A serine protease (CCP1) is sequestered in the cytoplasmic granules of cytotoxic T lymphocytes

J Immunol. 1987 Nov 15;139(10):3184-8.

Abstract

Based upon the use of a new predictive algorithm, three peptides were synthesized that correspond to likely antigenic sites of the cytotoxic T cell-specific protease cytotoxic cell protein 1 (CCP1). Antibodies raised against these peptides, under reducing conditions, bound to a single protein of m.w. 29,000 found in two actively cytotoxic T cells. This protein was absent from a "cytotoxic" T cell line that had lost its cytolytic properties. By using immunocytologic techniques, the protein was localized within cytoplasmic granules. In addition, granules purified from the cytoplasm of cytotoxic T cells were shown, by Western blot analysis, to contain the protein. The molecule detected by the antibodies behaves, upon reduction, similarly to a diisopropylfluorophosphate-binding protein. Thus, here we provide evidence that CCP1, a protein whose expression correlates with cytotoxicity, is contained within organelles which have been implicated in killing. These findings strongly suggest that CCP1 plays a key role in T cell-mediated target cell lysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Cytoplasmic Granules / enzymology*
  • Cytotoxicity, Immunologic
  • Epitopes / chemical synthesis
  • Epitopes / immunology
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / immunology
  • Serine Endopeptidases / analysis*
  • Serine Endopeptidases / immunology
  • T-Lymphocytes, Cytotoxic / enzymology*
  • T-Lymphocytes, Cytotoxic / ultrastructure

Substances

  • Epitopes
  • Peptide Fragments
  • Serine Endopeptidases