TY  - JOUR
AU  - Dukic, Barbara
AU  - Ruppert, Zsófia
AU  - Tóth, Erzsébet Melinda
AU  - Hunya, Ákos
AU  - Czibula, Ágnes
AU  - Bíró, Péter
AU  - Tiszlavicz, Ádám
AU  - Péter, Mária
AU  - Balogh, Gábor
AU  - Erdélyi, Miklós
AU  - Timinszky, Gyula
AU  - Vigh, László
AU  - Gombos, Imre
AU  - Török, Zsolt
TI  - Mild Hyperthermia-Induced Thermogenesis in the Endoplasmic Reticulum Defines Stress Response Mechanisms
JF  - CELLS
J2  - CELLS-BASEL
VL  - 13
PY  - 2024
IS  - 13
PG  - 16
SN  - 2073-4409
DO  - 10.3390/cells13131141
UR  - https://m2.mtmt.hu/api/publication/35083838
ID  - 35083838
N1  - Funding Agency and Grant Number: National Research, Development and Innovation Office [OTKA ANN132280, OTKA K135759, OTKA K143248, OTKA FK135699, 2018-1.1.2-KFI-2018-00202, TKP2021-NVA-19]; Hungarian Research Network [SA-72/2021]
            Funding text: This research was funded by the National Research, Development and Innovation Office(OTKA ANN132280, OTKA K135759, OTKA K143248, OTKA FK135699, 2018-1.1.2-KFI-2018-00202,TKP2021-NVA-19) and the Hungarian Research Network (SA-72/2021).
AB  - Previous studies reported that a mild, non-protein-denaturing, fever-like temperature increase induced the unfolded protein response (UPR) in mammalian cells. Our dSTORM super-resolution microscopy experiments revealed that the master regulator of the UPR, the IRE1 (inositol-requiring enzyme 1) protein, is clustered as a result of UPR activation in a human osteosarcoma cell line (U2OS) upon mild heat stress. Using ER thermo yellow, a temperature-sensitive fluorescent probe targeted to the endoplasmic reticulum (ER), we detected significant intracellular thermogenesis in mouse embryonic fibroblast (MEF) cells. Temperatures reached at least 8 °C higher than the external environment (40 °C), resulting in exceptionally high ER temperatures similar to those previously described for mitochondria. Mild heat-induced thermogenesis in the ER of MEF cells was likely due to the uncoupling of the Ca2+/ATPase (SERCA) pump. The high ER temperatures initiated a pronounced cytosolic heat-shock response in MEF cells, which was significantly lower in U2OS cells in which both the ER thermogenesis and SERCA pump uncoupling were absent. Our results suggest that depending on intrinsic cellular properties, mild hyperthermia-induced intracellular thermogenesis defines the cellular response mechanism and determines the outcome of hyperthermic stress.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Hetényi, Anasztázia
AU  - Szabó, Enikő
AU  - Imre, Norbert
AU  - Nath Bhaumik, Kaushik
AU  - Tököli, Attila
AU  - Füzesi, Tamás
AU  - Hollandi, Réka
AU  - Horváth, Péter
AU  - Czibula, Ágnes
AU  - Monostori, Éva
AU  - Deli, Mária Anna
AU  - Martinek, Tamás
TI  - α/β-Peptides as Nanomolar Triggers of Lipid Raft-Mediated Endocytosis through GM1 Ganglioside Recognition
JF  - PHARMACEUTICS
J2  - PHARMACEUTICS
VL  - 14
PY  - 2022
IS  - 3
PG  - 11
SN  - 1999-4923
DO  - 10.3390/pharmaceutics14030580
UR  - https://m2.mtmt.hu/api/publication/32733913
ID  - 32733913
N1  - Funding Agency and Grant Number: National Research, Development and Innovation Office of HungaryNational Research, Development & Innovation Office (NRDIO) - Hungary [GINOP-2.2.1-15-2016-00007]; Hungarian Ministry of Innovation and Technology [TUDFO/47138-1/2019-ITM]; Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG); Hungarian Academy of Sciences LENDULET-FoldamerHungarian Academy of Sciences; NKFINational Research, Development & Innovation Office (NRDIO) - Hungary [K134754]; Finnish TEKES FiDiPro Fellow Grant [40294/13]; Hungarian Academy of Sciences LENDULET-BiomagHungarian Academy of Sciences; Ministry of Innovation and Technology of Hungary through the National Research, Development and Innovation Fund [TKP2021-EGA-32]
            Funding text: This research was funded by the National Research, Development and Innovation Office of Hungary, grant number GINOP-2.2.1-15-2016-00007, the Hungarian Ministry of Innovation and Technology, TUDFO/47138-1/2019-ITM, and the Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG). T.A.M. acknowledges support from the Hungarian Academy of Sciences LENDULET-Foldamer, and NKFI K134754. P.H. acknowledges support from the Finnish TEKES FiDiPro Fellow Grant 40294/13, and the Hungarian Academy of Sciences LENDULET-Biomag. Support by the Ministry of Innovation and Technology of Hungary through the National Research, Development and Innovation Fund (TKP2021-EGA-32) is acknowledged.
