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1.

001-es BibID:BIBFORM040627
Első szerző:Agarwal, Anupam
Cím:Renal tubular epithelial cells mimic endothelial cells upon exposure to oxidized LDL / Agarwal A., Balla J., Balla G., Croatt A. J., Vercellotti G. M., Nath K.
Dátum:1996
ISSN:0002-9513
Megjegyzések:In protein-uric states, renal tubular epithelial cells are exposed to diverse macromolecules, including low-density lipoproteins (LDL), normally excluded from the urinary space. Oxidized LDL (LDLox) is incriminated in atherogenesis and glomerulosclerosis. Since urine is prooxidant, we considered whether LDLox injuries renal tubular epithelial cells (LLC-PK1). We demonstrate that the cytotoxicity of LDLox on LLC-PK1 cells resembles its toxicity to human umbilical vein endothelial cells (HUVEC) in that oxidized but not native LDL is injurious. Pretreatment of LLC-PK1 cells and HUVEC with antioxidants markedly reduced the cytotoxicity of LDLox. Pretreatment of LDL with antioxidants, prior to oxidation of LDL, vitiated its cytotoxicity. That LDLox is prooxidant was supported by expression of heme oxygenase, a redox-sensitive enzyme. LDLox induced heme oxygenase mRNA and enzyme activity. Pretreatment of LDL with antioxidants prior to oxidation attenuated heme oxygenase mRNA induction in LLC-PK1 and HUVEC. An iron chelator prevented cytotoxicity and heme oxygenase expression induced by LDLox. Based on these effects of LDLox, we draw an analogy between tubulointerstitial disease and atherogenesis and speculate that LDLox contributes to tubulointerstitial disease in proteinuric states.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:American Journal Of Physiology. - 271 : 4 Pt2 (1996), p. F814-F823. -
További szerzők:Balla József (1959-) (belgyógyász, nephrológus) Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Croatt, Anthony J. Vercellotti, Gregory M. Nath, Karl
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2.

