TY - JOUR AU - Bitay, Enikő AU - Pilbat, Ana Maria AU - Indrea, Emil AU - Kacso, Iren AU - Mate, Marton AU - Gergely, Attila Levente AU - Veress, Erzsebet TI - INFLUENCE OF THE BALL MILLING PROCESS AND AIR SINTERING CONDITIONS ON THE SYNTHESIS OF La0.7Sr0.3MnO3 CERAMICS JF - STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA J2 - STUD UNIV BABES-BOLYAI CHEM VL - 64 PY - 2019 IS - 2 SP - 447 EP - 456 PG - 10 SN - 1224-7154 DO - 10.24193/subbchem.2019.2.38 UR - https://m2.mtmt.hu/api/publication/30807719 ID - 30807719 N1 - Part number: 2 AB - Conventional solid-state synthesis was used to produce mixed valence manganite La0.7Ca0.3MnO3 (LCMO) from the mechanochemically activated mixture of the corresponding metal oxides. Prepared samples were characterized by XRD and SEM measurements. The results showed that it is possible to produce single phase LCMO perovskite after at least 2h of ball milling of the reaction mixture, followed by 1400 degrees C sintering of the dry-pressed sample pellets. The prolonged milling time as well as the higher sintering temperature leads to further stabilization of crystal structure. LA - English DB - MTMT ER - TY - JOUR AU - Mészáros, Mária AU - Porkoláb, Gergő AU - Kiss, Lóránd AU - Pilbat, Ana Maria AU - Kóta, Zoltán AU - Kupihár, Zoltán AU - Kéri, Albert AU - Galbács, Gábor AU - Siklós, László AU - Tóth, András AU - Fülöp, Lívia AU - Czirjákné Csete, Mária AU - Sipos, Áron AU - Hulper, P AU - Sipos, Péter AU - Páli, Tibor AU - Rákhely, Gábor AU - Révész, Piroska AU - Deli, Mária Anna AU - Veszelka, Szilvia TI - Niosomes decorated with dual ligands targeting brain endothelial transporters increase cargo penetration across the blood-brain barrier JF - EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES J2 - EUR J PHARM SCI VL - 123 ET - 0 PY - 2018 SP - 228 EP - 240 PG - 13 SN - 0928-0987 DO - 10.1016/j.ejps.2018.07.042 UR - https://m2.mtmt.hu/api/publication/3399566 ID - 3399566 AB - Nanoparticles targeting transporters of the blood-brain barrier (BBB) are promising candidates to increase the brain penetration of biopharmacons. Solute carriers (SLC) are expressed at high levels in brain endothelial cells and show a specific pattern at the BBB. The aim of our study was to test glutathione and ligands of SLC transporters as single or dual BBB targeting molecules for nanovesicles. High mRNA expression levels for hexose and neutral amino acid transporting SLCs were found in isolated rat brain microvessels and our rat primary cell based co-culture BBB model. Niosomes were derivatized with glutathione and SLC ligands glucopyranose and alanine. Serum albumin complexed with Evans blue (67kDa), which has a very low BBB penetration, was selected as a cargo. The presence of targeting ligands on niosomes, especially dual labeling, increased the uptake of the cargo molecule in cultured brain endothelial cells. This cellular uptake was temperature dependent and could be decreased with a metabolic inhibitor and endocytosis blockers filipin and cytochalasin D. Making the negative surface charge of brain endothelial cells more positive with a cationic lipid or digesting the glycocalyx with neuraminidase elevated the uptake of the cargo after treatment with targeted nanocarriers. Treatment with niosomes increased plasma membrane fluidity, suggesting the fusion of nanovesicles with endothelial cell membranes. Targeting ligands elevated the permeability of the cargo across the BBB in the culture model and in mice, and dual-ligand decoration of niosomes was more effective than single ligand labeling. Our data indicate that dual labeling with ligands of multiple SLC transporters can potentially be exploited for BBB targeting of nanoparticles. LA - English DB - MTMT ER - TY - JOUR AU - Glatz, Attila AU - Pilbat, Ana Maria AU - Nemeth, GL AU - Kontár, Katalin AU - Jósvay, Katalin AU - Hunya, Ákos AU - Udvardy, Andor AU - Gombos, Imre AU - Péter, Mária AU - Balogh, Gábor AU - Horváth, Ibolya