The Heat Shock Response and Heat Shock Protein 70: Cytoprotection in Acute Lung Injury

2001 ◽  
pp. 275-288 ◽  
Author(s):  
Hector R. Wong
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Lung Injury ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Heat Shock Protein 70 ◽  
Shock Response

Hypobaric hypoxia preconditioning attenuates acute lung injury during high-altitude exposure in rats via up-regulating heat-shock protein 70

2011 ◽  
Vol 121 (5) ◽  
pp. 223-231 ◽  
Author(s):  
Hung-Jung Lin ◽  
Chia-Ti Wang ◽  
Ko-Chi Niu ◽  
Chungjin Gao ◽  
Zhuo Li ◽  
...  
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Lung Injury ◽  
Heat Shock Protein ◽  
Oxidative Damage ◽  
Pulmonary Oedema ◽  
Heat Shock Protein 70 ◽  
Hypobaric Hypoxia ◽  
Altitude Exposure ◽  
Hypoxia Preconditioning

HHP (hypobaric hypoxia preconditioning) induces the overexpression of HSP70 (heat-shock protein 70), as well as tolerance to cerebral ischaemia. In the present study, we hypothesized that HHP would protect against HAE (high-altitude exposure)-induced acute lung injury and oedema via promoting the expression of HSP70 in lungs prior to the onset of HAE. At 2 weeks after the start of HHP, animals were exposed to a simulated HAE of 6000 m in a hypobaric chamber for 24 h. Immediately after being returned to ambient pressure, the non-HHP animals had higher scores of alveolar oedema, neutrophil infiltration and haemorrhage, acute pleurisy (e.g. increased exudate volume, increased numbers of polymorphonuclear cells and increased lung myeloperoxidase activity), increased pro-inflammatory cytokines [e.g. TNF-α (tumour necrosis factor-α), IL (interleukin)-1β and IL-6], and increased cellular ischaemia (i.e. glutamate and lactate/pyruvate ratio) and oxidative damage [glycerol, NOx (combined nitrate+nitrite) and 2,3-dihydroxybenzoic acid] markers in the BALF (bronchoalveolar fluid). HHP, in addition to inducing overexpression of HSP70 in the lungs, significantly attenuated HAE-induced pulmonary oedema, inflammation, and ischaemic and oxidative damage in the lungs. The beneficial effects of HHP in preventing the occurrence of HAE-induced pulmonary oedema, inflammation, and ischaemic and oxidative damage was reduced significantly by pretreatment with a neutralizing anti-HSP70 antibody. In conclusion, HHP may attenuate the occurrence of pulmonary oedema, inflammation, and ischaemic and oxidative damage caused by HAE in part via up-regulating HSP70 in the lungs.

scholarly journals Heat shock response and acute lung injury☆

2007 ◽  
Vol 42 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Derek S. Wheeler ◽  
Hector R. Wong
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Lung Injury ◽  
Heat Shock Response ◽  
Shock Response

Heat shock response decreases endotoxin-induced acute lung injury in rats

Respirology ◽  
1999 ◽  
Vol 4 (4) ◽  
pp. 325-330 ◽  
Author(s):  
Younsuck Koh ◽  
Chae-Man Lim ◽  
Mi Jung Kim ◽  
Tae Sun Shim ◽  
Sang Do Lee ◽  
...  
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Lung Injury ◽  
Heat Shock Response ◽  
Shock Response

Induction of the heat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model

1994 ◽  
Vol 22 (6) ◽  
pp. 917-921 ◽  
Author(s):  
JESUS VILLAR ◽  
SERGIO P. RIBEIRO ◽  
J. BRENDAN M. MULLEN ◽  
MACIEK KULISZEWSKI ◽  
MARTIN POST ◽  
...  
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Mortality Rate ◽  
Lung Injury ◽  
Heat Shock Response ◽  
Organ Damage ◽  
Injury Model ◽  
Shock Response ◽  
Lung Injury Model

A non-toxic heat shock protein 70 inducer, geranylgeranylacetone, effectively restores the heat shock response in gastric mucosa of protein-malnourished rats

