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1.

001-es BibID:BIBFORM014283
Első szerző:Bai Péter (biokémikus)
Cím:Partial protection by poly(ADP-ribose) polymerase inhibitors from nitroxyl-induced cytotoxity in thymocytes / Bai Péter, Bakondi Edina, Szabó Éva, Gergely Pál, Szabo Csaba, Virág László
Dátum:2001
ISSN:0891-5849 (Print)
Megjegyzések:Nitroxyl (NO(-)/HNO), has been proposed to be one of the NO(*)-derived cytotoxic species. Although the biological effect of nitroxyl is largely unknown, it has been reported to cause DNA breakage and cytotoxicity. We have therefore investigated whether NO(-)/HNO-induced DNA single-strand breakage activates the nuclear nick sensor enzyme poly(ADP-ribose) polymerase (PARP) and whether PARP activation affects the mode of NO(-)/HNO- induced cell death. NO(-)/HNO generated from Angeli's salt (AS, sodium trioxodinitrate) (0-300 microM) induced DNA single-strand breakage, PARP activation, and a concentration-dependent cytotoxicity in murine thymocytes. AS-induced cell death was also accompanied by decreased mitochondrial membrane potential and increased secondary superoxide production. The cytotoxicity of AS, as measured by propidium iodide uptake, was abolished by electron acceptors potassium ferricyanide, TEMPOL, the intracellular calcium chelator BAPTA-AM, and by PARP inhibitors 3-aminobenzamide (3-AB) and PJ-34. The cytoprotective effect of 3-AB was paralleled by increased output of AS-induced apoptotic parameters such as phosphatidylserine exposure, caspase activation, and DNA fragmentation. No significant increase in tyrosine nitration could be observed in AS-treated thymocytes as opposed to peroxynitrite-treated cells, indicating that tyrosine nitration is not likely to contribute to NO(-)/HNO-induced cytotoxicity. Our results demonstrate that NO(-)/HNO-induced PARP activation shifts the default apoptotic cell death toward necrosis in thymocytes. However, as total PARP inhibition resulted only in 30% cytoprotection, PARP-independent mechanisms dominate NO(-)/HNO-induced cytotoxicity in thymocytes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
egyetemen (Magyarországon) készült közlemény
Apoptosis
Benzamides/ pharmacology
Caspases/metabolism
Cells, Cultured
DNA Damage/drug effects
DNA Fragmentation/drug effects
Enzyme Activation/drug effects/physiology
Enzyme Inhibitors/ pharmacology
Male
Mice
Mice, Inbred C57BL
Mitochondria/ drug effects
Nitrates
Nitrites/toxicity
Nitrogen Oxides/ toxicity
Poly(ADP-ribose) Polymerases/ antagonists & inhibitors/metabolism
Protective Agents/ pharmacology
Thymus Gland/cytology/ drug effects
Tyrosine
Megjelenés:Free radical biology and medicine. - 31 : 12 (2001), p. 1616-1623. -
További szerzők:Bakondi Edina (1975-) (biokémikus, vegyész) Szabó Éva (1965-) (bőrgyógyász, kozmetológus) Gergely Pál (1947-) (biokémikus) Szabó Csaba Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
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DOI
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2.

