TY - JOUR AU - Németh, Tamás AU - Balogh, Lili AU - Káposztás, Eszter Gertrúd AU - Szilveszter, Kata AU - Mócsai, Attila TI - Neutrophil-specific Syk expression is crucial for skin disease in experimental epidermolysis bullosa acquisita JF - JOURNAL OF INVESTIGATIVE DERMATOLOGY J2 - J INVEST DERMATOL VL - 143 PY - 2023 IS - 7 SP - 1147 EP - 1156 PG - 10 SN - 0022-202X DO - 10.1016/j.jid.2022.12.016 UR - https://m2.mtmt.hu/api/publication/33623361 ID - 33623361 LA - English DB - MTMT ER - TY - JOUR AU - Bátai, István Zoárd AU - Pápayné Sár, Cecília AU - Horváth, Ádám István AU - Borbély, Éva AU - Bölcskei, Kata AU - Kemény, Ágnes AU - Sándor, Zoltán AU - Nemes, Balázs AU - Helyes, Zsuzsanna AU - Perkecz, Anikó AU - Mócsai, Attila AU - Pozsgai, Gábor AU - Pintér, Erika TI - TRPA1 Ion Channel Determines Beneficial and Detrimental Effects of GYY4137 in Murine Serum-Transfer Arthritis JF - FRONTIERS IN PHARMACOLOGY J2 - FRONT PHARMACOL VL - 10 PY - 2019 PG - 15 SN - 1663-9812 DO - 10.3389/fphar.2019.00964 UR - https://m2.mtmt.hu/api/publication/30803235 ID - 30803235 N1 - * Megosztott szerzőség LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Ádám István AU - Botz, Bálint AU - Kiss, Tamas AU - Csekő, Kata AU - Kiss, Ibolya AU - Felinger, Attila AU - Szabados, Tamara AU - Kenyeres, Éva AU - Bencsik, Péter AU - Mócsai, Attila AU - Ferdinandy, Péter AU - Helyes, Zsuzsanna TI - Subantimicrobial Dose Doxycycline Worsens Chronic Arthritis-Induced Bone Microarchitectural Alterations in a Mouse Model: Role of Matrix Metalloproteinases? JF - FRONTIERS IN PHARMACOLOGY J2 - FRONT PHARMACOL VL - 10 PY - 2019 PG - 15 SN - 1663-9812 DO - 10.3389/fphar.2019.00233 UR - https://m2.mtmt.hu/api/publication/30620557 ID - 30620557 N1 - Export Date: 20 September 2023 Correspondence Address: Helyes, Z.; Department of Pharmacology and Pharmacotherapy, Hungary; email: zsuzsanna.helyes@aok.pte.hu AB - Background: Rheumatoid arthritis (RA) is a chronic inflammatory joint disease hallmarked by irreversible damage of cartilage and bone. Matrix metalloproteinases (MMPs) involved in connective tissue remodeling play an important role in this process. Numerous MMPs have been examined in humans and animals, but their functions are still not fully understood. Therefore, we investigated the role of MMPs in the K/BxN serum-transfer model of RA with the broad-spectrum MMP inhibitor subantimicrobial dose doxycycline (SDD) using complex in vivo and in vitro methodolgy. Methods: Chronic arthritis was induced by repetitive i.p. injections of K/BxN serum in C57BL/6J mice. SDD was administered daily in acidified drinking water (0.5 mg/mL, 80 mg/kg) during the 30 days experimental period. Mechanonociceptive threshold of the paw was evaluated by aesthesiometry, grasping ability by grid test, arthritis severity by scoring, neutrophil myeloperoxidase activity by luminescence, vascular hyperpermeability and MMP activity by fluorescence in vivo imaging and the latter also by gelatin zymography, bone structure by micro-computed tomography (micro-CT). Plasma concentrations of doxycycline were determined by liquid chromatography-mass spectrometry analysis. Results: K/BxN serum induced significant inflammatory signs, mechanical hyperalgesia, joint function impairment, increased myeloperoxidase activity and vascular hyperpermeability. Significant increase of MMP activity was also observed both in vivo and ex vivo with elevation of the 57-60, 75, and 92 kDa gelatinolytic isoforms in the arthritic ankle joints, but neither MMP activity nor any above described functional parameters were influenced by SDD. Most importantly, SDD significantly reduced bone mineral density in the distal tibia and enhanced the Euler number in the