Anoxia/reoxygenation-induced leukocyte-endothelial cell interactions

Free Radic Biol Med. 2002 Aug 15;33(4):427-32. doi: 10.1016/s0891-5849(02)00852-3.

Abstract

It is increasingly apparent that oxidants can play an important role in mediating specific cell responses and expression of genes involved in degenerative pathophysiologic states, such as inflammation. In particular, oxidant-induced activation of the multisubunit nuclear transcription factor, NFkappaB, has been implicated in the transcriptional upregulation of inflammatory genes like endothelial cell adhesion glycoproteins. A second emerging concept is the recognition that the oxidant effects in cellular and molecular regulation may be mediated by oxidant-induced loss of cellular oxidation-reduction (redox) balance. This review will provide an overview of our current understanding of leukocyte-endothelial cell interactions derived from in vitro studies of endothelial cell monolayers exposed to anoxia/reoxygenation, with specific emphasis on the molecular determinants mediating this inflammatory process and the contribution of reoxygenation-induced cellular redox imbalance to the activation of NFkappaB and the expression of endothelial surface adhesion molecules.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Adhesion Molecules / metabolism
  • Cell Hypoxia
  • Cysteine Endopeptidases
  • Endothelium, Vascular / pathology*
  • Gene Expression Regulation
  • Humans
  • Ischemia / metabolism
  • Ischemia / pathology*
  • Leukocytes / pathology*
  • Multienzyme Complexes / antagonists & inhibitors
  • NF-kappa B / metabolism
  • Neutrophils / pathology
  • Oxidation-Reduction
  • Oxidative Stress
  • Protease Inhibitors / pharmacology
  • Proteasome Endopeptidase Complex
  • Reperfusion Injury / metabolism
  • Reperfusion Injury / pathology*
  • Sulfhydryl Compounds / metabolism
  • T-Lymphocytes / pathology

Substances

  • Cell Adhesion Molecules
  • Multienzyme Complexes
  • NF-kappa B
  • Protease Inhibitors
  • Sulfhydryl Compounds
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex