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 ◽  
...  

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.

2006 ◽  
Vol 15 (1) ◽  
pp. 11-15
Author(s):  
Kang Jin ◽  
You Tian ◽  
Jin Xin ◽  
Masahisa Inoue ◽  
Kojun Setsu ◽  
...  

1997 ◽  
Vol 273 (1) ◽  
pp. L1-L9 ◽  
Author(s):  
H. R. Wong ◽  
J. R. Wispe

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.


2012 ◽  
Vol 344 (5) ◽  
pp. 383-390 ◽  
Author(s):  
Liang-Chao Wang ◽  
Chih-Yuan Huang ◽  
Ming-Hsiu Wu ◽  
Ying-Sheng Lee ◽  
Kuen-Jer Tsai ◽  
...  

2015 ◽  
pp. 505-512 ◽  
Author(s):  
I.-C. CHUANG ◽  
M.-S. HUANG ◽  
L.-J. HUANG ◽  
S.-H. CHOU ◽  
T.-N. TSAI ◽  
...  

Studies have demonstrated that heat shock protein 70 (HSP70) plays an important role in the protection of stressed organisms. The development of strategies for enhancing HSPs expression may provide novel means of minimizing inflammatory lung conditions, such as acute lung injury. This study aimed to examine the effect of L-alanyl-L-glutamine (GLN) inhalation in enhancing pulmonary HSP72 (inducible HSP70) expression and attenuating lung damage in a model of acute lung injury induced by Lipopolysaccharide (LPS) inhalation. The experimental rats were randomly assigned to one of four experimental groups: (1) NS: saline inhalation; (2) NS-LPS: pretreatment by saline inhalation 12 h before LPS inhalation; (3) GLN: glutamine inhalation; (4) GLN-LPS: pretreatment by glutamine inhalation 12 h before LPS inhalation. The results show that GLN compared with saline administration, led to significant increase in lung HSP72 both in non LPS-treated rats and LPS-treated rats. In LPS-treated rats, pretreatment by GLN inhalation produced less lung injury as evidenced by the decrease in lung injury score and dramatic decrease in lactate dehydrogenase (LDH) activity and polymorphonuclear leukocyte cell differentiation counts (PMN %) in the bronchoalveolar lavage fluid. The study indicates that prophylactic glutamine inhalation associated with the enhancement of HSP72 synthesis attenuates tissue damage in experimental lung injury.


Lung ◽  
2017 ◽  
Vol 195 (4) ◽  
pp. 469-476 ◽  
Author(s):  
Shuko Tokuriki ◽  
Aiko Igarashi ◽  
Takashi Okuno ◽  
Genrei Ohta ◽  
Hironobu Naiki ◽  
...  

2009 ◽  
Vol 9 (1) ◽  
Author(s):  
Takayoshi Fujibayashi ◽  
Naozumi Hashimoto ◽  
Mayumi Jijiwa ◽  
Yoshinori Hasegawa ◽  
Toshihisa Kojima ◽  
...  

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