001-es BibID:BIBFORM014285
Első szerző:Bakondi Edina (biokémikus, vegyész)
Cím:Cytoprotective effect of gallotannin in oxidatively stressed HaCaT keratinocytes : the role of poly(ADP-ribose) metabolism / Edina Bakondi, Péter Bai, Katalin Erdélyi, Csaba Szabó, Pál Gergely, László Virág
Dátum:2004
ISSN:0891-5849 (Print)
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Astringents/ pharmacology
Cell Line
Cytoprotection
Humans
Hydrolyzable Tannins/ pharmacology
Keratinocytes/cytology/drug effects/ metabolism
NAD/metabolism
Oxidative Stress/drug effects
Poly(ADP-ribose) Polymerases/ metabolism
Animals
Asthma/ drug therapy
Bronchoalveolar Lavage
Catalysis
Cell Death
Cell Movement
Chemokine CXCL2
Chemokines/metabolism
Cytokines/metabolism
Disease Models, Animal
Down-Regulation
Enzyme Inhibitors/ pharmacology
Interleukin-10/metabolism
Interleukin-12/metabolism
Interleukin-13/metabolism
Interleukin-5/metabolism
Leukocytes, Mononuclear/metabolism
Lung/pathology
Male
Mice
Mice, Inbred BALB C
Ovalbumin/metabolism/pharmacology
Peroxidase/metabolism
Poly(ADP-ribose) Polymerases/ antagonists & inhibitors
Time Factors
Tumor Necrosis Factor-alpha/metabolism
Antineoplastic Agents/toxicity
Biological Markers/analysis
Cardiomyopathy, Dilated/chemically induced/enzymology
Doxorubicin/ toxicity
Enzyme Activation
Heart/ drug effects
Heart Failure/chemically induced
Matrix Metalloproteinases/ metabolism
Models, Animal
Myocardium/enzymology/ pathology
Reperfusion Injury/chemically induced/enzymology
Acute Disease
Catalysis/drug effects
Chronic Disease
Creatine Kinase/blood
Enzyme Inhibitors/pharmacology
Heart/ drug effects/physiopathology
Heart Failure/ chemically induced/physiopathology/prevention & control
L-Lactate Dehydrogenase/blood
Metalloporphyrins/ pharmacology
Mice, Inbred C57BL
Mice, Knockout
Nitric Oxide Synthase/antagonists & inhibitors/genetics/metabolism
Nitric Oxide Synthase Type II
Nitric Oxide Synthase Type III
Oxidative Stress/drug effects/genetics
Peroxynitrous Acid/ metabolism
Survival Rate
Antibiotics, Antineoplastic
Creatine Kinase/metabolism
Doxorubicin
Enzyme Activation/drug effects
Heart Failure/ chemically induced/pathology/physiopathology
Hemodynamics/drug effects
L-Lactate Dehydrogenase/metabolism
Metalloendopeptidases/metabolism
Poly(ADP-ribose) Polymerases/ genetics/ metabolism
Survival Analysis
Ventricular Function, Left/genetics
Apoptosis
Benzamides/ pharmacology
Caspases/metabolism
Cells, Cultured
DNA Damage/drug effects
DNA Fragmentation/drug effects
Enzyme Activation/drug effects/physiology
Mitochondria/ drug effects
Nitrates
Nitrites/toxicity
Nitrogen Oxides/ toxicity
Poly(ADP-ribose) Polymerases/ antagonists & inhibitors/metabolism
Protective Agents/ pharmacology
Thymus Gland/cytology/ drug effects
Tyrosine
Megjelenés:Experimental Dermatology 13 : 3 (2004), p. 170-178. -
További szerzők:Bai Péter (1976-) (biokémikus) Erdélyi Katalin (1978-) (molekuláris biológus, biokémikus) Szabó Csaba Gergely Pál (1947-) (biokémikus) Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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3.

001-es BibID:BIBFORM014256
Első szerző:Bakondi Edina (biokémikus, vegyész)
Cím:Detection of poly(ADP-ribose) polymerase activation in oxidatively stressed cells and tissues using biotinylated NAD substrate / Bakondi, E., Bai, P., Szabo, E., Hunyadi, J., Gergely, P., Szabo, C., Virag, L.