ankle. Arthritis-induced microarchitectural alterations demonstrating increased irregularity and cancellous bone remodeling, such as increased Euler number was significantly elevated by SDD in both regions. Conclusion: We showed increase of various MMP activities in the joints by in vivo fluorescence imaging together with ex vivo zymography, and investigated their functional significance using the broad-spectrum MMP inhibitor SDD in the translational RA model. This is the first demonstration that SDD worsens arthritis-induced bone microarchitectural alterations, but it appears to be independent of MMP inhibition. LA - English DB - MTMT ER - TY - JOUR AU - Csepregi, Janka Zsófia AU - Orosz, Anita AU - Zajta, Erik AU - Kása, Orsolya AU - Németh, Tamás AU - Simon, Edina AU - Fodor, Szabina AU - Csonka, Katalin AU - Barátki, Balázs Lajos AU - Kövesdi, Dorottya AU - He, You-Wen AU - Gácser, Attila AU - Mócsai, Attila TI - Myeloid-Specific Deletion of Mcl-1 Yields Severely Neutropenic Mice That Survive and Breed in Homozygous Form JF - JOURNAL OF IMMUNOLOGY J2 - J IMMUNOL VL - 201 ET - 0 PY - 2018 IS - 12 SP - 3793 EP - 3803 PG - 11 SN - 0022-1767 DO - 10.4049/jimmunol.1701803 UR - https://m2.mtmt.hu/api/publication/30349930 ID - 30349930 N1 - Janka Zsofia Csepregi and Anita Orosz contributed equally to this work AB - Mouse strains with specific deficiency of given hematopoietic lineages provide invaluable tools for understanding blood cell function in health and disease. Whereas neutrophils are dominant leukocytes in humans and mice, there are no widely useful genetic models of neutrophil deficiency in mice. In this study, we show that myeloid-specific deletion of the Mcl-1 antiapoptotic protein in Lyz2Cre/CreMcl1flox/flox (Mcl1ΔMyelo) mice leads to dramatic reduction of circulating and tissue neutrophil counts without affecting circulating lymphocyte, monocyte, or eosinophil numbers. Surprisingly, Mcl1ΔMyelo mice appeared normally, and their survival was mostly normal both under specific pathogen-free and conventional housing conditions. Mcl1ΔMyelo mice were also able to breed in homozygous form, making them highly useful for in vivo experimental studies. The functional relevance of neutropenia was confirmed by the complete protection of Mcl1ΔMyelo mice from arthritis development in the K/B×N serum-transfer model and from skin inflammation in an autoantibody-induced mouse model of epidermolysis bullosa acquisita. Mcl1ΔMyelo mice were also highly susceptible to systemic Staphylococcus aureus or Candida albicans infection, due to defective clearance of the invading pathogens. Although neutrophil-specific deletion of Mcl-1 in MRP8-CreMcl1flox/flox (Mcl1ΔPMN) mice also led to severe neutropenia, those mice showed an overt wasting phenotype and strongly reduced survival and breeding, limiting their use as an experimental model of neutrophil deficiency. Taken together, our results with the Mcl1ΔMyelo mice indicate that severe neutropenia does not abrogate the viability and fertility of mice, and they provide a useful genetic mouse model for the analysis of the role of neutrophils in health and disease. LA - English DB - MTMT ER - TY - JOUR AU - Wannick, M. AU - Bezdek, S. AU - Guillen, N. AU - Thieme, M. AU - Meshrkey, F. AU - Mousavi, S. AU - Seeling, M. AU - Nimmerjahn, F. AU - Mócsai, Attila AU - Zillikens, D. AU - Sezin, T. AU - Sadik, C.D. TI - Oral administration of the selective GPR120/FFA4 agonist compound A is not effective in alleviating tissue inflammation in mouse models of prototypical autoimmune diseases JF - PHARMACOLOGY RESEARCH AND PERSPECTIVES J2 - PHARMACOL RES PERSPECT VL - 6 ET - 0 PY - 2018 IS - 6 PG - 8 SN - 2052-1707 DO - 10.1002/prp2.438 UR - https://m2.mtmt.hu/api/publication/30331540 ID - 30331540 AB - ω3-polyunsaturated free fatty acids (ω3-PUFAs), particularly docosahexaenoic (DHA) and eicosapentaenoic acid (EPA), are thought to exert health promoting effects in metabolic and in inflammatory diseases. The molecular mechanisms of these beneficial effects are only partially understood. DHA and EPA activate Free Fatty Acid receptor 4 (GPR120/FFA4). Recently, the first orally available, synthetic ligand of FFA4, 3-[2-chloro-5-(trifluoromethoxy)phenyl]-3-azaspiro[5.5]undecane-9-acetic acid ("compound A"; cpd A) has been developed. Cpd A exhibits distinctly higher potency, efficiency, and selectivity at FFA4 than ω3-PUFAs and ameliorates insulin resistance and adipose tissue inflammation in the mouse. With GPR120/FFA4 activation believed to also attenuate tissue inflammation in autoimmune diseases, cpd A may also have a beneficial effect in these diseases. We have therefore addressed the therapeutic potential of cpd A in mouse models of three prototypical autoimmune diseases, specifically psoriasis, rheumatoid arthritis, and bullous pemphigoid. The effect of cpd A on the course of Aldara™-induced psoriasis-like dermatitis, K/BxN serum transfer arthritis, and antibody transfer pemphigoid disease-like dermatitis was scrutinized. Cpd A did not alter the course of Aldara-induced psoriasis-like dermatitis, K/BxN serum transfer arthritis, or antibody transfer pemphigoid disease-like dermatitis. Our results suggest that therapeutic regimens solely relying on FFA4 activation do not bear the potential to treat inflammatory diseases. With cpd A distinctly more potent in activating GPR120/FFA4 than ω3-PUFAs, this also suggests that GPR120/FFA4 activation by ω3-PUFAs does not significantly contribute to the health-promoting effects of ω3-PUFAs in autoimmune diseases. LA - English DB - MTMT ER - TY - JOUR AU - Goncalves-de-Albuquerque, CF AU - Rohwedder, I AU - Silva, AR AU - Ferreira, AS AU - Kurz, ARM AU - Cougoule, C AU - Klapproth, S AU - Eggersmann, T AU - Silva, JD AU - de Oliveira, GP AU - Capelozzi, VL AU - Schlesinger, GG AU - Costa, ER AU - Marins, RDEE AU - Mócsai, Attila AU - Maridonneau-Parini, I AU - Walzog, B AU - Rocco, PRM AU - Sperandio, M AU - de Castro-Faria, HC TI - The Yin and Yang of Tyrosine Kinase inhibition During experimental Polymicrobial sepsis JF - FRONTIERS IN IMMUNOLOGY J2 - FRONT IMMUNOL VL - 9 PY - 2018 PG - 16 SN - 1664-3224 DO - 10.3389/fimmu.2018.00901 UR - https://m2.mtmt.hu/api/publication/3375759 ID - 3375759 AB - Neutrophils are the first cells of our immune system to arrive at the site of inflammation. They release cytokines, e.g., chemokines, to attract further immune cells, but also actively start to phagocytose and kill pathogens. In the case of sepsis, this tightly regulated host defense mechanism can become uncontrolled and hyperactive resulting in severe organ damage. Currently, no effective therapy is available to fight sepsis; therefore, novel treatment targets that could prevent excessive inflammatory responses are warranted. Src Family tyrosine Kinases (SFK), a group of tyrosine kinases, have been shown to play a major role in regulating immune cell recruitment and host defense. Leukocytes with SFK depletion display severe spreading and migration defects along with reduced cytokine production. Thus, we investigated the effects of dasatinib, a tyrosine kinase inhibitor, with a strong inhibitory capacity on SFKs during sterile inflammation and polymicrobial sepsis in mice. We found that dasatinib-treated mice displayed diminished leukocyte adhesion and extravasation in tumor necrosis factor-alpha-stimulated cremaster muscle venules in vivo. In polymicrobial sepsis, sepsis severity, organ damage, and