001-es BibID:BIBFORM028392
Első szerző:Balla György (csecsemő és gyermekgyógyász, neonatológus)
Cím:Ferritin : a cytoprotective antioxidant strategem of endothelium / Balla G., Jacob H. S., Balla J., Rosenberg M., Nath K., Apple F., Eaton J. W., Vercellotti G. M.
Dátum:1992
Megjegyzések:Phagocyte-mediated oxidant damage to vascular endothelium is likely involved in various vasculopathies including atherosclerosis and pulmonary leak syndromes such as adult respiratory distress syndrome. We have shown that heme, a hydrophobic iron chelate, is rapidly incorporated into endothelial cells where, after as little as 1 h, it markedly aggravates cytotoxicity engendered by polymorphonuclear leukocyte oxidants or hydrogen peroxide (H2O2). In contrast, however, if cultured endothelial cells are briefly pulsed with heme and then allowed to incubate for a prolonged period (16 h), the cells become highly resistant to oxidant-mediated injury and to the accumulation of endothelial lipid peroxidation products. This protection is associated with the induction within 4 h of mRNAs for both heme oxygenase and ferritin. After 16 h heme oxygenase and ferritin have increased approximately 50-fold and 10-fold, respectively. Differential induction of these proteins determined that ferritin is probably the ultimate cytoprotectant. Ferritin inhibits oxidant-mediated cytolysis in direct relation to its intracellular concentration. Apoferritin, when added to cultured endothelial cells, is taken up in a dose-responsive manner and appears as cytoplasmic granules by immunofluorescence; in a similar dose-responsive manner, added apoferritin protects endothelial cells from oxidant-mediated cytolysis. Conversely, a site-directed mutant of ferritin (heavy chain Glu62----Lys; His65----Gly) which lacks ferroxidase activity and is deficient in iron sequestering capacity, is completely ineffectual as a cytoprotectant. We conclude that endothelium and perhaps other cell types may be protected from oxidant damage through the iron sequestrant, ferritin.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Journal of Biological Chemistry. - 267 : 25 (1992), p. 18148-18153. -
További szerzők:Jacob, Harry S. Balla József (1959-) (belgyógyász, nephrológus) Rosenberg, M. Nath, Karl Apple, F. Eaton, John W. Vercellotti, Gregory M.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM041562
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Role of heme, heme oxygenase and ferritin in free radical mediated vascular endothelial cell injury / József Balla, Gregory M. Vercellotti, Karl A. Nath, John W. Eaton, John D. Belcher, Harry S. Jacob, György Balla
Dátum:1994
Tárgyszavak:Orvostudományok Klinikai orvostudományok könyvfejezet
Megjelenés:Free Radicals in the Environment, Medicine and Toxicology : Critical Aspects and Current Highlights / ed. by H. Nohl, H. Esterbauer, C. Rice-Evans. - p. 429-466.
További szerzők:Vercellotti, Gregory M. Nath, Karl Eaton, John W. Belcher, John D. Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM040628
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Endothelial cell heme oxygenase and ferritin induction in rat lung by hemoglobin in vivo / Balla J., Nath K., Balla G., Juckett M. B., Jacob H. S., Vercellotti G. M.
Dátum:1995
ISSN:0002-9513
Megjegyzések:Iron-derived reactive oxygen species play an important role in the pathogenesis of various vascular disorders including vasculitis, atherosclerosis, and capillary leak syndromes such as the adult respiratory distress syndrome (ARDS). We have suggested that acute incorporation of the heme moiety of hemoglobin released from red blood cells into endothelium could provide catalytically active iron to the vasculature. Adaptation to chronic heme stress involves the induction of heme oxygenase and ferritin; the latter provides cytoprotection against free radicals in vitro. The present studies examine the bioavailability of heme, derived from hemoglobin, to induce heme oxygenase and ferritin in rat lungs in vivo. Intravenous injection of methemoglobin, but not oxyhemoglobin, increases total lung heme oxygenase mRNA approximately fivefold after 16 h. Accompanying this mRNA induction, expression of total lung heme oxygenase enzyme activity is also markedly enhanced. In situ hybridization for heme oxygenase reveals mRNA accumulation in the lung microvascular endothelium, implying incorporation of heme into endothelial cells. Similarly, methemoglobin significantly increases the ferritin protein content of rat lungs and in parallel, ferritin light-chain mRNA increases approximately 1.6-fold, whereas heavy-chain mRNA is upregulated by approximately 1.9-fold. Immunoreactive ferritin is present in lung microvascular endothelium after methemoglobin treatment, suggesting incorporation of heme iron into pulmonary vasculature. Subcutaneous injection of Sn-protoporphyrin IX, a competitive inhibitor of heme oxygenase, does not affect methemoglobin-induced ferritin synthesis in lungs. We speculate that methemoglobin, which might be generated by activated leukocytes in ARDS associated with disseminated interavascular coagulation, can provide heme iron to lung microvascular endothelium to induce heme oxygenase and ferritin.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:American journal of physiology. Lung cellular and molecular physiology. - 268 : 2 Pt1 (1995), p. L321-L327. -
További szerzők:Nath, Karl Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Juckett, Mark B. Jacob, Harry S. Vercellotti, Gregory M.
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5.