Dátum:2002
ISSN:0022-1554 (Print)
Megjegyzések:Poly(ADP-ribose) polymerase (PARP) is a nuclear enzyme activated by DNA damage. Activated PARP cleaves NAD(+) into nicotinamide and (ADP-ribose) and polymerizes the latter on nuclear acceptor proteins. Over-activation of PARP by reactive oxygen and nitrogen intermediates represents a pathogenetic factor in various forms of inflammation, shock, and reperfusion injury. Using a novel commercially available substrate, 6-biotin-17-nicotinamide-adenine-dinucleotide (bio-NAD(+)), we have developed three applications, enzyme cytochemistry, enzyme histochemistry, and cell ELISA, to detect the activation of PARP in oxidatively stressed cells and tissues. With the novel assay we were able to detect basal and hydrogen peroxide-induced PARP activity in J774 macrophages. We also observed that mitotic cells display remarkably elevated PARP activity. Hydrogen peroxide-induced PARP activation could also be detected in wild-type peritoneal macrophages but not in macrophages from PARP-deficient mice. Application of hydrogen peroxide to the skin of mice also induced bio-NAD(+) incorporation in the keratinocyte nuclei. Hydrogen peroxide-induced PARP activation and its inhibition by pharmacological PARP inhibitors could be detected in J774 cells with the ELISA assay that showed good correlation with the traditional [(3)H]-NAD incorporation method. The bio-NAD(+) assays represent sensitive, specific, and non-radioactive alternatives for detection of PARP activation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Biotin/analogs & derivatives
Cells, Cultured
egyetemen (Magyarországon) készült közlemény
Enzyme Activation
Enzyme-Linked Immunosorbent Assay
Hydrogen Peroxide
Macrophages
Mice
Mice, Inbred C57BL
Mice, Mutant Strains
NAD/analogs & derivatives
Oxidative Stress
Poly(ADP-ribose) Polymerases
Skin/drug effects
Megjelenés:The Journal of Histochemistry and Cytochemistry. - 50 : 1 (2002), p. 91-98. -
További szerzők:Bai Péter (1976-) (biokémikus) Szabó Éva (1965-) (bőrgyógyász, kozmetológus) Hunyadi János (1943-) (bőrgyógyász, kozmetológus, allergológus) Gergely Pál (1947-) (biokémikus) Szabó Csaba Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
Internet cím:elektronikus változat
DOI
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4.

001-es BibID:BIBFORM007444
Első szerző:Erdélyi Katalin (molekuláris biológus, biokémikus)
Cím:Dual role of poly(ADP-ribose) glycohydrolase in the regulation of cell death in oxidatively stressed A549 cells / Erdélyi K., Bai P., Kovács I., Szabó É., Mocsár G., Kakuk A., Szabó Cs., Gergely P., Virág L.
Dátum:2009
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
DNA damage
gene silencing
egyetemen (Magyarországon) készült közlemény
apoptosis
necrosis
hydrogen peroxide
apoptosis-inducing factor
Megjelenés:The FASEB Journal. - 23 : 10 (2009), p. 3553-3563. -
További szerzők:Bai Péter (1976-) (biokémikus) Kovács István (1985-) (biokémikus) Szabó Éva (1965-) (bőrgyógyász, kozmetológus) Mocsár Gábor (1981-) (biofizikus) Kakuk Annamária (1976-) (molekuláris biológus) Szabó Csaba Gergely Pál (1947-) (biokémikus) Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
Internet cím:elektronikus változat
DOI
Borító:

5.

001-es BibID:BIBFORM039793
035-os BibID:PMID:12102657
Első szerző:Virág László (biokémikus, sejtbiológus, farmakológus)
Cím:Nitric oxide-peroxynitrite-poly(ADP-ribose) polymerase pathway in the skin / László Virág, Éva Szabó, Edina Bakondi, Péter Bai, Pál Gergely, János Hunyadi, Csaba Szabo
Dátum:2002
ISSN:0906-6705
Megjegyzések:In the last decade it has become well established that in the skin, nitric oxide (NO), a diffusable gas, mediates various physiologic functions ranging from the regulation of cutaneous blood flow to melanogenesis. If produced in excess, NO combines with superoxide anion to form peroxynitrite (ONOO-), a cytotoxic oxidant that has been made responsible for tissue injury during shock, inflammation and ischemia-reperfusion. The opposite effects of NO and ONOO- on various cellular processes may explain the 'double-edged sword' nature of NO depending on whether or not cellular conditions favour peroxynitrite formation. Peroxynitrite has been shown to activate the nuclear nick sensor enzyme, poly(ADP-ribose) polymerase (PARP). Overactivation of PARP depletes the cellular stores of NAD+, the substrate of PARP, and the ensuing 'cellular energetic catastrophy' results in necrotic cell death. Whereas the role of NO in numerous skin diseases including wound healing, burn injury, psoriasis, irritant and allergic contact dermatitis, ultraviolet (UV) light-induced sunburn erythema and the control of skin infections has been extensively documented, the intracutaneous role of peroxynitrite and PARP has not been fully explored. We have recently demonstrated peroxynitrite production, DNA breakage and PARP activation in a murine model of contact hypersensitivity, and propose that the peroxynitrite-PARP route represents a common pathway in the pathomechanism of inflammatory skin diseases. Here we briefly review the role of NO in skin pathology and focus on the possible roles played by peroxynitrite and PARP in various skin diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Experimental Dermatology 11 : 3 (2002), p. 189-202. -
További szerzők:Szabó Éva (1965-) (bőrgyógyász, kozmetológus) Bakondi Edina (1975-) (biokémikus, vegyész) Bai Péter (1976-) (biokémikus) Gergely Pál (1947-) (biokémikus) Hunyadi János (1943-) (bőrgyógyász, kozmetológus, allergológus) Szabó Csaba
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM014289
Első szerző:Virág László (biokémikus, sejtbiológus, farmakológus)
Cím:Effects of poly(ADP-ribose) polymerase inhibition on inflammatory cell migration in a murine model of asthma / Virag, L., Bai, P., Bak, I., Pacher, P., Mabley, J. G., Liaudet, L., Bakondi, E., Gergely, P., Kollai, M., Szabo, C.