clinical outcome improved in a dose-dependent fashion pointing toward an optimal therapeutic window for dasatinib dosage during polymicrobial sepsis. Dasatinib treatment may, therefore, provide a balanced immune response by preventing an overshooting inflammatory reaction on the one side and bacterial overgrowth on the other side. LA - English DB - MTMT ER - TY - JOUR AU - Németh, Tamás AU - Futosi, Krisztina AU - Szilveszter, Kata AU - Vilinovszki, O AU - Kiss-Pápai, Levente AU - Mócsai, Attila TI - Lineage-specific analysis of Syk function in autoantibody-induced arthritis JF - FRONTIERS IN IMMUNOLOGY J2 - FRONT IMMUNOL VL - 9 PY - 2018 PG - 10 SN - 1664-3224 DO - 10.3389/fimmu.2018.00555 UR - https://m2.mtmt.hu/api/publication/3374084 ID - 3374084 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences [LP2013-66/2013]; Hungarian National Research, Development and Innovation Office [NVKP_16-2016-1-0039]; Hungarian Ministry of National Economy [VEKOP-2.3.2-16-2016-00002]; Janos Bolyai Research Scholarships of the Hungarian Academy of Sciences; Wellcome Trust International Senior Research Fellowship [087782] Funding text: We thank Edina Simon for expert technical assistance; Gabor Banhegyi for access to equipment; Diane Mathis, Christophe Benoist, Victor Tybulewicz, Emmanuelle Passegue, Axel Roers, and Alexander Tarakhovsky for transgenic animals. This work was supported by the Lendulet program of the Hungarian Academy of Sciences (LP2013-66/2013 to AM), the Hungarian National Research, Development and Innovation Office (NVKP_16-2016-1-0039 to AM), the Hungarian Ministry of National Economy (VEKOP-2.3.2-16-2016-00002 to AM), and the Janos Bolyai Research Scholarships of the Hungarian Academy of Sciences (to TN and KF). AM was a recipient of a Wellcome Trust International Senior Research Fellowship (Grant No. 087782). AB - Autoantibody production and autoantibody-mediated inflammation are hallmarks of a number of autoimmune diseases. The K/BxN serum-transfer arthritis is one of the most widely used models of the effector phase of autoantibody-induced pathology. Several hematopoietic lineages including neutrophils, platelets, and mast cells have been proposed to contribute to inflammation and tissue damage in this model. We have previously shown that the Syk tyrosine kinase is critically involved in the development in K/BxN serum-transfer arthritis and bone marrow chimeric experiments indicated that Syk is likely involved in one or more hematopoietic lineages during the disease course. The aim of the present study was to further define the lineage(s) in which Syk expression is required for autoantibody-induced arthritis. To this end, K/BxN serum-transfer arthritis was tested in conditional mutant mice in which Syk was deleted in a lineage-specific manner from neutrophils, platelets, or mast cells. Combination of the MRP8-Cre, PF4-Cre, or Mcpt5-Cre transgene with floxed Syk alleles allowed efficient and selective deletion of Syk from neutrophils, platelets, or mast cells, respectively. This has also been confirmed by defective Syk-dependent in vitro functional responses of the respective cell types. In vivo studies revealed nearly complete defect of the development of K/BxN serum-transfer arthritis upon neutrophil-specific deletion of Syk. By contrast, Syk deletion from platelets or mast cells did not affect the development of K/BxN serum-transfer arthritis. Our results indicate that autoantibody-induced arthritis requires Syk expression in neutrophils, whereas, contrary to prior assumptions, Syk expression in platelets or mast cells is dispensable for disease development in this model. © 2018 Németh, Futosi, Szilveszter, Vilinovszki, Kiss-Pápai and