001-es BibID:BIBFORM040822
035-os BibID:PMID:12817058
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Haem, haem oxygenase and ferritin in vascular endothelial cell injury / József Balla, Gregory M. Vercellotti, Karl Nath, Akihiro Yachie, Emőke Nagy, John W. Eaton, György Balla
Dátum:2003
Megjegyzések:Iron-derived reactive oxygen species (ROS) are implicated in the pathogenesis of numerous vascular disorders including atherosclerosis, microangiopathic haemolytic anaemia, vasculitis and reperfusion injury. One abundant source of redox-active iron is haem, which is inherently dangerous when released from intracellular haem proteins. The present review concerns the likely involvement of haem in vascular endothelial cell damage and the strategies used by endothelium to minimize such damage. Exposure of endothelial cells to haem greatly potentiates cell killing mediated by polymorphonuclear leukocytes and other sources of ROS. Free haem also promotes the conversion of low-density lipoprotein to cytotoxic oxidized products. If only because of its abundance, haemoglobin probably represents the most important potential source of haem within the vascular endothelium; free haemoglobin in plasma, when oxidized, can transfer haem to endothelium, thereby enhancing cellular susceptibility to oxidant-mediated injury. As a defence against such toxicity, upon exposure to free haem, endothelial cells up-regulate haem oxygenase-1 and ferritin. Haem oxygenase is a haem-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide and a most dangerous product-free redox-active iron. The latter can be controlled effectively by sequestration within ferritin, a multimeric protein with a very high capacity for storing iron. These homeostatic adjustments have been shown to be effective in the protection of endothelium against the damaging effects of exogenous haem and oxidants. The central importance of this protective system was highlighted recently by the discovery of a child diagnosed with haem oxygenase-1 deficiency, who exhibited extensive endothelial damage.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Nephrology, dialysis, transplantation. - 18 : Suppl. 5. (2003), p. v8-v12. -
További szerzők:Vercellotti, Gregory M. Nath, Karl Yachie, Akihiro Nagy Emőke (neonatológus, gyermekgyógyász) Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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DOI
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6.

001-es BibID:BIBFORM040465
035-os BibID:PMID:1308986
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Endothelial cell heme oxygenase and ferritin induction by heme proteins : a possible mechanism limiting shock damage / J. Balla, H. S. Jacob, Gy. Balla, K. Nath, G. M. Vercellotti
Dátum:1992
Megjegyzések:Acutely, hemin sensitizes endothelial cells to oxidants but chronically protects the endothelium through the induction of ferritin. By releasing its heme, methemoglobin can sensitize endothelial cells in a fashion similar to free hemin. Furthermore, prolonged incubation with the endothelium allows methemoglobin to induce heme oxygenase and ferritin and concomitantly to modulate oxidant-mediated cytotoxicity. Methemoglobin but not hemoglobin, metmyoglobin or cytochrome c induces heme oxygenase and ferritin. Heme needs to be released from methemoglobin, since sodium cyanide, haptoglobin, and hemopexin inhibit the induction of these proteins. Neutrophils can oxidize hemoglobin to methemoglobin, which can subsequently induce both heme oxygenase and ferritin. We speculate that in shock with disseminated intravascular coagulation, marginated PMNs oxidize hemoglobin to heme-releasing methemoglobin. If critical defenses such as haptoglobin and hemopexin are overwhelmed, heme enters the endothelin cells, sensitizing them to oxidant damage. Endothelial cell adaptation via heme-induced heme oxygenase and ferritin production might limit ultimate progression to pulmonary and other vascular leak syndromes.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
egyetemen (Magyarországon) készült közlemény
Megjelenés:Transactions of the Association of American Physicians. - 105 (1992), p. 1-6. -
További szerzők:Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Nath, Karl Vercellotti, Gregory M.
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7.

001-es BibID:BIBFORM040454
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Heme oxygenase and ferritin induction in kidney and endothelium to prevent oxidant damage / J. Balla, Gy. Balla, H. S. Jacob, G. M. Vercellotti, K. Nath
Dátum:1994
Tárgyszavak:Orvostudományok Klinikai orvostudományok előadáskivonat
Megjelenés:22nd Congress of International Society of Internal Medicine : abstract book. - p. 225-228.
További szerzők:Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Jacob, Harry S. Vercellotti, Gregory M. Nath, Karl
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8.

