Role of haem oxygenase-1 in microbial host defence

被引：86

作者：

Chung, Su Wol ^{[1
,2
]}

Hall, Sean R. ^{[2
]}

Perrella, Mark A. ^{[2
]}

机构：

[1] Univ Ulsan, Coll Nat Sci, Dept Sci Biol, Ulsan 680749, South Korea

[2] Brigham & Womens Hosp, Dept Med, Div Pulm & Crit Care Med, Boston, MA 02115 USA

来源：

CELLULAR MICROBIOLOGY | 2009年 / 11卷 / 02期

基金：

美国国家卫生研究院;

关键词：

HEPATITIS-B-VIRUS; CARBON-MONOXIDE; MYCOBACTERIUM-TUBERCULOSIS; OXIDATIVE STRESS; GENE-EXPRESSION; IN-VIVO; SEPSIS; PATHOGENESIS; SARCOMA; BACH1;

D O I：

10.1111/j.1462-5822.2008.01261.x

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Haem oxygenase (HO)-1 is a cytoprotective enzyme that plays a critical role in defending the body against oxidant-induced injury during inflammatory processes. HO catalydes the degradation of haem to carbon monoxide (CO), biliverdin and ferrous iron. Biliverdin is converted to bilirubin, a potent endogenous antioxidant. CO has a number of biological functions, including anti-inflammatory properties. In various models of disease, HO-1 is known to play a critical role by ameliorating the pathological consequences of injury. In many of these models, the beneficial effects of HO-1 and its products of haem catabolism are by suppressing an inflammatory response. However, when investigating diseases due to microbial infections, inhibition of the inflammatory response could disrupt the ability of the immune system to eradicate an invading pathogen. Thus, questions remain regarding the role of HO-1 in microbial host defence. This microreview will address our present understanding of HO-1 and its functional significance in a variety of microbial infections.

引用

页码：199 / 207

页数：9

共 69 条

[1] Hepatitis C virus-core and non structural proteins lead to different effects on cellular antioxidant defenses [J].

Abdalla, MY ;

Ahmad, IM ;

Spitz, DR ;

Schmidt, WN ;

Britigan, BE .

JOURNAL OF MEDICAL VIROLOGY, 2005, 76 (04) :489-497

[2] Down-regulation of heme oxygenase-1 by hepatitis C virus infection in vivo and by the in vitro expression of hepatitis C core protein [J].

Abdalla, MY ;

Britigan, BE ;

Wen, F ;

Icardi, M ;

McCormick, ML ;

LaBrecque, DR ;

Voigt, M ;

Brown, KE ;

Schmidt, WN .

JOURNAL OF INFECTIOUS DISEASES, 2004, 190 (06) :1109-1118

[3] Heme oxygenase and the cardiovascular-renal system [J].

Abraham, NG ;

Kappas, A .

FREE RADICAL BIOLOGY AND MEDICINE, 2005, 39 (01) :1-25

[4] Epidemiology of severe sepsis in the United States: Analysis of incidence, outcome, and associated costs of care [J].

Angus, DC ;

Linde-Zwirble, WT ;

Lidicker, J ;

Clermont, G ;

Carcillo, J ;

Pinsky, MR .

CRITICAL CARE MEDICINE, 2001, 29 (07) :1303-1310

[5] Septic shock [J].

Annane, D ;

Bellissant, E ;

Cavaillon, JM .

LANCET, 2005, 365 (9453) :63-78

[6] THE PATHOGENESIS OF SEPSIS [J].

BONE, RC .

ANNALS OF INTERNAL MEDICINE, 1991, 115 (06) :457-469

[7] Sepsis: A new hypothesis for pathogenesis of the disease process [J].

Bone, RC ;

Grodzin, CJ ;

Balk, RA .

CHEST, 1997, 112 (01) :235-243

[8] Animal models of sepsis: Setting the stage [J].

Buras, JA ;

Holzmann, B ;

Sitkovsky, M .

NATURE REVIEWS DRUG DISCOVERY, 2005, 4 (10) :854-865

[9] Oxidant stress responses in influenza virus pneumonia: Gene expression and transcription factor activation [J].

Choi, AMK ;

Knobil, K ;

Otterbein, SL ;

Eastman, DA ;

Jacoby, DB .

AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY, 1996, 271 (03) :L383-L391

[10] Heme oxygenase-1-derived carbon monoxide enhances the host defense response to microbial sepsis in mice [J].

Chung, Su Wol ;

Liu, Xiaoli ;

Macias, Alvaro A. ;

Baron, Rebecca M. ;

Perrella, Mark A. .

JOURNAL OF CLINICAL INVESTIGATION, 2008, 118 (01) :239-247

← 1 2 3 4 5 6 7 →