Mócsai. LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Ádám István AU - Tékus, Valéria AU - Bencze, Noémi AU - Szentes, Nikolett AU - Scheich, Bálint AU - Bölcskei, Kata AU - Szőke, Éva AU - Mócsai, Attila AU - Toth-Sarudy, E AU - Mátyus, Péter AU - Pintér, Erika AU - Helyes, Zsuzsanna TI - Analgesic effects of the novel semicarbazide-sensitive amine oxidase inhibitor SZV 1287 in mouse pain models with neuropathic mechanisms: involvement of transient receptor potential vanilloid 1 and ankyrin 1 receptors JF - PHARMACOLOGICAL RESEARCH J2 - PHARMACOL RES VL - 131 ET - 0 PY - 2018 SP - 231 EP - 243 PG - 13 SN - 1043-6618 DO - 10.1016/j.phrs.2018.02.006 UR - https://m2.mtmt.hu/api/publication/3334900 ID - 3334900 N1 - Funding Agency and Grant Number: National Brain Research Program [20017-1.2.1-NKP-2017-00002, OTKA-NN 114458]; New National Excellence Program of the Ministry of Human Capacities [UNKP-17-3-III-PTE-79]; Wellcome Trust [087782]; "Lendulet" program of the Hungarian Academy of Sciences [P2013-66/2013]; [GINOP-2.2.1-15-2016-00020]; [EFOP-3.6.1-16-2016-00004] Funding text: The research infrastructure was supported by GINOP-2.2.1-15-2016-00020 ("Development of a multi-targeting innovative analgesic drug: pharmacodynamics, preclinical and human phase I. studies"), EFOP-3.6.1-16-2016-00004 (Comprehensive development for implementing smart specialization strategies at the University of Pecs"), National Brain Research Program 20017-1.2.1-NKP-2017-00002 and OTKA-NN 114458. Adam Horvath was supported by the UNKP-17-3-III-PTE-79 New National Excellence Program of the Ministry of Human Capacities, Attila Mocsai was supported by the Wellcome Trust (087782) and the "Lendulet" program of the Hungarian Academy of Sciences (P2013-66/2013). AB - Semicarbazide-sensitive amine oxidase (SSAO) produces tissue irritants by deamination of primary amines, which activate transient receptor potential ankyrin 1 (TRPA1) and vanilloid 1 (TRPV1) receptors expressed predominantly on nociceptors. Since there are no data about its functions in pain, we studied the effects and mechanisms of action of our novel SSAO inhibitor and dual TRPA1/TRPV1 antagonist multi-target drug SZV 1287 in different pain models. Acute chemonociception was induced by TRPV1 and TRPA1 activation (resiniferatoxin and formalin, respectively), chronic arthritis by K/BxN serum transfer, traumatic mononeuropathy by sciatic nerve ligation. SZV 1287 (20mg/kg i.p.) was investigated in C57Bl/6J wildtype (WT), TRPA1- (TRPA1(-/-)) and TRPV1-deficient (TRPV1(-/-)) mice. Paw mechanonociception was measured by aesthesiometry, thermonociception by hot plate, nocifensive behavior by licking duration, volume by plethysmometry, myeloperoxidase activity by luminescence and plasma extravasation by fluorescence imaging, glia activation in pain-related brain regions by immunohistochemistry. SZV 1287 significantly inhibited both TRPA1 and TRPV1 activation-induced acute chemonociception and hyperalgesia. In K/BxN arthritis, daily SZV 1287 injections significantly decreased hyperalgesia, L4-L6 spinal dorsal horn microgliosis, edema and myeloperoxidase activity. SZV 1287-evoked antihyperalgesic and anti-edema effects were absent in TRPV1(-/-), and remarkably reduced in TRPA1(-/-) mice. In contrast, myeloperoxidase-inhibitory effect was absent in TRPA1(-/-,) but not in TRPV1(-/-) animals. Acute SZV 1287 administration resulted in approximately 50% significant reduction of neuropathic hyperalgesia 7days after nerve ligation, which was not observed in either TRPA1(-/-) or TRPV1(-/-) mice. SZV 1287 inhibits chronic inflammatory and neuropathic pain via TRPV1 and TRPA1/TRPV1 activation, respectively, highlighting its drug developmental potential. LA - English DB - MTMT ER - TY - JOUR AU - Németh, Tamás AU - Virtic, O AU - Sitaru, C AU - Mócsai, Attila TI - The Syk tyrosine kinase is required for skin inflammation in an in vivo mouse model of epidermolysis bullosa acquisita JF - JOURNAL OF INVESTIGATIVE DERMATOLOGY J2 - J INVEST DERMATOL VL - 137 PY - 2017 IS - 10 SP - 2131 EP - 2139 PG - 9 SN - 0022-202X DO - 10.1016/j.jid.2017.05.017 UR - https://m2.mtmt.hu/api/publication/3269267 ID - 3269267 N1 - Funding Agency and Grant Number: European Union's FP7 Cooperation Program [282095]; Lendulet program of the Hungarian Academy of Sciences [LP2013-66/2013]; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SI-1281/5-1]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; Wellcome Trust International Senior Research FellowshipWellcome Trust [087782] Funding text: We thank Edina Simon for expert technical assistance; Kinga Csorba, Levente Kiss-Papai, and Krisztina Futosi for help with experiments; Kitti Ajtay and Zoltan Jakus for the histological images; Gabor Banhegyi for access to equipment; and Clifford Lowell and Victor Tybulewicz for transgenic animals. This work was supported by the European Union's FP7 Cooperation Program (Project No. 282095 [TARKINAID] to AM and CS), the Lendulet program of the Hungarian Academy of Sciences (LP2013-66/2013 to AM), the Deutsche Forschungsgemeinschaft (SI-1281/5-1 to CS), and the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (to TN). AM was a recipient of a Wellcome Trust International Senior Research Fellowship (grant no. 087782). AB - The inflammatory form of epidermolysis bullosa acquisita is caused by autoantibodies against type VII collagen (C7), a component of the dermal-epidermal junction. We have previously shown that myeloid Src-family kinases mediate skin inflammation triggered by anti-C7 antibodies. Here we identify the Syk tyrosine kinase as a critical component of autoantibody-induced skin inflammation downstream of Src-family kinases. Immobilized C7-anti-C7 immune complexes triggered neutrophil activation and Syk phosphorylation in a Src-family kinase-dependent manner. Bone marrow chimeric mice lacking Syk in their hematopoietic compartment were completely protected from skin inflammation triggered by anti-C7 antibodies despite normal circulating anti-C7 levels. Syk deficiency abrogated the accumulation of CXCL2, IL-1beta and LTB4 at the site of inflammation and resulted in defective in vivo neutrophil recruitment. Syk-/- neutrophils had a normal intrinsic migratory capacity but failed to release CXCL2 or LTB4 upon activation by immobilized C7-anti-C7 immune complexes, indicating a role for Syk in the amplification of the inflammation process. These results identify Syk as a critical component of skin inflammation in a mouse model of epidermolysis bullosa acquisita and as a potential therapeutic target in epidermolysis bullosa acquisita and other mechanistically related inflammatory skin diseases such as bullous pemphigoid. LA - English DB - MTMT ER - TY - JOUR AU - Marton, Nikolett AU - Kovács, Orsolya Tünde AU - Baricza, Eszter AU - Kittel, Ágnes AU - Győri, Dávid Sándor AU - Mócsai, Attila AU - Meier, Florian M P AU - Goodyear, Carl S AU - McInnes, Iain B AU - Buzás, Edit Irén AU - Nagy, György TI - Extracellular vesicles regulate the human osteoclastogenesis: divergent roles in discrete inflammatory arthropathies JF - CELLULAR AND MOLECULAR LIFE SCIENCES J2 - CELL MOL LIFE SCI VL - 74 PY - 2017 IS - 19 SP - 3599 EP - 3611 PG - 13 SN - 1420-682X DO - 10.1007/s00018-017-2535-8 UR - https://m2.mtmt.hu/api/publication/3221690 ID - 3221690 N1 - Funding Agency and Grant Number: Hungarian Scientific Research Fund, OTKA-NKFIH [OTKA-NN111023, 11958]; MEDINPROT; BMBS COST Action [BM1202 ME