AU - Vigh, László AU - Török, Zsolt TI - Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe. JF - CELL STRESS & CHAPERONES J2 - CELL STRESS CHAPERON VL - 21 PY - 2016 IS - 2 SP - 327 EP - 338 PG - 12 SN - 1355-8145 DO - 10.1007/s12192-015-0662-4 UR - https://m2.mtmt.hu/api/publication/2990307 ID - 2990307 N1 - Export Date: 20 June 2019 CODEN: CSCHF Cited By :24 Export Date: 27 May 2021 CODEN: CSCHF Correspondence Address: Török, Z.; Institute of Biochemistry, Hungary; email: torok.zsolt@brc.mta.hu AB - Changes in the levels of three structurally and functionally different important thermoprotectant molecules, namely small heat shock proteins (sHsps), trehalose, and lipids, have been investigated upon heat shock in Schizosaccharomyces pombe. Both alpha-crystallin-type sHsps (Hsp15.8 and Hsp16) were induced after prolonged high-temperature treatment but with different kinetic profiles. The shsp null mutants display a weak, but significant, heat sensitivity indicating their importance in the thermal stress management. The heat induction of sHsps is different in wild type and in highly heat-sensitive trehalose-deficient (tps1Delta) cells; however, trehalose level did not show significant alteration in shsp mutants. The altered timing of trehalose accumulation and induction of sHsps suggest that the disaccharide might provide protection at the early stage of the heat stress while elevated amount of sHsps are required at the later phase. The cellular lipid compositions of two different temperature-adapted wild-type S. pombe cells are also altered according to the rule of homeoviscous adaptation, indicating their crucial role in adapting to the environmental temperature changes. Both Hsp15.8 and Hsp16 are able to bind to different lipids isolated from S. pombe, whose interaction might provide a powerful protection against heat-induced damages of the membranes. Our data suggest that all the three investigated thermoprotectant macromolecules play a pivotal role during the thermal stress management in the fission yeast. LA - English DB - MTMT ER - TY - JOUR AU - Lénárt, Nikolett AU - Walter, Fruzsina AU - Bocsik, Alexandra AU - Sántha, Petra AU - Tóth, Erzsébet Melinda AU - Harazin, András AU - Tóth, Andrea AU - Vizler, Csaba AU - Török, Zsolt AU - Pilbat, Ana Maria AU - Vigh, László AU - Puskás, László AU - Sántha, Miklós AU - Deli, Mária Anna TI - Cultured cells of the blood-brain barrier from apolipoprotein B-100 transgenic mice: effects of oxidized low-density lipoprotein treatment JF - FLUIDS AND BARRIERS OF THE CNS J2 - FLUIDS BARRIERS CNS VL - 12 PY - 2015 PG - 16 SN - 2045-8118 DO - 10.1186/s12987-015-0013-y UR - https://m2.mtmt.hu/api/publication/2920970 ID - 2920970 LA - English DB - MTMT ER - TY - JOUR AU - Kiss, Lóránd AU - Virághné Hellinger, Éva AU - Pilbat, Ana Maria AU - Kittel, Ágnes AU - Török, Zsolt AU - Füredi, András AU - Szakács, Gergely AU - Veszelka, Szilvia AU - Sipos, Péter AU - Ózsvári, B AU - Puskás, László AU - Vastag, M AU - Révész, Piroska AU - Deli, Mária Anna TI - Sucrose esters increase drug penetration, but do not inhibit P-glycoprotein in Caco-2 intestinal epithelial cells JF - JOURNAL OF PHARMACEUTICAL SCIENCES J2 - J PHARM SCI VL - 103 PY - 2014 IS - 10 SP - 3107 EP - 3119 PG - 13 SN - 0022-3549 DO - 10.1002/jps.24085 UR - https://m2.mtmt.hu/api/publication/2709800 ID - 2709800 AB - Sucrose fatty acid esters are increasingly used as excipients in pharmaceutical products, but few data are available on their toxicity profile, mode of action, and efficacy on intestinal epithelial models. Three water-soluble sucrose esters, palmitate (P-1695), myristate (M-1695), laurate (D-1216), and two reference absorption enhancers, Tween 80 and Cremophor RH40, were tested on Caco-2 cells. Caco-2 monolayers formed a good barrier as reflected by high transepithelial resistance and positive immunostaining for junctional proteins claudin-1, ZO-1, and -catenin. Sucrose esters in nontoxic