001-es BibID:BIBFORM028399
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Endothelial-cell heme uptake from heme proteins : induction of sensitization and desensitization to oxidant damage / J. Balla, H. S. Jacob, G. Balla, K. Nath, J. W. Eaton, G. M. Vercellotti
Dátum:1993
Megjegyzések:Iron-derived reactive oxygen species are implicated in the pathogenesis of various vascular disorders including atherosclerosis, vasculitis, and reperfusion injury. The present studies examine whether heme, when liganded to physiologically relevant proteins as in hemoglobin, can provide potentially damaging iron to intact endothelium. We demonstrate that reduced ferrohemoglobin, while relatively innocuous to cultured endothelial cells, when oxidized to ferrihemoglobin (methemoglobin), greatly amplifies oxidant (H2O2)-mediated endothelial-cell injury. Drawing upon our previous observation that free heme similarly primes endothelium for oxidant damage, we posited that methemoglobin, but not ferrohemoglobin, releases its hemes that can then be incorporated into endothelial cells. In support, cultured endothelial cells exposed to methemoglobin--in contrast to exposure to ferrohemoglobin, cytochrome c, or metmyoglobin--rapidly increased their heme oxygenase mRNA and enzyme activity, thereby supporting heme uptake; ferritin production was also markedly increased after such exposure, thus attesting to eventual incorporation of Fe. These cellular methemoglobin effects were inhibited by the heme-scavenging protein hemopexin and by haptoglobin or cyanide, agents that strengthen the liganding between heme and globin. If the endothelium is exposed to methemoglobin for a more prolonged period (16 hr), it accumulates large amounts of ferritin; concomitantly, and presumably associated with iron sequestration by this protein, the endothelium converts from hypersusceptible to hyperresistant to oxidative damage. We conclude that when oxidation of hemoglobin facilitates release of its heme groups, catalytically active iron is provided to neighboring tissue environments. The effect of this relinquished heme on the vasculature is determined both by extracellular factors--i.e., plasma proteins, such as haptoglobin and hemopexin--as well as intracellular factors, including heme oxygenase and ferritin. Acutely, if both extra- and intracellular defenses are overwhelmed, cellular toxicity arises; chronically, when ferritin is induced, resistance to oxidative injury may supervene.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 90 : 20 (1993), p. 9285-9289. -
További szerzők:Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Nath, Karl Eaton, John W. Vercellotti, Gregory M.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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9.

001-es BibID:BIBFORM040457
035-os BibID:PMID:8221666
Első szerző:Cermak, Jaroslav
Cím:Tumor cell heme uptake induces ferritin synthesis resulting in altered oxidant sensitivity : possible role in chemotherapy efficacy / Jaroslav Cermak, József Balla, Harry S. Jacob, György Balla, Helen Enright, Karl Nath, Gregory M. Vercellotti
Dátum:1993
ISSN:0008-5472
Megjegyzések:Neovascularization and hemorrhage are common features of malignant tumors. We wondered whether hemoglobin derived from extravasated RBC deposits heme-derived iron into the tumor, which could modulate the sensitivity of cancer cells to oxidant-mediated injury. A brief exposure (1 h) of 51Cr-radiolabeled breast cancer cells (BT-20) but not colon cancer cells (Caco-2) to hemin (10 microM) or FeSO4 (10 microM) significantly enhances cytotoxicity mediated by 0.5 mM hydrogen peroxide (H2O2). Associated with Caco-2 resistance, these cells were found to be enriched in the endogenous iron chelator, ferritin. If cellular ferritin is even further increased through 1 h incubation (24 h prior to H2O2 exposure) of both cell types with hemin, FeSO4, or exogenous spleen apoferritin itself (24 h), marked resistance to H2O2-mediated cytotoxicity is manifest. Under several conditions, the sensitivity of tumor cells to oxidant-mediated lysis is inversely proportional to their ferritin content. Pretreatment of BT-20 and Caco-2 cells with hemin or FeSO4 rapidly increases H-ferritin mRNA but only slightly increases L-ferritin mRNA; nevertheless, large increases in overall ferritin content of iron-exposed cells result. Data analogous to those with H2O2-mediated cytotoxicity were obtained in studies of bleomycin-engendered DNA strand breakage and cell damage, i.e., brief treatment of BT-20 cells with both hemin or FeSO4 significantly increases their sensitivity to bleomycin (100 micrograms/ml), whereas treatment followed by 24 h incubation with media alone significantly protects against bleomycin toxicity. We speculate that acute exposure of tumors to iron (e.g., derived from heme-proteins in hemorrhagic cancerous lesions) may increase sensitivity of some cancer cells, particularly those relatively low in endogenous ferritin, to oxidant-mediated lysis. In contrast, repeated, more chronic, exposure effector cells or chemotherapeutic agents, an effect derived from their increased synthesis and accumulation of the intracellular iron scavenger, ferritin.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Cancer Research 53 : 21 (1993), p. 5308-5313. -
További szerzők:Balla József (1959-) (belgyógyász, nephrológus) Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Enright, Helen Nath, Karl Vercellotti, Gregory M.
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10.

