Proteomic global proteins analysis in blast lung injury reveals the altered characteristics of crucial proteins in response to oxidative stress, oxidation-reduction process and lipid metabolic process

ABSTRACT

Background: Blast lung injury (BLI) is the most common fatal blast injury induced by overpressure wave in the events of terrorist attack, gas and underground explosion. Our previous work revealed the characteristics of inflammationrelated key proteins involved in BLI, including those regulating inflammatory response, leukocyte transendothelial migration, phagocytosis, and immune process. However, the molecular characteristics of oxidative-related proteins in BLI ar still lacking. Methods: In this study, protein expression profiling of the blast lungs obtained by tandem mass tag (TMT) spectrometry quantitative proteomics were re-analyzed to identify the characteristics of oxidative-related key proteins. Forty-eight male C57BL/6 mice were randomly divided into six groups: control, 12 h, 24 h, 48 h, 72 h and 1 w after blast exposure. The differential protein expression was identified by bioinformatics analysis and verified by western blotting. Results: The results demonstrated that thoracic blast exposure induced reactive oxygen species generation and lipid peroxidation in the lungs. Analysis of global proteins and oxidative-related proteomes showed that 62, 59, 73, 69, 27 proteins (accounted for 204 distinct proteins) were identified to be associated with oxidative stress at 12 h, 24 h, 48 h, 72 h, and 1 week after blast exposure, respectively. These 204 distinct proteins were mainly enriched in response to oxidative stress, oxidation-reduction process and lipid metabolic process. We also validated these results by western blotting. Conclusions: These findings provided new perspectives on blast-induced oxidative injury in lung, which may potentially benefit the development of future treatment of BLI.

KEYWORDS:

• Blast lung injury
• lipid peroxidation
• oxidative stress
• oxidation-reduction process
• tandem mass tag spectrometry quantitative proteomics

Acknowledgements

We would like to thank the PTM-Biolabs Co., Ltd. (Hangzhou, China) for the mass spectrometry analysis and help in preparing the manuscript. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with dataset identifier PXD025183.

Disclosure statement

No potential conflict of interest was reported by the authors.

Ethics approval and consent to participate

This study was approved by the Ethics Committee of the General Hospital of Northern theater command.

Author contributions

Mingxiao Hou and Hongxu Jin designed experiments. Yunen Liu and Peifang Cong wrote the manuscript. Peifang Cong, Changci Tong and Shun Mao performed the animal experiments and analyzed the data. Xiuyun Shi, Ying Liu and Lin Shi completed pathological staining and western blot.

Additional information

Funding

This work was supported by the PLA fundation of China under Grant No. AWS14L008.