Dátum:2004
ISSN:0891-5849 (Print)
Megjegyzések:Poly(ADP-ribose) polymerase-1 (PARP-1), a monomeric nuclear enzyme present in eukaryotes, plays a role in cell death, inflammatory mediator expression, and mononuclear cell recruitment in various experimental models of inflammation and reperfusion injury. Part of the molecular mechanism of this function involves the regulation of cytokine and chemokine production. Since chemokines are principal regulators of mononuclear and polymorphonuclear cell trafficking in asthma, we investigated the possibility whether PARP modulates chemokine production and cell recruitment in a murine model of asthma. MATERIAL/METHODS: We studied ovalbumin-sensitized mice challenged with a single dose of ovalbumin. RESULTS: PARP inhibition with the phenanthridinone-based PARP inhibitor PJ34 suppressed inflammatory cell migration. These effects were associated with downregulation of the CC chemokine MIP-1alpha, but not the CXC chemokine MIP-2. The production of TNF- alpha and IL-12, but not IL-5 or IL-13, was also suppressed by PARP inhibition. CONCLUSIONS: Our results demonstrate the pathogenetic role of PARP activation in a murine model of asthma. PARP selectively regulates the production of certain chemokines and cytokines in this experimental model, which may be responsible for some of the observed protective effects seen in the current murine asthma model.Matrix metalloproteinase (MMP) activation contributes to the development of various pathophysiological conditions, including dilated cardiomyopathy, congestive heart failure, and reperfusion injury. Increased oxidative and nitrosative stress have been implicated in the activation of MMPs and also in the cardiotoxicity of doxorubicin (DOX), a commonly used antitumor agent. Thus, we hypothesized that MMP activation occurs in DOX-induced cardiotoxicity. Male Balb/c mice received a single injection of DOX (25 mg/kg i.p.) and were sacrificed 12 h, 1, 2, 3 and 4 days later. Hearts and aortae were harvested for MMP zymography. DOX induced time-dependent activation of MMPs both in the heart and in the aortic tissue with an earlier onset in the latter. These results demonstrate that MMP activation is an early event in DOX-induced cardiotoxicity and raises the possibility that MMP inhibitors may influence the outcome of this severe complication.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Asthma/ drug therapy
Bronchoalveolar Lavage
Catalysis
Cell Death
Cell Movement
Chemokine CXCL2
Chemokines/metabolism
Cytokines/metabolism
Disease Models, Animal
Down-Regulation
Enzyme Inhibitors/ pharmacology
Interleukin-10/metabolism
Interleukin-12/metabolism
Interleukin-13/metabolism
Interleukin-5/metabolism
Leukocytes, Mononuclear/metabolism
Lung/pathology
Male
Mice
Mice, Inbred BALB C
Ovalbumin/metabolism/pharmacology
Peroxidase/metabolism
Poly(ADP-ribose) Polymerases/ antagonists & inhibitors
Time Factors
Tumor Necrosis Factor-alpha/metabolism
Antineoplastic Agents/toxicity
Biological Markers/analysis
Cardiomyopathy, Dilated/chemically induced/enzymology
Doxorubicin/ toxicity
Enzyme Activation
Heart/ drug effects
Heart Failure/chemically induced
Matrix Metalloproteinases/ metabolism
Models, Animal
Myocardium/enzymology/ pathology
Reperfusion Injury/chemically induced/enzymology
Acute Disease
Catalysis/drug effects
Chronic Disease
Creatine Kinase/blood
Enzyme Inhibitors/pharmacology
Heart/ drug effects/physiopathology
Heart Failure/ chemically induced/physiopathology/prevention & control
L-Lactate Dehydrogenase/blood
Metalloporphyrins/ pharmacology
Mice, Inbred C57BL
Mice, Knockout
