalunyaGeneralitat de Catalunya [2017 SGR 106]; Hungarian Science FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA K 116525]; Semmelweis University [STIA-KFI-2020/132257/AOMBT/2020] Funding text: This study was supported by the Ministerio de Economia, Industria y Competitividad (Agencia Estatal de Investigacion, AEI) and Fondo Europeo de Desarrollo Regional (MINECO-FEDER) (PID2019-106285RB and PCIN-2015-229, and Generalitat de Catalunya (2017 SGR 106) to M. P. The work was funded by grants from the Hungarian Science Foundation (OTKA K 116525), and from the Semmelweis University (STIA-KFI-2020/132257/AOMBT/2020) to C.S. LA - English DB - MTMT ER - TY - JOUR AU - Lovas, Attila AU - Szilágyi, Brigitta AU - Bosnyák, Edit AU - Ács, Pongrác AU - Oláh, András AU - Komka, Zsolt AU - Tóth, Miklós AU - Merkely, Béla Péter AU - Németh, Endre AU - Gilányi, Beatrix AU - Krepuska, Miklós AU - Sőti, Csaba AU - Sótonyi, Péter TI - Reaction Kinetics Modeling of eHsp70 Induced by Norepinephrine in Response to Exercise Stress JF - INTERNATIONAL JOURNAL OF SPORTS MEDICINE J2 - INT J SPORTS MED VL - 42 PY - 2021 IS - 6 SP - 506 EP - 512 PG - 7 SN - 0172-4622 DO - 10.1055/a-1224-3792 UR - https://m2.mtmt.hu/api/publication/31781703 ID - 31781703 N1 - Institute of Mathematics, Budapest University of Technology and Economics, Budapest, Hungary Department of Health Sciences and Sport Medicine, University of Physical Education, Budapest, Hungary Faculty of Health Sciences, University of Pecs, Pecs, Hungary Department of Cardiology, Heart and Vascular Center, FIFA, Medical Centre of Excellence, Semmelweis University Budapest, Hungary Department of Combat Sports, University of Physical Education, Budapest, Hungary Institute of Medical Chemistry Molecular Biology and Pathobiochemistry, Semmelweis University, Budapest, Hungary Department of Vascular Surgery, Heart and Vascular Center, Semmelweis University, Budapest, Hungary Pázmány Péter Catholic University, Faculty of Information Technology and Bionics, Budapest, Hungary Cited By :1 Export Date: 14 November 2022 CODEN: IJSMD Correspondence Address: Krepuska, M.; Vascular Surgery, Városmajor u. 68., Hungary; email: mkrepuska@gmail.com LA - English DB - MTMT ER - TY - JOUR AU - Hajdú, Gábor AU - Gecse, Eszter AU - Taisz, István AU - Móra , István András AU - Sőti, Csaba TI - Toxic stress-specific cytoprotective responses regulate learned behavioral decisions in C. elegans JF - BMC BIOLOGY J2 - BMC BIOL VL - 19 PY - 2021 IS - 1 PG - 20 SN - 1741-7007 DO - 10.1186/s12915-021-00956-y UR - https://m2.mtmt.hu/api/publication/31206109 ID - 31206109 N1 - Department of Molecular Biology, Semmelweis University, Budapest, Hungary Current Address: Neurobiology Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom Cited By :1 Export Date: 12 November 2022 Correspondence Address: Sőti, C.; Department of Molecular Biology, Hungary; email: soti.csaba@med.semmelweis-univ.hu LA - English DB - MTMT ER - TY - JOUR AU - Fenyves, Bánk AU - Szilágyi, Gábor S. AU - Vassy, Zsolt AU - Sőti, Csaba AU - Csermely, Péter TI - Synaptic polarity and sign-balance prediction using gene expression data in the Caenorhabditis elegans chemical synapse neuronal connectome network JF - PLOS COMPUTATIONAL BIOLOGY J2 - PLOS COMPUT BIOL VL - 16 PY - 2020 IS - 12 PG - 19 SN - 1553-734X DO - 10.1371/journal.pcbi.1007974 UR - https://m2.mtmt.hu/api/publication/31790902 ID - 31790902 N1 - Department of Molecular Biology, Semmelweis University, Budapest, Hungary Department of Emergency Medicine, Semmelweis University, Budapest, Hungary Cited By :6 Export Date: 31 July 2023 Correspondence Address: Csermely, P.; Department of Molecular Biology, Hungary; email: csermelynet@gmail.com Chemicals/CAS: Caenorhabditis elegans Proteins AB - Graph theoretical analyses of nervous systems usually omit the aspect of connection polarity, due to data insufficiency. The chemical synapse network of Caenorhabditis elegans is a well-reconstructed directed network, but the signs of its connections are yet to be elucidated. Here, we present the gene expression-based sign prediction of the ionotropic chemical synapse connectome of C. elegans (3,638 connections and 20,589 synapses total), incorporating available presynaptic neurotransmitter and postsynaptic receptor gene expression data for three major neurotransmitter systems. We made predictions for more than two-thirds of these chemical synapses and observed an excitatory-inhibitory (E:I) ratio close to 4:1 which was found similar to that observed in many real-world networks. Our open source tool (http://EleganSign.linkgroup.hu) is simple but efficient in predicting polarities by integrating neuronal connectome and gene expression data. LA - English DB - MTMT ER - TY - JOUR AU - Eőry, Ajándék AU - Szabó, János AU - Csik, Ivett AU - Csupor, Dezső AU - Sőti, Csaba AU - Kalabay, László AU - Varsányi, Péter AU - Komsa, Ildikó AU - Eőry, Ajándok AU - Torzsa, Péter TI - Az integratív medicina képzésének hazai koncepciója nemzetközi minták alapján JF - ORVOSI HETILAP J2 - ORV HETIL VL - 161 PY - 2020 IS - 27 SP - 1122 EP - 1130 PG - 9 SN - 0030-6002 DO - 10.1556/650.2020.31754 UR - https://m2.mtmt.hu/api/publication/31356446 ID - 31356446 N1 - * Megosztott szerzőség LA - Hungarian DB - MTMT ER - TY - GEN AU - Hajdú, Gábor AU - Taisz, I AU - Móra, I AU - Sőti, Csaba TI - Toxic stress-pecific molecular cytoprotective responses determine behavioural adaptation in C. elegans PY - 2019 UR - https://m2.mtmt.hu/api/publication/31173629 ID - 31173629 N1 - poszter LA - English DB - MTMT ER -