concentrations significantly reduced resistance and impedance, and increased permeability for atenolol, fluorescein, vinblastine, and rhodamine 123 in Caco-2 monolayers. No visible opening of the tight junctions was induced by sucrose esters assessed by immunohistochemistry and electron microscopy, but some alterations were seen in the structure of filamentous actin microfilaments. Sucrose esters fluidized the plasma membrane and enhanced the accumulation of efflux transporter ligands rhodamine 123 and calcein AM in epithelial cells, but did not inhibit the P-glycoprotein (P- gp)-mediated calcein AM accumulation in MES-SA/Dx5 cell line. These data indicate that in addition to their dissolution-increasing properties sucrose esters can enhance drug permeability through both the transcellular and paracellular routes without inhibiting P- LA - English DB - MTMT ER - TY - CHAP AU - Török, Zsolt AU - Pilbat, Ana Maria AU - Gombos, Imre AU - Hocsák, Enikő AU - Sümegi, Balázs AU - Horváth, Ibolya AU - Vigh, László ED - Henderson, B ED - Pockley, AG TI - Evidence on cholesterol-controlled lipid raft interaction of the small heat shock protein Hspb11. Chapter 5 TS - Chapter 5 T2 - Cellular Trafficking of Cell Stress Proteins in Health and Disease PB - Springer Netherlands CY - Dordrecht SN - 9789400747395 PY - 2012 SP - 75 EP - 86 PG - 12 DO - 10.1007/978-94-007-4740-1_5 UR - https://m2.mtmt.hu/api/publication/2192976 ID - 2192976 LA - English DB - MTMT ER - TY - JOUR AU - Gombos, Imre AU - Crul, Tim AU - Piotto, S AU - Güngör, Burcin AU - Török, Zsolt AU - Balogh, Gábor AU - Péter, Mária AU - Slotte, JP AU - Campana, F AU - Pilbat, Ana Maria AU - Hunya, Ákos AU - Crul-Tóth, Noémi AU - Literáti-Nagy, Zsuzsanna AU - Vígh, László Jr. AU - Glatz, Attila AU - Brameshuber, M AU - Schutz, GJ AU - Hevener, A AU - Febbraio, MA AU - Horváth, Ibolya AU - Vigh, László TI - Membrane-Lipid Therapy in Operation: The HSP Co-Inducer BGP-15 Activates Stress Signal Transduction Pathways by Remodeling Plasma Membrane Rafts. JF - PLOS ONE J2 - PLOS ONE VL - 6 PY - 2011 IS - 12 PG - 10 SN - 1932-6203 DO - 10.1371/journal.pone.0028818 UR - https://m2.mtmt.hu/api/publication/1921996 ID - 1921996 N1 - Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary Department of Pharmaceutical and Biomedical Sciences, University of Salerno, Salerno, Italy Department of Biosciences, Abo Akademi University, Turku, Finland LipidArt Ltd, Szeged, Hungary Institute of Applied Physics, Vienna University of Technology, Vienna, Austria Department of Medicine, Division of Endocrinology, University of California, Los Angeles, Los Angeles, CA, United States Cellular and Molecular Metabolism Laboratory, Baker Heart and Diabetes Institute, Prahran, VIC, Australia Cited By :58 Export Date: 26 May 2022 Correspondence Address: Vígh, L.; Institute of Biochemistry, , Szeged, Hungary; email: vigh@brc.hu Chemicals/CAS: cholesterol, 57-88-5; o (2 hydroxy 3 piperidinopropyl)nicotinic amidoxime, 66611-37-8; beta cyclodextrin, 7585-39-9; BGP 15; Cholesterol, 57-88-5; Green Fluorescent Proteins, 147336-22-9; Heat-Shock Proteins; Membrane Lipids; Oximes; Piperidines; beta-Cyclodextrins; betadex, 7585-39-9; rac1 GTP-Binding Protein, 3.6.5.2 Tradenames: bgp 15, N Gene Research, Hungary Manufacturers: N Gene Research, Hungary AB - Aging and pathophysiological conditions are linked to membrane changes which modulate membrane-controlled molecular switches, causing dysregulated heat shock protein (HSP) expression. HSP co-inducer hydroxylamines such as BGP-15 provide advanced therapeutic candidates for many diseases since they preferentially affect stressed cells and are unlikely have major side effects. In the present study in vitro molecular dynamic simulation, experiments with lipid monolayers and in vivo ultrasensitive fluorescence microscopy showed that BGP-15 alters the organization of cholesterol-rich membrane domains. Imaging of nanoscopic long-lived platforms using the raft marker