AB  - Cell delivery of therapeutic macromolecules and nanoparticles is a critical drug development challenge. Translocation through lipid raft-mediated endocytic mechanisms is being sought, as it can avoid rapid lysosomal degradation. Here, we present a set of short alpha/beta-peptide tags with high affinity to the lipid raft-associated ganglioside GM1. These sequences induce effective internalization of the attached immunoglobulin cargo. The structural requirements of the GM1-peptide interaction are presented, and the importance of the membrane components are shown. The results contribute to the development of a receptor-based cell delivery platform.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Hetényi, Anasztázia
AU  - Imre, Norbert
AU  - Szabó, Enikő
AU  - Bodnár, Brigitta
AU  - Szkalisity, Ábel
AU  - Gróf, Ilona
AU  - Bocsik, Alexandra
AU  - Deli, Mária Anna
AU  - Horváth, Péter
AU  - Czibula, Ágnes
AU  - Monostori, Éva
AU  - Martinek, Tamás
TI  - Fehérje méretű molekulák humán sejtekbe juttatása lipid-raft mediált endocitózissal
JF  - BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA
J2  - BIOKÉMIA
VL  - 45
PY  - 2021
IS  - 4
SP  - 67
EP  - 83
PG  - 17
SN  - 0133-8455
UR  - https://m2.mtmt.hu/api/publication/32570862
ID  - 32570862
N1  - Nincs jelölve levelező szerzőség a közleményen. (BÉ SZTE admin5)
LA  - Hungarian
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Tököli, Attila
AU  - Mag, Beáta Zsófia
AU  - Bartus, Éva
AU  - Wéber, Edit
AU  - Szakonyi, Gerda
AU  - Simon, Márton
AU  - Czibula, Ágnes
AU  - Monostori, Éva
AU  - Nyitray, László
AU  - Martinek, Tamás
TI  - Proteomimetic surface fragments distinguish targets by function
JF  - CHEMICAL SCIENCE
J2  - CHEM SCI
VL  - 11
PY  - 2020
IS  - 38
SP  - 10390
EP  - 10398
PG  - 9
SN  - 2041-6520
DO  - 10.1039/d0sc03525d
UR  - https://m2.mtmt.hu/api/publication/31598466
ID  - 31598466
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Imre, Norbert
AU  - Hetényi, Anasztázia
AU  - Szabó, Enikő
AU  - Bodnár, Brigitta
AU  - Szkalisity, Ábel
AU  - Gróf, Ilona
AU  - Bocsik, Alexandra
AU  - Deli, Mária Anna
AU  - Horváth, Péter
AU  - Czibula, Ágnes
AU  - Monostori, Éva
AU  - Martinek, Tamás
TI  - Routing Nanomolar Protein Cargoes to Lipid Raft‐Mediated/Caveolar Endocytosis through a Ganglioside GM1‐Specific Recognition Tag
JF  - ADVANCED SCIENCE
J2  - ADV SCI
VL  - 7
PY  - 2020
IS  - 4
PG  - 10
SN  - 2198-3844
DO  - 10.1002/advs.201902621
UR  - https://m2.mtmt.hu/api/publication/31126947
ID  - 31126947
N1  - Funding text: This research was funded by the National Research, Development and Innovation Office of Hungary, grant number GINOP-2.2.1-15-2016-00007, the Hungarian Ministry of Innovation and Technology, TUDFO/47138-1/2019-ITM, and Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG). T.A.M. acknowledges support from the Hungarian Academy of Sciences LENDULET-Foldamer. P.H. acknowledges support from the Finnish TEKES FiDiPro Fellow Grant 40294/13, the Hungarian Academy of Sciences LENDULET-Biomag.