001-es BibID:BIBFORM023656
Első szerző:Nath, Karl
Cím:Induction of heme oxygenase is a rapid, protective response in rhabdomyolysis in the rat / Nath K. A., Balla G., Vercellotti G. M., Balla J., Jacob H. S., Levitt M. D., Rosenberg M. E.
Dátum:1992
Megjegyzések:Heme proteins such as myoglobin or hemoglobin, when released into the extracellular space, can instigate tissue toxicity. Myoglobin is directly implicated in the pathogenesis of renal failure in rhabdomyolysis. In the glycerol model of this syndrome, we demonstrate that the kidney responds to such inordinate amounts of heme proteins by inducing the heme-degradative enzyme, heme oxygenase, as well as increasing the synthesis of ferritin, the major cellular repository for iron. Prior recruitment of this response with a single preinfusion of hemoglobin prevents kidney failure and drastically reduces mortality (from 100% to 14%). Conversely, ablating this response with a competitive inhibitor of heme oxygenase exacerbates kidney dysfunction. We provide the first in vivo evidence that induction of heme oxygenase coupled to ferritin synthesis is a rapid, protective antioxidant response. Our findings suggest a therapeutic strategy for populations at a high risk for rhabdomyolysis.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Journal of Clinical Investigation. - 90 : 1 (1992), p. 267-270. -
További szerzők:Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Vercellotti, Gregory M. Balla József (1959-) (belgyógyász, nephrológus) Jacob, Harry S. Levitt, M. D. Rosenberg, M.
Internet cím:DOI
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11.

001-es BibID:BIBFORM040452
035-os BibID:PMID:8087243
Első szerző:Vercellotti, Gregory M.
Cím:Heme and the vasculature : an oxidative hazard that induces antioxidant defenses in the endothelium / Gregory M. Vercellotti, György Balla, József Balla, Karl Nath, John W. Eaton, Harry S. Jacob
Dátum:1994
ISSN:1073-1199
Megjegyzések:Heme proteins transport oxygen and facilitate redox reactions. Heme, however, may be dangerous, especially when free in biologic systems. For example, iron released from hemoglobin-derived heme can catalyze oxidative injury to neuronal cell membranes and may be a factor in post-traumatic damage to the central nervous system. We have shown that heme catalyzes the oxidation of low density lipoproteins which can damage vascular endothelial cells. The endothelium is susceptible to damage by oxidants generated by activated phagocytes, and this has been invoked as an important mechanism in a number of pathologies including the Adulte Respiratory Distress Syndrome (ARDS), acute tubular necrosis, reperfusion injury and atherosclerosis. Because of its highly hydrophobic nature, heme readily intercalates into endothelial membranes and potentiates oxidant-mediated damage. This injury is dependent on the iron content of heme and is completely blocked when concomitant hemopexin is added. Ferrohemoglobin, when added to cultured endothelial cells, is without deleterious effects, but if oxidized to ferrihemoglobin (methemoglobin), it greatly amplifies oxidant damage. Methemoglobin, but not ferrohemoglobin, releases its hemes which can then be incorporated into endothelial cells. Cultured endothelial cells, when exposed to methemoglobin but not ferrohemoglobin, cytochrome c or metmyoglobin, potentiate this oxidant injury. Stabilization of the methemoglobin by cyanide, haptoglobin or capture of the heme by hemopexin abrogates this effect. Paradoxically, more prolonged exposure of endothelium to heme or methemoglobin renders them remarkably resistant to oxidant challenge. Endothelium defends itself from heme by induction of the heme degrading enzyme heme oxygenase and the concomitant production of large amounts of the iron binding protein ferritin.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Artificial Cells, Blood Substitutes, and Immobilization Biotechnology 22 : 2 (1994), p. 207-213. -
További szerzők:Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Balla József (1959-) (belgyógyász, nephrológus) Nath, Karl Eaton, John W. Jacob, Harry S.
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