glycosylphosphatidylinositol-anchored monomeric green fluorescent protein diffusing in the live Chinese hamster ovary (CHO) cell plasma membrane demonstrated that BGP-15 prevents the transient structural disintegration of rafts induced by fever-type heat stress. Moreover, BGP-15 was able to remodel cholesterol-enriched lipid platforms reminiscent of those observed earlier following non-lethal heat priming or membrane stress, and were shown to be obligate for the generation and transmission of stress signals. BGP-15 activation of HSP expression in B16-F10 mouse melanoma cells involves the Rac1 signaling cascade in accordance with the previous observation that cholesterol affects the targeting of Rac1 to membranes. Finally, in a human embryonic kidney cell line we demonstrate that BGP-15 is able to inhibit the rapid heat shock factor 1 (HSF1) acetylation monitored during the early phase of heat stress, thereby promoting a prolonged duration of HSF1 binding to heat shock elements. Taken together, our results indicate that BGP-15 has the potential to become a new class of pharmaceuticals for use in 'membrane-lipid therapy' to combat many various protein-misfolding diseases associated with aging. LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Krisztina AU - Pilbat, Ana Maria AU - Groma, Géza AU - Szalontai, Balázs AU - Cuisinier, FJG TI - Casein Aggregates Built Step-by-Step on Charged Polyelectrolyte Film Surfaces Are Calcium Phosphate-cemented JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 285 PY - 2010 IS - 50 SP - 38811 EP - 38817 PG - 7 SN - 0021-9258 DO - 10.1074/jbc.M110.151167 UR - https://m2.mtmt.hu/api/publication/1921483 ID - 1921483 AB - The possible mechanism of casein aggregation and micelle buildup was studied in a new approach by letting alpha-casein adsorb from low concentration (0.1 mg.ml(-1)) solutions onto the charged surfaces of polyelectrolyte films. It was found that alpha-casein could adsorb onto both positively and negatively charged surfaces. However, only when its negative phosphoseryl clusters remained free, i.e. when it adsorbed onto a negative surface, could calcium phosphate (CaP) nanoclusters bind to the casein molecules. Once the CaP clusters were in place, step-by-step building of multilayered casein architectures became possible. The presence of CaP was essential; neither Ca2+ nor phosphate could alone facilitate casein aggregation. Thus, it seems that CaP is the organizing motive in the casein micelle formation. Atomic force microscopy revealed that even a single adsorbed casein layer was composed of very small (in the range of tens of nanometers) spherical forms. The stiffness of the adsorbed casein layer largely increased in the presence of CaP. On this basis, we can imagine that casein micelles emerge according to the following scheme. The amphipathic casein monomers aggregate into oligomers via hydrophobic interactions even in the absence of CaP. Full scale, CaP-carrying micelles could materialize by interlocking these casein oligomers with CaP nanoclusters. Such a mechanism would not contradict former experimental results and could offer a synthesis between the submicelle and the block copolymer models of casein micelles. LA - English DB - MTMT ER - TY - THES AU - Pilbat, Ana Maria TI - Poly-(amino-acid) Polyelectrolyte Films: Structure and Interactions with Proteins and Lipids PB - Szegedi Tudományegyetem (SZTE) PY - 2009 SP - 48 UR - https://m2.mtmt.hu/api/publication/1918196 ID - 1918196 LA - English DB - MTMT ER - TY - JOUR AU - Pilbat, Ana Maria AU - Szegletes, Zsolt AU - Kóta, Zoltán AU - Ball, V AU - Schaaf, P AU - Voegel, JC AU - Szalontai, Balázs TI - Phospholipid Bilayers as Biomembrane-like Barriers in Layer-by-layer Polyelectrolyte Films JF - LANGMUIR J2 - LANGMUIR VL - 23 PY - 2007 IS - 15 SP - 8236 EP - 8242 PG - 7 SN - 0743-7463 DO - 10.1021/la700839p UR - https://m2.mtmt.hu/api/publication/1915118 ID - 1915118 LA - English DB - MTMT ER -