Alpha-galactosyl epitope-mediated activation of porcine aortic endothelial cells: type II activation

Transplantation. 1998 Apr 15;65(7):971-8. doi: 10.1097/00007890-199804150-00018.

Abstract

Background: Xenoreactive natural antibodies (XNAs) and complement mediate hyperacute rejection of discordant xenografts. Inhibition of complement alone results in some prolongation of graft survival, but delayed xenograft rejection still precludes long-term graft survival. In vitro data provide evidence for the direct proinflammatory activation of endothelial cells (ECs) by XNAs. These antibodies are primarily directed against galactose alpha(1-3)-galactose (alpha-gal), the major xenoantigen in the pig to primate xenotransplant model. Previous studies have shown EC activation by XNAs but failed to address the question of whether alpha-gal-specific ligands can induce EC activation. The aim of this study was to investigate whether agonist binding to the alpha-gal epitope by alpha-gal-specific lectins as compared with XNAs or elicited xenoreactive antibodies can directly elicit type II porcine aortic EC (PAEC) activation (i.e., activation that requires protein synthesis).

Methods and results: The tetravalent, alpha-gal-binding Bandeiraea simplicifolia lectin I (BS-I), the wholly alpha-gal-specific BS-I isolectin B4, and elicited primate anti-pig xenoreactive antibodies (decomplemented cynomolgus monkey anti-porcine serum) induced E-selectin protein expression in PAECs. This induction was alpha-gal-specific, as preincubation with synthetic alpha-gal carbohydrate or adsorption of lectin or serum to rabbit, but not human, red blood cells removed the activating component. E-selectin expression, induced by BS-I, was inhibited in the presence of genistein, a tyrosine kinase inhibitor, and by mepacrine, an inhibitor of phospholipase A2. Human and primate XNAs lacked this activity when tested at relevant concentrations; however, stimulation of PAECs with affinity-purified human XNA (IgM and IgG) resulted in slightly increased interleukin-8 and P-selectin mRNA levels but had no apparent effects on E-selectin transcription. BS-I strongly induced E-selectin, P-selectin, intercellular adhesion molecule-1, and interleukin-8 mRNA in an NF-kappaB-dependent manner.

Conclusions: Several agonists that specifically bind to alpha-gal can evoke type II EC activation. Hence, anti-Gal antibodies may contribute directly to xenograft rejection in the absence of complement activation.

Publication types

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

MeSH terms

  • Animals
  • Antibodies / immunology
  • Antibodies / metabolism
  • Antibodies / pharmacology
  • Antibody Specificity
  • Aorta / cytology
  • Carbohydrate Sequence
  • Cells, Cultured
  • Complement Activation*
  • Disaccharides / immunology*
  • Disaccharides / metabolism
  • E-Selectin / biosynthesis
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / immunology*
  • Endothelium, Vascular / metabolism
  • Epitopes / immunology*
  • Epitopes / metabolism
  • Genistein / pharmacology
  • Haplorhini
  • Humans
  • Immunoglobulin G / metabolism
  • Immunoglobulin M / metabolism
  • Lectins / metabolism
  • Lectins / pharmacology
  • Molecular Sequence Data
  • Plant Lectins*
  • Quinacrine / pharmacology
  • Rabbits
  • Swine
  • Transplantation, Heterologous / immunology
  • Tumor Necrosis Factor-alpha / pharmacology

Substances

  • Antibodies
  • Disaccharides
  • E-Selectin
  • Epitopes
  • Griffonia simplicifolia lectins
  • Immunoglobulin G
  • Immunoglobulin M
  • Lectins
  • Plant Lectins
  • Tumor Necrosis Factor-alpha
  • galactosyl-(1-3)galactose
  • Genistein
  • Quinacrine