TY - JOUR AU - Farkas, Sándor AU - Cioca, Daniel AU - Murányi, József AU - Hornyák, Péter AU - Brunyánszki, Attila AU - Szekér, Patrik AU - Boros, Eszter AU - Horváth, Patrik AU - Hujber, Zoltán AU - Rácz, Gábor Z. AU - Nagy, Noémi AU - Tóth, Rebeka AU - Nyitray, László AU - Péterfi, Zalán TI - Chlorotoxin binds to both matrix metalloproteinase 2 and neuropilin 1 JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 299 PY - 2023 IS - 9 PG - 16 SN - 0021-9258 DO - 10.1016/j.jbc.2023.104998 UR - https://m2.mtmt.hu/api/publication/34046199 ID - 34046199 LA - English DB - MTMT ER - TY - JOUR AU - Medgyaszai, Melinda AU - Péterfi, Zalán AU - Valkó, Anna TI - Lehetőségek és buktatók a SARS-CoV-2-antigén és az ellene termelt antitestek kimutatásában = Possibilities and pitfalls of virus antigen and antibody detection of SARS-CoV-2 JF - ORVOSI HETILAP J2 - ORV HETIL VL - 162 PY - 2021 IS - 15 SP - 563 EP - 570 PG - 8 SN - 0030-6002 DO - 10.1556/650.2021.32210 UR - https://m2.mtmt.hu/api/publication/31966884 ID - 31966884 AB - Összefoglaló. A koronavírus-betegség 2019 (COVID–19)-pandémia komoly kihívás elé állította nemcsak a mikrobiológiai laboratóriumokat, hanem az eredmények interpretálásában a klinikumban dolgozó kollégákat is. Az orvostudomány specializált világában az immunológiai és a fertőző betegségekkel kapcsolatos ismeretek az antimikrobás terápiás megoldások sikeressége, valamint a széles körű vakcináció miatt az idők folyamán számos szakterületen háttérbe szorultak, felfrissítésük sürgető és elengedhetetlen része a pandémiával való megküzdésnek. A diagnosztikai vizsgálatok fontos eszközei a járvány megfékezésének, illetve a betegek ellátásának, azonban a vírus és az emberi szervezet interakciójának megértése elengedhetetlenül szükséges a korrekt epidemiológiai és gyógyászati véleményalkotáshoz. Jelen cikkünk az orvosi gyakorlat számára foglalja össze a súlyos akut légzőszervi szindrómát okozó koronavírus-2 (SARS-CoV-2) kimutatására, valamint az immunrendszer specifikus immunválaszának szerológiai vizsgálatára irányuló, gyakorlatban használatos módszereket, azok helyét, szerepét és értékelésük szempontjait a tudomány jelen állása szerint. Orv Hetil. 2021; 162(15): 563–570. Summary. The coronavirus disease 2019 (COVID-19) pandemic posed a serious challenge not only for microbiology laboratories, but also for the clinicians in interpretation of the results. In the specialized world of medicine, knowledge of immunological and infectious diseases has been relegated to the background in many disciplines over time due to the success of antimicrobial therapies and widespread vaccination, so updating them is an urgent and essential part of the fight against the pandemic. Diagnostic tests are important tools for controlling the epidemic and caring for patients, but understanding the interaction between the virus and the human body is essential to form a correct epidemiological and medical opinion. This paper summarizes the medical methods for the detection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the serological testing of the specific immune response of the immune system, their place, role and criteria of their evaluation according to current scientific knowledge. Orv Hetil. 2021; 162(15): 563–570. LA - Hungarian DB - MTMT ER - TY - JOUR AU - Zana, Melinda AU - Péterfi, Zalán AU - Kovács, Hajnal Anna AU - Tóth, Zsuzsanna AU - Enyedi, Balázs AU - Morel, F AU - Paclet, MH AU - Donkó, Ágnes AU - Morand, S AU - Leto, TL AU - Geiszt, Miklós TI - Interaction between p22(phox) and Nox4 in the endoplasmic reticulum suggests a unique mechanism of NADPH oxidase complex formation. JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 116 PY - 2018 SP - 41 EP - 49 PG - 9 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2017.12.031 UR - https://m2.mtmt.hu/api/publication/3324695 ID - 3324695 N1 - Department of Physiology, Faculty of Medicine, Semmelweis University, Budapest, Hungary ”Momentum” Peroxidase Enzyme Research Group of the Semmelweis University and the Hungarian Academy of Sciences, Budapest, Hungary Department of Anatomy, Histology and Embryology, Semmelweis University, Budapest, Hungary GREPI AGIM FRE CNRS 3405, Joseph Fourier University Grenoble France, EFS Rhône-Alpes, France Laboratory of Host Defenses, NIAID, NIH, United States L′Oreal Biotechnologies Research Laboratory, Aulnay-Sous-Bois, France Cited By :22 Export Date: 9 August 2022 CODEN: FRBME Correspondence Address: Geiszt, M.; Department of Physiology, PO Box 259, Hungary; email: geiszt.miklos@med.semmelweis-univ.hu Chemicals/CAS: dual oxidase; reduced nicotinamide adenine dinucleotide phosphate oxidase, 9032-22-8; cytochrome b, 9035-37-4; hydrogen peroxide, 7722-84-1; rapamycin, 53123-88-9; Cytochrome b Group; Hydrogen Peroxide; Multiprotein Complexes; NADPH Oxidase 4; NADPH Oxidases; Nox4 protein, mouse; p22(phox) protein, mouse; Reactive Oxygen Species; Sirolimus; Transforming Growth Factor beta1 Funding details: National Institute of Allergy and Infectious Diseases, NIAID, ZIAAI000614 Funding details: Hungarian Scientific Research Fund, OTKA, K106138, K119955 Funding details: Magyar Tudományos Akadémia, MTA, LP2011-001 Funding text 1: We are grateful to Beáta Molnár and Katalin Meczker for technical assistance. This work was supported by the Hungarian Research Fund (OTKA K106138 and K119955 ). This work was also supported by “Momentum” grant from the Hungarian Academy of Sciences ( LP2011-001 ). AB - The p22(phox) protein is an essential component of the phagocytic- and inner ear NADPH oxidases but its relationship to other Nox proteins is less clear. We have studied the role of p22(phox) in the TGF-beta1-stimulated H2O2 production of primary human and murine fibroblasts. TGF-beta1 induced H2O2 release of the examined cells, and the response was dependent on the expression of both Nox4 and p22(phox). Interestingly, the p22(phox) protein was present in the absence of any detectable Nox/Duox expression, and the p22(phox) level was unaffected by TGF-beta1. On the other hand, Nox4 expression was dependent on the presence of p22(phox), establishing an asymmetrical relationship between the two proteins. Nox4 and p22(phox) proteins localized to the endoplasmic reticulum and their distribution was unaffected by TGF-beta1. We used a chemically induced protein dimerization method to study the orientation of p22(phox) and Nox4 in the endoplasmic reticulum membrane. This technique is based on the rapamycin-mediated heterodimerization of the mammalian FRB domain with the FK506 binding protein. The results of these experiments suggest that the enzyme complex produces H2O2 into the lumen of the endoplasmic reticulum, indicating that Nox4 contributes to the development of the oxidative milieu within this organelle. LA - English DB - MTMT ER - TY - JOUR AU - Lázár, Enikő AU - Péterfi, Zalán AU - Sirokmány, Gábor AU - Kovács, Hajnal Anna AU - Klement, Éva AU - Medzihradszky F., Katalin AU - Geiszt, Miklós TI - Structure-function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 83 PY - 2015 SP - 273 EP - 282 PG - 10 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2015.02.015 UR - https://m2.mtmt.hu/api/publication/2891430 ID - 2891430 AB - Basement membranes provide structural support and convey regulatory signals to cells in diverse tissues. Assembly of collagen IV into a sheet-like network is a fundamental mechanism during the formation of basement membranes. Peroxidasin (PXDN) was recently described to catalyze crosslinking of collagen IV through the formation of sulfilimine bonds. Despite the significance of this pathway in tissue genesis, our understanding of PXDN function is far from complete. In this work we demonstrate that collagen IV crosslinking is a physiological function of mammalian PXDN. Moreover, we carried out structure-function analysis of PXDN to gain a better insight into its role in collagen IV synthesis. We identify conserved cysteines in PXDN that mediate the oligomerization of the protein into a trimeric complex. We also demonstrate that oligomerization is not an absolute requirement for enzymatic activity, but optimal collagen IV coupling is only catalyzed by the PXDN trimers. Localization experiments of different PXDN mutants in two different cell models revealed that PXDN oligomers, but not monomers, adhere on the cell surface in "hot spots," which represent previously unknown locations of collagen IV crosslinking. ©2015 Published by Elsevier Inc. LA - English DB - MTMT ER - TY - JOUR AU - Péterfi, Zalán AU - Geiszt, Miklós TI - Peroxidasins: novel players in tissue genesis JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI VL - 39 PY - 2014 IS - 7 SP - 305 EP - 307 PG - 3 SN - 0968-0004 DO - 10.1016/j.tibs.2014.05.005 UR - https://m2.mtmt.hu/api/publication/2706633 ID - 2706633 AB - Stabilization of extracellular matrix by protein crosslinking is a universal and essential process in multicellular organisms. Recent findings revealed that peroxidasin, a unique heme-peroxidase, produces hypohalides to support matrix synthesis. Unexpectedly, the highly reactive and potentially damaging hypohalides mediate the formation of sulfilimine bonds between adjacent collagen IV protomers. This crosslink is a fundamental feature of basal membranes, defining peroxidasin-dependent oxidant generation and sulfilimine crosslink formation as an elemental mechanism of tissue biogenesis. © 2014 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Péterfi, Zalán AU - Tóth, Zsuzsanna AU - Kovács, Hajnal Anna AU - Lázár, Enikő AU - Sum, A AU - Donkó, Ágnes AU - Sirokmány, Gábor AU - Shah, AM AU - Geiszt, Miklós