Macrophage galactose lectin is critical for Kupffer cells to clear aged platelets

J Exp Med. 2020 Apr 6;217(4):e20190723. doi: 10.1084/jem.20190723.

Abstract

Every day, megakaryocytes produce billions of platelets that circulate for several days and eventually are cleared by the liver. The exact removal mechanism, however, remains unclear. Loss of sialic acid residues is thought to feature in the aging and clearance of platelets. Using state-of-the-art spinning disk intravital microscopy to delineate the different compartments and cells of the mouse liver, we observed rapid accumulation of desialylated platelets predominantly on Kupffer cells, with only a few on endothelial cells and none on hepatocytes. Kupffer cell depletion prevented the removal of aged platelets from circulation. Ashwell-Morell receptor (AMR) deficiency alone had little effect on platelet uptake. Macrophage galactose lectin (MGL) together with AMR mediated clearance of desialylated or cold-stored platelets by Kupffer cells. Effective clearance is critical, as mice with an aged platelet population displayed a bleeding phenotype. Our data provide evidence that the MGL of Kupffer cells plays a significant role in the removal of desialylated platelets through a collaboration with the AMR, thereby maintaining a healthy and functional platelet compartment.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies / immunology
  • Asialoglycoproteins / immunology
  • Asialoglycoproteins / metabolism*
  • Blood Platelets / metabolism*
  • Cells, Cultured
  • Galactose / metabolism*
  • Healthy Volunteers
  • Humans
  • Kupffer Cells / metabolism*
  • Lectins, C-Type / immunology
  • Lectins, C-Type / metabolism*
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Phagocytosis*
  • Staphylococcal Infections / metabolism
  • Staphylococcal Infections / microbiology
  • Staphylococcus aureus / metabolism

Substances

  • Antibodies
  • Asialoglycoproteins
  • CLEC10A protein, human
  • Clec10a protein, mouse
  • Lectins, C-Type
  • MGL2 protein, mouse
  • Membrane Proteins
  • Galactose