HAD]; National Heart Program [OTKA 120237, NKFIA, KP-16-1-2016-0017] Funding text: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :8 Export Date: 2 August 2019 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :9 Export Date: 5 August 2019 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :9 Export Date: 7 August 2019 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :9 Export Date: 14 August 2019 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: BM1202 Funding details: Hungarian Scientific Research Fund, OTKA-NN111023 Funding details: 120237 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, KP-16-1-2016-0017 Funding details: 11958 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Funding Agency and Grant Number: Hungarian Scientific Research Fund, OTKA-NKFIH [OTKA-NN111023, 11958]; MEDINPROT; BMBS COST ActionEuropean Cooperation in Science and Technology (COST) [BM1202 ME HAD]; National Heart Program [OTKA 120237, NKFIA, KP-16-1-2016-0017] Funding text: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :13 Export Date: 11 March 2020 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding details: 11958 Funding details: OTKA 120237 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :13 Export Date: 31 May 2020 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding details: 11958 Funding details: OTKA 120237 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :13 Export Date: 1 June 2020 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding details: 11958 Funding details: OTKA 120237 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :13 Export Date: 13 June 2020 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :14 Export Date: 4 August 2020 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding details: 11958 Funding details: OTKA 120237 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :17 Export Date: 7 March 2021 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: OTKA 120237 Funding details: 11958 Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :17 Export Date: 21 April 2021 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: OTKA 120237 Funding details: 11958 Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, 1089, Hungary Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary MTA-SE “Lendület” Inflammation Physiology Research Group of the Hungarian Academy of Sciences and the Semmelweis University, Budapest, Hungary Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, United Kingdom Department of Rheumatology, 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary Cited By :20 Export Date: 7 September 2021 CODEN: CMLSF Correspondence Address: Nagy, G.; Department of Genetics, Nagyvárad tér 4, Hungary; email: gyorgyngy@gmail.com Chemicals/CAS: colony stimulating factor 1, 81627-83-0; osteoclast differentiation factor, 200145-93-3; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; TNFRSF11A protein, human Funding details: OTKA 120237 Funding details: 11958 Funding details: Hungarian Scientific Research Fund, OTKA, OTKA-NN111023 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, KP-16-1-2016-0017 Funding text 1: This work was supported by the Hungarian Scientific Research Fund OTKA-NN111023, OTKA-NKFIH #11958; MEDINPROT and BMBS COST Action BM1202 ME HAD. Funding was provided by National Heart Program (Grant Nos. OTKA 120237, NKFIA, and KP-16-1-2016-0017). AB - Extracellular vesicles (EVs) are subcellular signalosomes. Although characteristic EV production is associated with numerous physiological and pathological conditions, the effect of blood-derived EVs on bone homeostasis is unknown. Herein we evaluated the role of circulating EVs on human osteoclastogenesis. LA - English DB - MTMT ER -