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


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 interaction1–4. Major proteins in mouse CTL granules are a family of seven serine proteases designated granzymes A to G5, and a pore-forming protein called perforin (cytolysin) 1–4,6. Purified perforin is cytolytic in the presence of Ca2+ and shows ultrastructural, immunological and ammo-acid sequence similarities to complement component C96–8. 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 C89 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.

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Tschopp, J., Schäfer, S., Masson, D. et al. Phosphorylcholine acts as a Ca2+-dependent receptor molecule for lymphocyte perforin. Nature 337, 272–274 (1989).

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