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An inhibitor specific for the mouse T‐cell associated serine proteinase 1 (TSP‐1) inhibits the cytolytic potential of cytoplasmic granules but not of intact cytolytic T cells
Author(s) -
Simon Markus M.,
Prester Marlot,
Kramer Michael D.,
Fruth Uli
Publication year - 1989
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240400102
Subject(s) - cytolysis , cytotoxicity , cytoplasm , biology , effector , serine , cytotoxic t cell , cell culture , microbiology and biotechnology , granule (geology) , biochemistry , lysis , enzyme , in vitro , paleontology , genetics
We have investigated a proteinase inhibitor, designed according to the preferred amino acid sequence that is cleaved by the murine T‐cell specific serine proteinase 1 (TSP‐1) for its effect on the cytolytic potential of cloned cytotoxic T‐cell lines (CTLL) and of cytoplasmic granules, derived from these cells. Pretreatment of effector cells with H‐D‐Pro‐Phe‐Arg‐chloromethyl‐ketone (PFR‐CK) prior to the cytotoxicity assay did not result in inhibition of cytolytic activity of three independent CTLL and did not effect their granule‐associated TSP‐1 activity after extraction with Triton X‐100. Furthermore, PFR‐CK did not interfere with cytolysis of target cells by CTLL when present for the entire incubation period. In contrast, PFR‐CK inhibited in a dose‐dependent manner both TSP‐1 activity and the hemolytic/cytolytic potential of isolated cytoplasmic granules after their pretreatment with high‐salt concentration. We interpret these results to mean that cytolysis of target cells by CTLL involves the granule‐associated proteinase TSP‐1, which probably becomes active upon exocytosis following effector‐target cell interactions.