title: Dynamic changes in rat mesenteric lymph proteins following trauma using label-free mass spectrometry.
abstract: Early events triggered by posttrauma/hemorrhagic shock currently represent a leading cause of morbidity and mortality in these patients. The causative agents of these events have been associated with increased neutrophil priming secondary to shock-dependent alterations of mesenteric lymph. Previous studies have suggested that unknown soluble components of the postshock mesenteric lymph are main drivers of these events. In the present study, we applied a label-free proteomics approach to further delve into the early proteome changes of the mesenteric lymph in response to hemorrhagic shock. Time-course analyses were performed by sampling the lymph every 30 min after shock up until 3 h (the time window within which a climax in neutrophil priming was observed). There are novel, transient early post-hemorrhagic shock alterations to the proteome and previously undocumented postshock protein alterations. These results underlie the triggering of coagulation and proinflammatory responses secondary to trauma/hemorrhagic shock, metabolic deregulation and apoptosis, and alterations to proteases/antiproteases homeostasis, which are suggestive of the potential implication of extracellular matrix proteases in priming neutrophil activation. Finally, there is a likely correlation between early postshock mesenteric lymph-mediated neutrophil priming and proteomics changes, above all protease/antiproteases impaired homeostasis (especially of serine proteases and metalloproteases).
authors.affiliation: Departments of *Biochemistry Molecular Genetics, †Surgery, and ‡Pediatrics, University of Colorado Denver School of Medicine; and §Colorado Bonfils Blood Center, Denver, Colorado.
authors.forename: Angelo
authors.initials: A
authors.lastname: D'Alessandro
authors.forename: Monika
authors.initials: M
authors.lastname: Dzieciatkowska
authors.forename: Erik D
authors.initials: ED
authors.lastname: Peltz
authors.forename: Ernest E
authors.initials: EE
authors.lastname: Moore
authors.forename: Janeen R
authors.initials: JR
authors.lastname: Jordan
authors.forename: Christopher C
authors.initials: CC
authors.lastname: Silliman
authors.forename: Anirban
authors.initials: A
authors.lastname: Banerjee
authors.forename: Kirk C
authors.initials: KC
authors.lastname: Hansen
mesh_terms: D000209:Acute-Phase Proteins / Q000737:chemistry; D000818:Animals; D017209:Apoptosis; D001777:Blood Coagulation; D018260:Gelsolin / Q000737:chemistry; D007249:Inflammation; D007610:Kallikreins / Q000737:chemistry; D008196:Lymph / Q000378:metabolism*; D008297:Male; D013058:Mass Spectrometry / Q000379:methods*; D008643:Mesentery / Q000378:metabolism*; D018375:Neutrophil Activation; D009504:Neutrophils / Q000378:metabolism; D010101:Oxygen Consumption; D010447:Peptide Hydrolases / Q000737:chemistry; D040901:Proteomics / Q000379:methods*; D051381:Rats; D017207:Rats, Sprague-Dawley; D057057:Serine Proteases / Q000737:chemistry; D012771:Shock, Hemorrhagic / Q000378:metabolism; D013997:Time Factors; D014947:Wounds and Injuries / Q000378:metabolism
chemical_list: D000209:Acute-Phase Proteins; D018260:Gelsolin; D010447:Peptide Hydrolases; D057057:Serine Proteases; D007610:Kallikreins