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Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells.

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Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells. / Wu, Jian; Ma, Jian; Fan, Sheung-Tat; Schlitt, Hans J; Tsui, Tung Yu.

in: BIOCHEM BIOPH RES CO, Jahrgang 338, Nr. 2, 2, 2005, S. 890-896.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Wu, J, Ma, J, Fan, S-T, Schlitt, HJ & Tsui, TY 2005, 'Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells.', BIOCHEM BIOPH RES CO, Jg. 338, Nr. 2, 2, S. 890-896. <http://www.ncbi.nlm.nih.gov/pubmed/16246303?dopt=Citation>

APA

Wu, J., Ma, J., Fan, S-T., Schlitt, H. J., & Tsui, T. Y. (2005). Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells. BIOCHEM BIOPH RES CO, 338(2), 890-896. [2]. http://www.ncbi.nlm.nih.gov/pubmed/16246303?dopt=Citation

Vancouver

Wu J, Ma J, Fan S-T, Schlitt HJ, Tsui TY. Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells. BIOCHEM BIOPH RES CO. 2005;338(2):890-896. 2.

Bibtex

@article{60508c1be5864e4f93b88aace60bc6d9,
title = "Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells.",
abstract = "The enzymatic action of heme oxygenase (HO) is mediated by the cleavage of heme into carbon monoxide, ferrous iron, and biliverdin/bilirubin. Here, we show that induction of HO-1 expression, an inducible form of HO, down-regulates IFN-gamma-induced MHC class II expression in endothelial cells. Among three catalytic products of HO, bilirubin, but not carbon monoxide or ferrous iron, mediated the suppressive effects of HO through the reduction of mRNA levels of Stat-1-dependent class II transactivator. Expression of HO-1 could suppress the levels of IFN-gamma-induced Stat-1 phosphorylation. This effect could be mimicked by exposing the cells to one of its catalytic products, bilirubin. In addition, HO-1 or bilirubin could modulate the transcript activities of Stat-1-driven gene expression in luciferase reporter assays. These findings suggest an important role of HO-1 in the modulation of immune responses through suppression of MHC-II expression in antigen presenting cells. Our data provide a new line of evidence supporting HO-1-targeted therapy for immune modulation.",
author = "Jian Wu and Jian Ma and Sheung-Tat Fan and Schlitt, {Hans J} and Tsui, {Tung Yu}",
year = "2005",
language = "Deutsch",
volume = "338",
pages = "890--896",
journal = "BIOCHEM BIOPH RES CO",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Bilirubin derived from heme degradation suppresses MHC class II expression in endothelial cells.

AU - Wu, Jian

AU - Ma, Jian

AU - Fan, Sheung-Tat

AU - Schlitt, Hans J

AU - Tsui, Tung Yu

PY - 2005

Y1 - 2005

N2 - The enzymatic action of heme oxygenase (HO) is mediated by the cleavage of heme into carbon monoxide, ferrous iron, and biliverdin/bilirubin. Here, we show that induction of HO-1 expression, an inducible form of HO, down-regulates IFN-gamma-induced MHC class II expression in endothelial cells. Among three catalytic products of HO, bilirubin, but not carbon monoxide or ferrous iron, mediated the suppressive effects of HO through the reduction of mRNA levels of Stat-1-dependent class II transactivator. Expression of HO-1 could suppress the levels of IFN-gamma-induced Stat-1 phosphorylation. This effect could be mimicked by exposing the cells to one of its catalytic products, bilirubin. In addition, HO-1 or bilirubin could modulate the transcript activities of Stat-1-driven gene expression in luciferase reporter assays. These findings suggest an important role of HO-1 in the modulation of immune responses through suppression of MHC-II expression in antigen presenting cells. Our data provide a new line of evidence supporting HO-1-targeted therapy for immune modulation.

AB - The enzymatic action of heme oxygenase (HO) is mediated by the cleavage of heme into carbon monoxide, ferrous iron, and biliverdin/bilirubin. Here, we show that induction of HO-1 expression, an inducible form of HO, down-regulates IFN-gamma-induced MHC class II expression in endothelial cells. Among three catalytic products of HO, bilirubin, but not carbon monoxide or ferrous iron, mediated the suppressive effects of HO through the reduction of mRNA levels of Stat-1-dependent class II transactivator. Expression of HO-1 could suppress the levels of IFN-gamma-induced Stat-1 phosphorylation. This effect could be mimicked by exposing the cells to one of its catalytic products, bilirubin. In addition, HO-1 or bilirubin could modulate the transcript activities of Stat-1-driven gene expression in luciferase reporter assays. These findings suggest an important role of HO-1 in the modulation of immune responses through suppression of MHC-II expression in antigen presenting cells. Our data provide a new line of evidence supporting HO-1-targeted therapy for immune modulation.

M3 - SCORING: Zeitschriftenaufsatz

VL - 338

SP - 890

EP - 896

JO - BIOCHEM BIOPH RES CO

JF - BIOCHEM BIOPH RES CO

SN - 0006-291X

IS - 2

M1 - 2

ER -