Trauma-associated human neutrophil alterations revealed by comparative proteomics profiling Journal Article

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Authors: Zhou, J. Y.; Krovvidi, R. K.; Gao, Y.; Gao, H.; Petritis, B. O.; De, A. K.; Miller-Graziano, C. L.; Bankey, P. E.; Petyuk, V. A.; Nicora, C. D.; Clauss, T. R.; Moore, R. J.; Shi, T.; Brown, J. N.; Kaushal, A.; Xiao, W.; Davis, R. W.; Maier, R. V.; Tompkins, R. G.; Qian, W. J.; Camp, D. G., 2nd; Smith, R. D.; Inflammation and the Host Response to Injury Large Scale Collaborative Research Program
Article Title: Trauma-associated human neutrophil alterations revealed by comparative proteomics profiling
Abstract: PURPOSE: Polymorphonuclear neutrophils (PMNs) play an important role in mediating the innate immune response after severe traumatic injury; however, the cellular proteome response to traumatic condition is still largely unknown. EXPERIMENTAL DESIGN: We applied 2D-LC-MS/MS-based shotgun proteomics to perform comparative proteome profiling of human PMNs from severe trauma patients and healthy controls. RESULTS: A total of 197 out of ~2500 proteins (being identified with at least two peptides) were observed with significant abundance changes following the injury. The proteomics data were further compared with transcriptomics data for the same genes obtained from an independent patient cohort. The comparison showed that the protein abundance changes for the majority of proteins were consistent with the mRNA abundance changes in terms of directions of changes. Moreover, increased protein secretion was suggested as one of the mechanisms contributing to the observed discrepancy between protein and mRNA abundance changes. Functional analyses of the altered proteins showed that many of these proteins were involved in immune response, protein biosynthesis, protein transport, NRF2-mediated oxidative stress response, the ubiquitin-proteasome system, and apoptosis pathways. CONCLUSIONS AND CLINICAL RELEVANCE: Our data suggest increased neutrophil activation and inhibited neutrophil apoptosis in response to trauma. The study not only reveals an overall picture of functional neutrophil response to trauma at the proteome level, but also provides a rich proteomics data resource of trauma-associated changes in the neutrophil that will be valuable for further studies of the functions of individual proteins in PMNs.
Keywords: Burn and Shock Trauma Institute; Humans; Signal Transduction; Apoptosis; Case-Control Studies; NF-E2-Related Factor 2/metabolism; Neutrophils/immunology/metabolism; Oxidative Stress; Proteasome Endopeptidase Complex/metabolism; Protein Biosynthesis; Protein Transport; Proteomics; Transcriptome; Ubiquitin/metabolism; Wounds and Injuries/genetics/immunology/metabolism/pathology; Genomics; Human neutrophil; LC-MS/MS; Trauma
Journal Title: Proteomics.Clinical applications
Volume: 7
Issue: 7-8
ISSN: 1862-8354; 1862-8346
Publisher: WILEY-VCH Verlag GmbH Co. KGaA, Weinheim  
Journal Place: Germany
Date Published: 2013
Start Page: 571
End Page: 583
Language: eng
DOI/URL:

10.1002/prca.201200109
Notes: LR: 20140623; CI: (c) 2013; GR: DP2 OD006668/OD/NIH HHS/United States; GR: DP2OD006668/OD/NIH HHS/United States; GR: P41 GM103493/GM/NIGMS NIH HHS/United States; GR: P41 GM103493/GM/NIGMS NIH HHS/United States; GR: R24 GM102656/GM/NIGMS NIH HHS/United States; GR: T15 LM007033/LM/NLM NIH HHS/United States; GR: T32 GM-008256/GM/NIGMS NIH HHS/United States; GR: U54 GM-62119-02/GM/NIGMS NIH HHS/United States; GR: U54 GM062119/GM/NIGMS NIH HHS/United States; JID: 101298608; 0 (NF-E2-Related Factor 2); 0 (NFE2L2 protein, human); 0 (Ubiquitin); EC 3.4.25.1 (Proteasome Endopeptidase Complex); NIHMS485116; OID: NLM: NIHMS485116 [Available on 08/01/14]; OID: NLM: PMC3737403 [Available on 08/01/14]; OTO: NOTNLM; PMCR: 2014/08/01 00:00; 2012/09/13 [received]; 2013/01/31 [revised]; 2013/02/25 [accepted]; 2013/05/22 [aheadofprint]; ppublish