Publication: Altered plasma proteome during an early phase of peritonitis-induced sepsis
Issued Date
2009-05-01
Resource Type
ISSN
01435221
Other identifier(s)
2-s2.0-66949135058
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Clinical Science. Vol.116, No.9 (2009), 721-730
Suggested Citation
Visith Thongboonkerd, Wararat Chiangjong, Jan Mares, Jiri Moravec, Zdenek Tuma, Thomas Karvunidis, Supachok Sinchaikul, Shui Tein Chen, Karel Opatrný, Martin Matejovic Altered plasma proteome during an early phase of peritonitis-induced sepsis. Clinical Science. Vol.116, No.9 (2009), 721-730. doi:10.1042/CS20080478 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/28107
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Altered plasma proteome during an early phase of peritonitis-induced sepsis
Other Contributor(s)
Abstract
Sepsis is a systemic response to infection commonly found in critically ill patients and is associated with multi-organ failure and high mortality rate. Its pathophysiology and molecular mechanisms are complicated and remain poorly understood. In the present study, we performed a proteomics investigation to characterize early host responses to sepsis as determined by an altered plasma proteome in a porcine model of peritonitis-induced sepsis, which simulated several clinical characteristics of human sepsis syndrome. Haemodynamics, oxygen exchange, inflammatory responses, oxidative and nitrosative stress, and other laboratory parameters were closely monitored. Plasma samples were obtained from seven pigs before and 12 h after the induction of sepsis, and plasma proteins were resolved with two-dimensional gel electrophoresis (n = 7 gels/group; before being compared with during sepsis). The resolved proteins were stained with the SYPRO Ruby fluorescence dye and subjected to quantitative and comparative analyses. From approx. 1500 protein spots visualized in each gel, levels of 36 protein spots were significantly altered in the plasma of animals with sepsis (sepsis/basal ratios or degrees of change ranged from 0.07 to 21.24). Q-TOF (quadrupole-time-of-flight) MS and MS/MS (tandem MS) identified 30 protein forms representing 22 unique proteins whose plasma levels were increased, whereas six forms of five unique proteins were significantly decreased during sepsis. The proteomic results could be related to the clinical features of this animal model, as most of these altered proteins have important roles in inflammatory responses and some of them play roles in oxidative and nitrosative stress. In conclusion, these findings may lead to a better understanding of the pathophysiology and molecular mechanisms underlying the sepsis syndrome. © The Authors Journal compilation © 2009 Biochemical Society.