2000 ◽  
Vol 118 (4) ◽  
pp. A73
Author(s):  
Kazuhito Rokutan ◽  
Tomoko Kawai ◽  
Shigetada Teshima ◽  
Tsukasa Kawahara ◽  
Takeshi Nikawa ◽  
...  
Keyword(s):  
Heat Shock ◽  
Gastric Mucosa ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Heat Shock Protein 70 ◽  
Shock Response

scholarly journals Effect of Rhubarb on Heat Shock Protein 70 Expression in Lung Tissues from Rats with Acute Lung Injury Induced by Lipopolysaccharide

2006 ◽  
Vol 15 (1) ◽  
pp. 11-15
Author(s):  
Kang Jin ◽  
You Tian ◽  
Jin Xin ◽  
Masahisa Inoue ◽  
Kojun Setsu ◽  
...  
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Lung Injury ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70

The stress response and the lung

1997 ◽  
Vol 273 (1) ◽  
pp. L1-L9 ◽  
Author(s):  
H. R. Wong ◽  
J. R. Wispe
Keyword(s):  
Gene Expression ◽  
Acute Lung Injury ◽  
Stress Response ◽  
Heat Shock ◽  
Lung Injury ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Stress Proteins ◽  
Stress Protein ◽  
Lung Cells

The stress response is a highly conserved cellular defense mechanism defined by the rapid and specific expression of stress proteins, with concomitant transient inhibition of nonstress protein gene expression. The stress proteins mediate cellular and tissue protection against diverse cytotoxic stimuli. Among the many classes of stress proteins, heat shock protein 70 and heme oxygenase-1 are the best characterized with respect to lung biology. A potential role for stress proteins in human lung disease is inferred from studies demonstrating stress protein expression in the lungs of patients with cancer, asthma, and acute lung injury. Several examples of stress protein-mediated cytoprotection exist in cell and animal models of acute lung injury. Stress protein induction protects rats against acute lung injury caused by either systemic administration of endotoxin or intratracheal administration of phospholipase A1. In vitro, increased expression of stress proteins protects lung cells against endotoxin-mediated apoptosis and oxidant injury. The mechanisms of stress response-mediated cytoprotection may involve the enzymatic and molecular chaperone properties of stress proteins. Alternatively, the stress response may protect by modulating lung proinflammatory responses. Data from extrapulmonary systems suggest that stress response-associated factors (heat shock protein 70 and heat shock factor) are directly involved in modulation of proinflammatory gene expression. Recent evidence also demonstrates interactions between the stress response and the I-kappa B/nuclear factor-kappa B pathway in cultured lung cells. Increased understanding about the role of stress proteins in lung biology may support efforts to selectively increase expression of one or more stress proteins to provide protection against human acute lung injury.

scholarly journals Heat shock stimulation of a tilapia heat shock protein 70 promoter is mediated by a distal element

2001 ◽  
Vol 356 (2) ◽  
pp. 353-359 ◽  
Author(s):  
Alfredo MOLINA ◽  
Emmanuel Di MARTINO ◽  
Joseph A. MARTIAL ◽  
Marc MULLER
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Transient Expression ◽  
Heat Shock Response ◽  
Heat Shock Protein 70 ◽  
Zebrafish Embryos ◽  
Epithelioma Papulosum Cyprini ◽  
Hsp70 Promoter ◽  
Shock Response ◽  
Constitutive Factor

We reported previously that a tilapia (Oreochromis mossambicus) heat shock protein 70 (HSP70) promoter is able to confer heat shock response on a reporter gene after transient expression both in cell culture and in microinjected zebrafish embryos. Here we present the first functional analysis of a fish HSP70 promoter, the tiHSP70 promoter. Using transient expression experiments in carp EPC (epithelioma papulosum cyprini) cells and in microinjected zebrafish embryos, we show that a distal heat shock response element (HSE1) at approx. −800 is predominantly responsible for the heat shock response of the tiHSP70 promoter. This element specifically binds an inducible transcription factor, most probably heat shock factor, and a constitutive factor. The constitutive complex is not observed with the non-functional, proximal HSE3 sequence, suggesting that both factors are required for the heat shock response mediated by HSE1.

Sign in / Sign up

Export Citation Format

Share Document