Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte.
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Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte. / Tsui, Tung Yu; Siu, Yeung-Tung; Schlitt, Hans J; Fan, Sheung-Tat.
in: BIOCHEM BIOPH RES CO, Jahrgang 336, Nr. 3, 3, 2005, S. 898-902.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte.
AU - Tsui, Tung Yu
AU - Siu, Yeung-Tung
AU - Schlitt, Hans J
AU - Fan, Sheung-Tat
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
M3 - SCORING: Zeitschriftenaufsatz
VL - 336
SP - 898
EP - 902
JO - BIOCHEM BIOPH RES CO
JF - BIOCHEM BIOPH RES CO
SN - 0006-291X
IS - 3
M1 - 3
ER -
