Tsui, Tung-Yu ; Siu, Yeung-Tung ; Schlitt, Hans J. ; Fan, Sheung-Tat
Alternative Links zum Volltext:DOIVerlag
Dokumentenart: | Artikel |
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Titel eines Journals oder einer Zeitschrift: | Biochemical and Biophysical Research Communications |
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Verlag: | ACADEMIC PRESS INC ELSEVIER SCIENCE |
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Ort der Veröffentlichung: | SAN DIEGO |
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Band: | 336 |
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Nummer des Zeitschriftenheftes oder des Kapitels: | 3 |
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Seitenbereich: | S. 898-902 |
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Datum: | 2005 |
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Institutionen: | Medizin > Lehrstuhl für Chirurgie |
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Identifikationsnummer: | Wert | Typ |
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10.1016/j.bbrc.2005.08.187 | DOI |
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Stichwörter / Keywords: | NITRIC-OXIDE; ISCHEMIA/REPERFUSION INJURY; GUANYLYL CYCLASE; RAT-LIVER; MITOCHONDRIA; EXPRESSION; PROTECTS; SURVIVAL; SYSTEM; DEATH; adenosine triphosphate; energy metabolism; soluble guanylyl cyclase.; p38 mitogen-activated protein kinase; apoptosis; hepatocyte |
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Dewey-Dezimal-Klassifikation: | 600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin |
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Status: | Veröffentlicht |
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Begutachtet: | Ja, diese Version wurde begutachtet |
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An der Universität Regensburg entstanden: | Ja |
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Dokumenten-ID: | 70411 |
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Web of Science
Zusammenfassung
Heme oxygenases cleave the pro-oxidant heme molecule into carbon monoxide, ferrous iron, and biliverdin, which is subsequently converted to bilirubin. Increasing the enzymatic activities of heme oxygenase by expression of its inducible isoform, heme oxygenase-1, protects hepatocyte from apoptosis. In the present study, we investigated the mechanisms involving in heme oxygenase-1-mediated ...
Zusammenfassung
Heme oxygenases cleave the pro-oxidant heme molecule into carbon monoxide, ferrous iron, and biliverdin, which is subsequently converted to bilirubin. Increasing the enzymatic activities of heme oxygenase by expression of its inducible isoform, heme oxygenase-1, protects hepatocyte from apoptosis. In the present study, we investigated the mechanisms involving in heme oxygenase-1-mediated cytoprotection. Heme oxygenase-1 could induce the expression of anti-apoptotic protein-Bcl-xL in human hepatocyte. This effect is associated with the activation of p38 MAPK signaling pathway. Carbon monoxide derived from heme oxygenase activities significantly increased adenosine triphosphate levels in hepatocyte that was essential for potentiation of the activation of p38 MAPK signaling. Our demonstration of the importance of the energy status to maximize an anti-apoptotic response provides a new insight into HO-mediated cytoprotection. (c) 2005 Elsevier Inc. All rights reserved.