AB  - There is a pressing need to develop ways to deliver therapeutic macromolecules to their intracellular targets. Certain viral and bacterial proteins are readily internalized in functional form through lipid raft‐mediated/caveolar endocytosis, but mimicking this process with protein cargoes at therapeutically relevant concentrations is a great challenge. Targeting ganglioside GM1 in the caveolar pits triggers endocytosis. A pentapeptide sequence WYKYW is presented, which specifically captures the glycan moiety of GM1 (<jats:italic>K</jats:italic><jats:sub>D</jats:sub> = 24 n<jats:sc>m</jats:sc>). The WYKYW‐tag facilitates the GM1‐dependent endocytosis of proteins in which the cargo‐loaded caveosomes do not fuse with lysosomes. A structurally intact immunoglobulin G complex (580 kDa) is successfully delivered into live HeLa cells at extracellular concentrations ranging from 20 to 160 n<jats:sc>m</jats:sc>, and escape of the cargo proteins to the cytosol is observed. The short peptidic WYKYW‐tag is an advantageous endocytosis routing sequence for lipid raft‐mediated/caveolar cell delivery of therapeutic macromolecules, especially for cancer cells that overexpress GM1.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Szabó, Enikő
AU  - Hornung, Ákos
AU  - Monostori, Éva
AU  - Bocskai, Márta
AU  - Czibula, Ágnes
AU  - Kovács, László
TI  - Altered Cell Surface N-Glycosylation of Resting and Activated T Cells in Systemic Lupus Erythematosus
JF  - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
J2  - INT J MOL SCI
VL  - 20
PY  - 2019
IS  - 18
PG  - 14
SN  - 1661-6596
DO  - 10.3390/ijms20184455
UR  - https://m2.mtmt.hu/api/publication/30802849
ID  - 30802849
N1  - Institute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary            
            Department of Rheumatology and Immunology, Faculty of Medicine, University of Szeged, Szeged, 6725, Hungary            
            Export Date: 29 November 2019            
            Correspondence Address: Czibula, Á.; Institute of Genetics, Biological Research Centre of the Hungarian Academy of SciencesHungary; email: czibula.agnes@brc.hu            
            Chemicals/CAS: galectin 1, 258495-34-0; sialidase, 9001-67-6; sialyltransferase, 9075-81-4
Institute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary            
            Department of Rheumatology and Immunology, Faculty of Medicine, University of Szeged, Szeged, 6725, Hungary            
            Export Date: 2 December 2019            
            Correspondence Address: Czibula, Á.; Institute of Genetics, Biological Research Centre of the Hungarian Academy of SciencesHungary; email: czibula.agnes@brc.hu            
            Chemicals/CAS: galectin 1, 258495-34-0; sialidase, 9001-67-6; sialyltransferase, 9075-81-4
AB  - Altered cell surface glycosylation in congenital and acquired diseases has been shown to affect cell differentiation and cellular responses to external signals. Hence, it may have an important role in immune regulation; however, T cell surface glycosylation has not been studied in systemic lupus erythematosus (SLE), a prototype of autoimmune diseases. Analysis of the glycosylation of T cells from patients suffering from SLE was performed by lectin-binding assay, flow cytometry, and quantitative real-time PCR. The results showed that resting SLE T cells presented an activated-like phenotype in terms of their glycosylation pattern. Additionally, activated SLE T cells bound significantly less galectin-1 (Gal-1), an important immunoregulatory lectin, while other lectins bound similarly to the controls. Differential lectin binding, specifically Gal-1, to SLE T cells was explained by the increased gene expression ratio of sialyltransferases and neuraminidase 1 (NEU1), particularly by elevated ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1)/NEU1 and ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6)/NEU1 ratios. These findings indicated an increased terminal sialylation. Indeed, neuraminidase treatment of cells resulted in the increase of Gal-1 binding. Altered T cell surface glycosylation may predispose the cells to resistance to the immunoregulatory effects of Gal-1, and may thus contribute to the pathomechanism of SLE.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Li, Yang