Nitric Oxide Synthase/antagonists & inhibitors/genetics/metabolism
Nitric Oxide Synthase Type II
Nitric Oxide Synthase Type III
Oxidative Stress/drug effects/genetics
Peroxynitrous Acid/ metabolism
Survival Rate
Antibiotics, Antineoplastic
Creatine Kinase/metabolism
Doxorubicin
Enzyme Activation/drug effects
Heart Failure/ chemically induced/pathology/physiopathology
Hemodynamics/drug effects
L-Lactate Dehydrogenase/metabolism
Metalloendopeptidases/metabolism
Poly(ADP-ribose) Polymerases/ genetics/ metabolism
Survival Analysis
Ventricular Function, Left/genetics
Apoptosis
Benzamides/ pharmacology
Caspases/metabolism
Cells, Cultured
DNA Damage/drug effects
DNA Fragmentation/drug effects
Enzyme Activation/drug effects/physiology
Mitochondria/ drug effects
Nitrates
Nitrites/toxicity
Nitrogen Oxides/ toxicity
Poly(ADP-ribose) Polymerases/ antagonists & inhibitors/metabolism
Protective Agents/ pharmacology
Thymus Gland/cytology/ drug effects
Tyrosine
külföldön készült közlemény
Megjelenés:Medical Science Monitor. - 10 : 3 (2004), p. BR77-83. -
További szerzők:Bai Péter (1976-) (biokémikus) Bak István (1975-) (vegyész, analitikus, farmakológus) Pacher Pál Mabley, Jon G. Liaudet, Lucas Bakondi Edina (1975-) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus) Kollai, M. Szabó Csaba
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM014267
Első szerző:Virág László (biokémikus, sejtbiológus, farmakológus)
Cím:Peroxynitrite-induced cytotoxicity : mechanism and opportunities for intervention / Virag, L., Szabo, E., Gergely, P., Szabo, C.
Dátum:2003
ISSN:0378-4274 (Print)
Megjegyzések:Peroxynitrite is formed in biological systems when superoxide and nitric oxide are produced at near equimolar ratio. Although not a free radical by chemical nature (as it has no unpaired electron), peroxynitrite is a powerful oxidant exhibiting a wide array of tissue damaging effects ranging from lipid peroxidation, inactivation of enzymes and ion channels via protein oxidation and nitration to inhibition of mitochondrial respiration. Low concentrations of peroxynitrite trigger apoptotic death, whereas higher concentrations induce necrosis with cellular energetics (ATP and NAD) serving as switch between the two modes of cell death. Peroxynitrite also damages DNA and thus triggers the activation of DNA repair systems. A DNA nick sensor enzyme, poly(ADP-ribose) polymerase-1 (PARP-1) also becomes activated upon sensing DNA breakage. Activated PARP-1 cleaves NAD(+) into nicotinamide and ADP-ribose and polymerizes the latter on nuclear acceptor proteins. Peroxynitrite-induced overactivation of PARP consumes NAD(+) and consequently ATP culminating in cell dysfunction, apoptosis or necrosis. This cellular suicide mechanism has been implicated among others in the pathomechanism of stroke, myocardial ischemia, diabetes and diabetes-associated cardiovascular dysfunction. Here, we review the cytotoxic effects (apoptosis and necrosis) of peroxynitrite focusing on the role of accelerated ADP-ribose turnover. Regulatory mechanisms of peroxynitrite-induced cytotoxicity such as antioxidant status, calcium signalling, NFkappaB activation, protein phosphorylation, cellular adaptation are also discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Apoptosis
Humans
Peroxynitrous Acid/biosynthesis
Poly(ADP-ribose) Polymerases
egyetemen (Magyarországon) készült közlemény
Megjelenés:Toxicol Lett. - 140-141 (2003), p. 113-124. -
További szerzők:Szabó Éva (1965-) (bőrgyógyász, kozmetológus) Gergely Pál (1947-) (biokémikus) Szabó Csaba
Internet cím:DOI
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