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Serine esterase in cytolytic T lymphocytes

Abstract

The mechanisms that enable cytotoxic T lymphocytes (Tc cells) to destroy target cells are only vaguely understood. However, recent studies have identified in Tc cells1 and natural killer cells2 cytoplasmic granules that contain perform, a cytolytic protein that resembles the ninth component of complement (C9)3. Antigen-specific lysis of target cells, traditionally ascribed solely to Tc cells, has now also been demonstrated in some T-helper cell (Th cell) lines, referred to here as T helper–killer or Th/c cells4–6. We recently found a novel serine esterase that is present at greatly elevated levels in cloned murine Tc cell lines and one Th/c cell line, but not in two non-cytolytic Th cell lines7. These findings suggest that the serine esterase is involved in cytolytic activity and that a variety of effector cells share a common cytolytic mechanism. To explore the role of the serine esterase in this process, we have been studying additional properties of the enzyme in murine T cells. We show here that (1) it is a membrane-associated, disulphide-linked dimer, (2) it has trypsin-like properties but is not a general protease, (3) in density gradient centrifugation it sediments with perforin, (4) it is secreted by Tc cells during their cytolytic attack on target cells, and (5) antiserum to Tc-cell serine esterase reacts with the enzyme in Th/c cells.

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Pasternack, M., Verret, C., Liu, M. et al. Serine esterase in cytolytic T lymphocytes. Nature 322, 740–743 (1986). https://doi.org/10.1038/322740a0

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