Phospholipase A2 inhibition decouples lung injury from gut ischemia-reperfusion

Surgery. 1992 Aug;112(2):173-80.

Abstract

Background: Phospholipase A2 (PLA2) has recently been implicated as a key enzyme of local inflammation after gut ischemia-reperfusion (I/R). The hypothesis of this study is that PLA2 inhibition decouples remote organ injury from gut I/R.

Methods: Sprague-Dawley rats were pretreated with a PLA2 inhibitor, quinacrine (10 mg/kg, intravenously), before the induction of gut ischemia (45 minutes of superior mesenteric artery occlusion) followed by 6 hours of reperfusion. 125I-labeled albumin leak was employed as a marker of pulmonary endothelial permeability and myeloperoxidase as a monitor of neutrophil (PMN) traffic in the gut and lung. To further characterize the impact of PLA2 inhibition, PMNs were harvested at 6 hours of reperfusion and superoxide production was measured in the presence or absence of an activating stimulus, N-formyl-methionyl-leucyl-phenylalanine.

Results: Gut I/R increased gut PLA2 activity, elicited gut PMN influx, and produced lung leak; these events were prevented by PLA2 blockade. Gut I/R also markedly enhanced PMN superoxide production with N-formyl-methionyl-leucyl-phenylalanine, and this priming was ablated by PLA2 inhibition.

Conclusion: These data suggest that PLA2 activation is a proximal step in the pathogenesis of distant organ injury after splanchnic hypoperfusion, a process that appears to involve PMN priming in the gut bed.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Capillary Permeability
  • Intestines / blood supply*
  • Ischemia / pathology*
  • Lung / metabolism
  • Lung / pathology*
  • Male
  • Neutrophils / metabolism
  • Peroxidase / metabolism
  • Phospholipases A / antagonists & inhibitors*
  • Phospholipases A / metabolism
  • Phospholipases A2
  • Rats
  • Rats, Inbred Strains
  • Reperfusion Injury / pathology*
  • Serum Albumin / metabolism
  • Superoxides / metabolism

Substances

  • Serum Albumin
  • Superoxides
  • Peroxidase
  • Phospholipases A
  • Phospholipases A2