Regulation of macrophage-mediated xenocytotoxicity by overexpression of alpha-2,6-sialyltransferase in swine endothelial cells

Transplant Proc. 2014 May;46(4):1256-8. doi: 10.1016/j.transproceed.2013.11.026.

Abstract

Macrophages play an important role in xenogenic rejection and therefore may represent a major obstacle in clinical application of xenograft. CD33-related sialic acid-binding immunoglobulin-like lectins (Siglecs) belong to the immunoglobulin superfamily and contain a cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM) that is able to inhibit cytokine production. Because human macrophages express various CD33-related Siglecs, we hypothesized that overexpression of α-2,6-sialyltransferase (2,6-ST) in swine endothelial cells (SECs) might prevent the cytotoxicity mediated by macrophages. To confirm our hypothesis, the cytotoxicity of macrophages against 2,6-ST-overexpressing SECs was determined with the use of in vitro-generated macrophages as an effector and naïve or 2,6-ST-overexpressing SECs as a target. The 2,6-ST-overexpressing SECs were established by transfection with the genes for 2,6-ST. Transfection of 2,6-ST led to significant reduction in cytotoxicity compared with naïve SECs. These findings indicate that the sialylated ligands against CD33-related Siglecs may provide an effective therapeutic strategy to inhibit macrophage-mediated xenograft rejection in xenotransplantation.

MeSH terms

  • Animals
  • Cell Line
  • Coculture Techniques
  • Endothelial Cells / enzymology
  • Endothelial Cells / immunology*
  • Enzyme Induction
  • Graft Rejection / immunology
  • Graft Rejection / prevention & control
  • Humans
  • Ligands
  • Macrophage Activation*
  • Macrophages / immunology*
  • Macrophages / metabolism
  • Sialic Acid Binding Immunoglobulin-like Lectins / immunology
  • Sialic Acid Binding Immunoglobulin-like Lectins / metabolism
  • Sialyltransferases / biosynthesis
  • Sialyltransferases / genetics
  • Sialyltransferases / immunology*
  • Swine
  • Transfection
  • Transplantation, Heterologous
  • beta-D-Galactoside alpha 2-6-Sialyltransferase

Substances

  • Ligands
  • Sialic Acid Binding Immunoglobulin-like Lectins
  • Sialyltransferases
  • beta-D-Galactoside alpha 2-6-Sialyltransferase