TI - Peroxidasin-like protein: A novel peroxidase homologue in the human heart JF - CARDIOVASCULAR RESEARCH J2 - CARDIOVASC RES VL - 101 PY - 2014 IS - 3 SP - 393 EP - 399 PG - 7 SN - 0008-6363 DO - 10.1093/cvr/cvt256 UR - https://m2.mtmt.hu/api/publication/2553231 ID - 2553231 AB - AimsPeroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the expression and function of peroxidasin-like protein (PXDNL), a previously unknown peroxidase homologue.Methods and resultsWe cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.ConclusionPXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function. © 2013 The Author. LA - English DB - MTMT ER - TY - THES AU - Péterfi, Zalán TI - Új molekulák és jelátviteli folyamatok fibrotikus elváltozásokban PY - 2013 DO - 10.14753/SE.2013.1798 UR - https://m2.mtmt.hu/api/publication/2786895 ID - 2786895 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Fekete, Anna AU - Bőgel, Gábor AU - Pesti, Szabolcs AU - Péterfi, Zalán AU - Geiszt, Miklós AU - Buday, László TI - EGF regulates tyrosine phosphorylation and membrane-translocation of the scaffold protein Tks5 JF - JOURNAL OF MOLECULAR SIGNALING J2 - JOURNAL OF MOLECULAR SIGNALING VL - 8 PY - 2013 PG - 8 SN - 1750-2187 DO - 10.1186/1750-2187-8-8 UR - https://m2.mtmt.hu/api/publication/2397639 ID - 2397639 AB - Background: Tks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells. Recent data have suggested that a close homologue of Tks5, Tks4, is implicated in the EGF signaling.Results: Here, we report that Tks5 is a component of the EGF signaling pathway. In EGF-treated cells, Tks5 is tyrosine phosphorylated within minutes and the level of phosphorylation is sustained for at least 2 hours. Using specific kinase inhibitors, we demonstrate that tyrosine phosphorylation of Tks5 is catalyzed by Src tyrosine kinase. We show that treatment of cells with EGF results in plasma membrane translocation of Tks5. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutation of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks5.Conclusions: Our results identify Tks5 as a novel component of the EGF signaling pathway. © 2013 Fekete et al.; licensee BioMed Central Ltd. LA - English DB - MTMT ER - TY - JOUR AU - Lányi, Árpád AU - Barath, M AU - Péterfi, Zalán AU - Bőgel, Gábor AU - Orient, Anna AU - Simon, Tünde AU - Petrovszki, E AU - Kis-Tóth, Katalin AU - Sirokmány, Gábor AU - Rajnavölgyi, Éva AU - Terhorst, C AU - Buday, László AU - Geiszt, Miklós TI - The Homolog of the Five SH3-Domain Protein (HOFI/SH3PXD2B) Regulates Lamellipodia Formation and Cell Spreading JF - PLOS ONE J2 - PLOS ONE VL - 6 PY - 2011 IS - 8 PG - 14 SN - 1932-6203 DO - 10.1371/journal.pone.0023653 UR - https://m2.mtmt.hu/api/publication/1721813 ID - 1721813 N1 - Megjegyzés-21586556 : FN Thomson Reuters Web of Knowledge WC: Biology; Multidisciplinary Sciences Megjegyzés-21995193 : FN Thomson Reuters Web of Knowledge WC: Biology Megjegyzés-21931668 Chemicals/CAS: epidermal growth factor, 62229-50-9; protein tyrosine kinase, 80449-02-1 AB - Motility of normal and transformed cells within and across tissues requires specialized subcellular structures, e. g. membrane ruffles, lamellipodia and podosomes, which are generated by dynamic rearrangements of the actin cytoskeleton. Because the formation of these sub-cellular structures is complex and relatively poorly understood, we evaluated the role of the adapter protein SH3PXD2B [HOFI, fad49, Tks4], which plays a role in the development of the eye, skeleton and adipose tissue. Surprisingly, we find that SH3PXD2B is requisite for the development of EGF-induced membrane ruffles and lamellipodia, as well as for efficient cellular attachment and spreading of HeLa cells. Furthermore, SH3PXD2B is present in a complex with the non-receptor protein tyrosine kinase Src, phosphorylated by Src, which is consistent with SH3PXD2B accumulating in Src-induced podosomes. Furthermore, SH3PXD2B closely follows the subcellular relocalization of cortactin to Src-induced podosomes, EGF-induced membrane ruffles and lamellipodia. Because SH3PXD2B also forms a complex with the C-terminal region of cortactin, we propose that SH3PXD2B is a scaffold protein that plays a key role in regulating the actin cytoskeleton via Src and cortactin. LA - English DB - MTMT ER - TY - JOUR AU - Donkó, Ágnes AU - Ruisanchez, Éva AU - Orient, Anna AU - Enyedi, Balázs AU - Kapui, Réka AU - Péterfi, Zalán AU - de Deken, X AU - Benyó, Zoltán AU - Geiszt, Miklós TI - Urothelial cells produce hydrogen peroxide through the activation of Duox1 JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 49 PY - 2010 IS - 12 SP - 2040 EP - 2048 PG - 9 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2010.09.027 UR - https://m2.mtmt.hu/api/publication/1468050 ID - 1468050 LA - English DB - MTMT ER -