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001-es BibID:	BIBFORM023029
Első szerző:	Balla József (belgyógyász, nephrológus)
Cím:	Heme, heme oxygenase and ferritin in vascular endothelial cell injury / Balla József, Vercellotti Gregory M., Jeney Viktória, Yachie Akihiro, Varga Zsuzsa, Eaton John W., Balla György
Dátum:	2005
ISSN:	1613-4125
Megjegyzések:	Iron-derived reactive oxygen species are implicated in the pathogenesis of numerous vascular disorders including atherosclerosis, microangiopathic hemolytic anemia, vasculitis, and reperfusion injury. One abundant source of redox active iron is heme, which is inherently dangerous when released from intracellular heme proteins. The present review concerns the involvement of heme in vascular endothelial cell damage and the strategies used by endothelium to minimize such damage. Exposure of endothelium to heme greatly potentiates cell killing mediated by polymorphonuclear leukocytes and other sources of reactive oxygen. Free heme also promotes the conversion of low-density lipoprotein (LDL) into cytotoxic oxidized products. Only because of its abundance, hemoglobin probably represents the most important potential source of heme within the vascular endothelium; hemoglobin in plasma, when oxidized, transfers heme to endothelium and LDL, thereby enhancing cellular susceptibility to oxidant-mediated injury. As a defense against such toxicity, upon exposure to heme or hemoglobin, endothelial cells up-regulate heme oxygenase-1 and ferritin. Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron. The latter can be effectively controlled by ferritin via sequestration and ferroxidase activity. Ferritin serves as a protective gene by virtue of antioxidant, antiapoptotic, and antiproliferative actions. These homeostatic adjustments have been shown effective in the protection of endothelium against the damaging effects of exogenous heme and oxidants. The central importance of this protective system was recently highlighted by a child diagnosed with heme oxygenase-1 deficiency, who exhibited extensive endothelial damage.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Molecular Nutrition and Food Research. - 49 : 11 (2005), p. 1030-1043. -
További szerzők:	Vercellotti, Gregory M. Jeney Viktória (1971-) (vegyész, kémia tanár) Yachie, Akihiro Varga Zsuzsa (1951-) (biokémikus, nephrológus) Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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001-es BibID:	BIBFORM002292
Első szerző:	Balla József (belgyógyász, nephrológus)
Cím:	Heme, heme oxygenase and ferritin : how the vascular endothelium survives (and dies) in an iron-rich environment / J. Balla, G. M. Vercellotti, V. Jeney, A. Yachie, Zs. Varga, H. S. Jacob, J. W. Eaton, Gy. Balla
Dátum:	2007
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Antioxidants and Redox Signaling 9 : 12 (2007), p. 2119-2137. -
További szerzők:	Vercellotti, Gregory M. Jeney Viktória (1971-) (vegyész, kémia tanár) Yachie, Akihiro Varga Zsuzsa (1951-) (biokémikus, nephrológus) Jacob, Harry S. Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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001-es BibID:	BIBFORM023038
Első szerző:	Jeney Viktória (vegyész, kémia tanár)
Cím:	Pro-oxidant and cytotoxic effects of circulating heme / Jeney V., Balla J., Yachie A., Varga Zs., Vercellotti G. M., Eaton J. W., Balla G.
Dátum:	2002
ISSN:	0006-4971
Megjegyzések:	Numerous pathologies may involve toxic side effects of free heme and hemederived iron. Deficiency of the hemecatabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium. Although heme can be directly cytotoxic, the present investigations examine the possibility that hemoglobin-derived heme and iron might be indirectly toxic through the generation of oxidized forms of low-density lipoprotein (LDL). In support, hemoglobin in plasma, when oxidized to methemoglobin by oxidants such as leukocyte-derived reactive oxygen, causes oxidative modification of LDL. Heme, released from methemogiobin, catalyzes the oxidation of LDL, which in turn induces endothelial cytolysis primarily caused by lipid hydroperoxides. Exposure of endothelium to sublethal concentrations of this oxidized LDL leads to induction of both HO-1 and ferritin. Similar endothelial cytotoxicity was caused by LDL isolated from plasma of an HO-1-deficient child. Spectral analysis of the child's plasma revealed a substantial oxidation of plasma hemoglobin to methemoglobin. Iron accumulated in the HO-1-deficient child's LDL and several independent assays revealed oxidative modification of the LDL. We conclude that hemoglobin, when oxidized in plasma, can be. indirectly cytotoxic through the generation of oxidized LDL by released heme and that, in response, the intracellular defense-HO-1 and ferritin-Is induced. These results may be relevant to a variety of disorders-such as renal failure associated with intravascular hemolysis, hemorrhagic injury to the central nervous system, and, perhaps, atherogenesis-in which hemoglobin-derived heme may promote the formation of fatty acid hydroperoxides.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Blood. - 100 : 3 (2002), p. 879-887. -
További szerzők:	Balla József (1959-) (belgyógyász, nephrológus) Yachie, Akihiro Varga Zsuzsa (1951-) (biokémikus, nephrológus) Vercellotti, Gregory M. Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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