Phosphorylcholine acts as a Ca2+-dependent receptor molecule for lymphocyte perforin

Nature. 1989 Jan 19;337(6204):272-4. doi: 10.1038/337272a0.


Large granular lymphocytes and cytolytic T-lymphocytes (CTL) contain numerous cytoplasmic granules thought to be responsible, at least in part, for the cytolytic activity of these effector cells. Isolated granules are lytic for a variety of target cells and the granule proteins are specifically released upon target-cell interaction. Major proteins in mouse CTL granules are a family of seven serine proteases designated granzymes A to G, and a pore-forming protein called perforin (cytolysin). Purified perforin is cytolytic in the presence of Ca2+ and shows ultrastructural, immunological and amino-acid sequence similarities to complement component C9. Despite these similarities, perforin and C9 are clearly distinct in their mode of target-cell recognition. Whereas C9 insertion is absolutely dependent on a receptor moiety assembled from the complement proteins C5b, C6, C7, and C8 on the target-cell membrane, no requirement for a receptor molecule has been reported for perforin. Here, we demonstrate that phosphorylcholine acts as a specific, Ca2+-dependent receptor molecule for perforin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / pharmacology*
  • Choline / analogs & derivatives*
  • Chromatography, Affinity
  • Erythrocytes / metabolism
  • Hemolysis / drug effects
  • Membrane Glycoproteins*
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism*
  • Perforin
  • Phospholipids / pharmacology
  • Phosphorylcholine / metabolism*
  • Phosphorylcholine / pharmacology
  • Pore Forming Cytotoxic Proteins
  • Protein Binding
  • Sheep
  • T-Lymphocytes, Cytotoxic / metabolism*


  • Membrane Glycoproteins
  • Membrane Proteins
  • Phospholipids
  • Pore Forming Cytotoxic Proteins
  • Phosphorylcholine
  • Perforin
  • Choline
  • Calcium