AU  - James, Sharmy J
AU  - Wyllie, David H
AU  - Wynne, Claire
AU  - Czibula, Ágnes
AU  - Bukhari, Ahmed
AU  - Pye, Katherine
AU  - Bte Mustafah, Seri Musfirah
AU  - Fajka-Boja, Roberta
AU  - Szabó, Enikő
AU  - Angyal, Adrienn
AU  - Hegedűs, Zoltán
AU  - Kovács, László
AU  - Hill, Adrian V S
AU  - Jefferies, Caroline A
AU  - Wilson, Heather L
AU  - Yongliang, Zhang
AU  - Kiss-Tóth, Endre
TI  - TMEM203 is a binding partner and regulator of STING-mediated inflammatory signaling in macrophages
JF  - PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
J2  - P NATL ACAD SCI USA
VL  - 116
PY  - 2019
IS  - 33
SP  - 16479
EP  - 16488
PG  - 10
SN  - 0027-8424
DO  - 10.1073/pnas.1901090116
UR  - https://m2.mtmt.hu/api/publication/30750520
ID  - 30750520
AB  - Regulation of IFN signaling is critical in host recognition and response to pathogens while its dysregulation underlies the pathogenesis of several chronic diseases. STimulator of IFN Genes (STING) has been identified as a critical mediator of IFN inducing innate immune pathways, but little is known about direct coregulators of this protein. We report here that TMEM203, a conserved putative transmembrane protein, is an intracellular regulator of STING-mediated signaling. We show that TMEM203 interacts, functionally cooperates, and comigrates with STING following cell stimulation, which in turn leads to the activation of the kinase TBK1, and the IRF3 transcription factor. This induces target genes in macrophages, including IFN-β. Using Tmem203 knockout bone marrow-derived macrophages and transient knockdown of TMEM203 in human monocyte-derived macrophages, we show that TMEM203 protein is required for cGAMP-induced STING activation. Unlike STING, TMEM203 mRNA levels are elevated in T cells from patients with systemic lupus erythematosus, a disease characterized by the overexpression of type I interferons. Moreover, TMEM203 mRNA levels are associated with disease activity, as assessed by serum levels of the complement protein C3. Identification of TMEM203 sheds light into the control of STING-mediated innate immune responses, providing a potential novel mechanism for therapeutic interventions in STING-associated inflammatory diseases.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Kriston-Pál, Éva
AU  - Czibula, Ágnes
AU  - Gyuris, Z
AU  - Balka, Gyula
AU  - Seregi, A
AU  - Sükösd, Farkas
AU  - Süth, Miklós
AU  - Kiss-Tóth, E
AU  - Haracska, Lajos
AU  - Uher, Ferenc
AU  - Monostori, Éva
TI  - Characterization and therapeutic application of canine adipose mesenchymal stem cells to treat elbow osteoarthritis
JF  - CANADIAN JOURNAL OF VETERINARY RESEARCH-REVUE CANADIENNE DE RECHERCHE VETERINAIRE
J2  - CAN J VET RES
VL  - 81
PY  - 2017
IS  - 1
SP  - 73
EP  - 78
PG  - 6
SN  - 0830-9000
UR  - https://m2.mtmt.hu/api/publication/3190067
ID  - 3190067
N1  - Funding Agency and Grant Number:  [GINOP-2.3.2-15-2016-00020];  [GINOP-221-5-2016-00007]
            Funding text: The authors thank Karolina Korom and Marietta Gorog for collecting information from dogs' owners and liaising with the veterinarians involved in the program. We are grateful to the veterinarians, Drs. Otto Sebo (Small Animal Clinic, Mako), Peter Pal Muka (Profivet Veterinary Surgery Center and Animal Hospital, God), Peter Makai (MiniVet Small Animal Clinic, Budapest), Gyorgy Pelle (Teaching Animal Hospital, Nyiregyhaza), and Andras Banfi (PrimaVet Small Animal Clinic, Budapest), for surgery, transplantation, and supervision of the dogs. The authors also thank Akos Hornung for helpful advice about statistical evaluation and Mrs. Andrea Gercso and Katalin Kovacs for their excellent assistance. This work was supported by grants, GINOP-2.3.2-15-2016-00020 and GINOP-221-5-2016-00007.
