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1.

001-es BibID:BIBFORM046615
Első szerző:Agarwal, Anupam
Cím:Induction of heme oxygenase in toxic renal injury : a protective role in cisplatin nephrotoxicity in the rat / Anupam Agarwal, József Balla, Jawed Alam, Anthony J. Croatt, Karl A. Nath
Dátum:1995
ISSN:0085-2538
Megjegyzések:Cellular content of heme is regulated by heme oxygenase, the rate limiting enzyme in the degradation of heme. Induction of heme oxygenase is a protective response in an in vivo model of heme protein mediated renal injury, the glycerol model of acute renal failure. In addition to heme, heme oxygenase is induced by diverse forms of oxidative stress, the functional significance of which is currently unknown. We examined whether heme oxygenase is induced, and the functional significance of such induction, in two in vivo models of oxidant-induced toxic nephropathy, namely, cisplatin and gentamicin nephropathies; nephrotoxicity in these models is not dependent on the delivery of a burden of heme proteins to the kidney as occurs in the glycerol model. We demonstrate induction of heme oxygenase mRNA and protein in the kidney as early as 6 and 12 hours after a single dose of cisplatin (6 mg/kg i.v.). Pretreatment with tin protoporphyrin, a competitive inhibitor of heme oxygenase, led to higher serum creatinine values on days 3 through 5 and lower inulin clearances on day 5; tin protoporphyrin also exacerbated renal injury in this model. Renal hemodynamics studied at day 2 after cisplatin demonstrate reduced renal blood flow rates, increased renal vascular resistance and increased fractional excretion of sodium in rats treated with tin protoporphyrin. Tin protoporphyrin alone had no significant effect on serum creatinine and renal hemodynamics in rats with intact, disease-free kidneys. We confirmed that tin protoporphyrin prevented the increase in heme oxygenase activity induced by cisplatin. Induction of heme oxygenase by cisplatin was associated with increased kidney heme content and ferritin content.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Kidney International. - 48 : 4 (1995), p. 1298-1307. -
További szerzők:Balla József (1959-) (belgyógyász, nephrológus) Alam, Jawed Croatt, Anthony J. Nath, Karl
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2.

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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3.

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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4.

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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5.

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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6.

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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7.

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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8.

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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9.

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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10.

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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11.

001-es BibID:BIBFORM040446
035-os BibID:PMID:7723246
Első szerző:Nath, Karl
Cím:Heme protein-mediated renal injury : a protective role for 21-aminosteroids in vitro and in vivo / Karl A. Nath, József Balla, Anthony J. Croatt, Gregory M. Vercellotti
Dátum:1995
ISSN:0085-2538
Megjegyzések:21-aminosteroids ("lazaroids") have recently excited much interest by virtue of their ability to inhibit lipid peroxidation in vitro and to protect against neural injury in vivo. We tested the effect of these compounds in models of heme protein-mediated renal injury in vitro and in vivo. We devised an in vitro model of heme protein-induced toxicity in which renal epithelial cells were exposed to heme proteins for one hour, after which they were subjected to glutathione depletion by 1-chloro-2,4-dinitrobenzene (CDNB). This model was associated with more than a threefold increase in lipid peroxidation (as measured by thiobarbituric acid reactive substances, TBARS) and a marked reduction in cellular glutathione content. In this model, 21-aminosteroids virtually prevented cytotoxicity as measured by the 51-chromium release assay, and significantly reduced TBARS in a dose-dependent manner. Catalase was partially protective in this model, thereby indicating hydrogen peroxide-dependent toxicity. While pursuing mechanisms accounting for enhanced cellular generation of hydrogen peroxide, we uncovered the first direct evidence that the heme prosthetic group per se directly stimulates cellular generation of hydrogen peroxide; complementing these findings is the remarkable efficacy of 21-aminosteroids in protecting against cytotoxicity induced by hydrogen peroxide. We also tested the capacity of 21-aminosteroids to protect against heme protein-mediated renal injury in vivo. Prior administration of 21-aminosteroids attenuated reductions in GFR and renal blood flow rates following the systemic infusion of methemoglobin in normal rats. 21-aminosteroids also attenuated renal injury observed over three successive days in the glycerol model of heme protein-mediated injury when this model was induced at a higher dose of glycerol (8 ml/kg body wt) but not at a lower dose (5 ml/kg body wt). We conclude that 21-aminosteroids protect against heme protein-mediated renal injury in vitro and in vivo. We suggest that these compounds are potentially useful in such clinical conditions as rhabdomyolysis, intravascular hemolysis and renal injury associated with hemoglobin-based red blood cell substitutes.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Kidney International 47 : 2 (1995), p. 592-602. -
További szerzők:Balla József (1959-) (belgyógyász, nephrológus) Croatt, Anthony J. Vercellotti, Gregory M.
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12.

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.
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