AB  - Visceral adipose tissue (AT) obtained from surgical waste during routine ovariectomies was used as a source for isolating canine mesenchymal stem cells (MSCs). As determined by cytofluorimetry, passage 2 cells expressed MSC markers CD44 and CD90 and were negative for lineage-specific markers CD34 and CD45. The cells differentiated toward osteogenic, adipogenic, and chondrogenic directions. With therapeutic aims, 30 dogs (39 joints) suffering from elbow dysplasia (ED) and osteoarthritis (OA) were intra-articularly transplanted with allogeneic MSCs suspended in 0.5% hyaluronic acid (HA). A highly significant improvement was achieved without any medication as demonstrated by the degree of lameness during the follow-up period of 1 y. Control arthroscopy of 1 transplanted dog indicated that the cartilage had regenerated. Histological analysis of the cartilage biopsy confirmed that the regenerated cartilage was of hyaline type. These results demonstrate that transplantation of allogeneic adipose tissue-derived mesenchymal stem cells (AT-MSCs) is a novel, noninvasive, and highly effective therapeutic tool in treating canine elbow dysplasia. © 2017, Canadian Veterinary Medical Association. All rights reserved.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Kádár, Gabriella
AU  - Czibula, Ágnes
AU  - Szalay, Balázs
AU  - Nagy, K
AU  - Pusztai, A
AU  - Balog, Attila
AU  - Monostori, Éva
AU  - Vásárhelyi, Barna
AU  - Szekanecz, Z
AU  - Kovács, László
TI  - Predictors of disease course after the discontinuation of biologic therapy in Rheumatoid Arthritis patients with long-term
JF  - ANNALS OF THE RHEUMATIC DISEASES
J2  - ANN RHEUM DIS
VL  - 75
PY  - 2016
IS  - Suppl. 2
SP  - 1007
EP  - 1007
PG  - 1
SN  - 0003-4967
DO  - 10.1136/annrheumdis-2016-eular.5753
UR  - https://m2.mtmt.hu/api/publication/3117841
ID  - 3117841
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Kudlik, Gyöngyi
AU  - Hegyi, B
AU  - Czibula, Ágnes
AU  - Monostori, Éva
AU  - Buday, László
AU  - Uher, Ferenc
TI  - Mesenchymal stem cells promote macrophage polarization toward M2b-like cells.
JF  - EXPERIMENTAL CELL RESEARCH
J2  - EXP CELL RES
VL  - 348
PY  - 2016
IS  - 1
SP  - 36
EP  - 45
PG  - 10
SN  - 0014-4827
DO  - 10.1016/j.yexcr.2016.08.022
UR  - https://m2.mtmt.hu/api/publication/3115599
ID  - 3115599
N1  - Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary            
            Stem Cell Biology Unit, National Blood Service, Budapest, Hungary            
            Institute of Genetics, Biological Research Center of Hungarian Academy of Sciences, Szeged, Hungary            
            Cited By :17            
            Export Date: 10 February 2021            
            CODEN: ECREA            
            Correspondence Address: Uher, F.; National Blood Service, Karolina út 19-21., Hungary; email: uher.ferenc@gmail.com
AB  - Mesenchymal stem or stromal cells (MSCs) act on different components of the immune response including macrophages (MPhis). Therefore this study has been committed to explore how MSCs may modify the effect of MPhi polarization upon an inductive environment using mouse bone marrow (BM)-derived "naive", unpolarized MPhis. Phagocytosis of various MPhi subtypes was different since M1 and M2b showed poorer, while M2a higher rate of phagocytosis. MSCs significantly promoted yeast ingestion by M1 and M2b and diminished it by M2a cells. Under polarizing conditions, MSCs profoundly affected the TNFalpha production of MPhi subtypes since M1 and M2b MPhis produced less and M2a produced higher amount of TNFalpha while the amount of IL-10 was not affected. The most striking effect of MSCs was registered on M2b cells since the inflammatory TNFalpha dominance remarkably shifted to the immunosuppressive IL-10. Prepolarized M1 cells readily converted to M2a and M2b states when polarizing conditions changed from M1 to M2a or M2b induction, respectively. Repolarizing from M1 to M2a resulted in the decline of IL-10 and TNFalpha and defined elevation of Ym1 similar to levels characteristic to M2a primarily polarized from naive BM-MPhis. Similarly, polarization of M1 to M2b MPhis was successful showing increase in IL-10 and reduction in TNFalpha levels characteristic to M2b cells. However, when co-culturing with MSCs, M1-M2a or M1-M2b transition was not affected. Crosstalk between MPhis and MSCs depended on PGE-2 since COX-2 inhibition reduced the effect of MSCs to establish an IL-10-dominant cytokine production by MPhis.
LA  - English
DB  - MTMT
ER  -