The cytotoxic T cell proteinase granzyme B does not activate interleukin-1 beta-converting enzyme.

The results revealed that acid residue astite P1, is unique among eukaryotic ser- only granzyme B expression is correlated with thdeevelopment ine proteases andis shared with only one othekrnown of cytotoxicity in T cells in response to stimulatiobny mitogen, eukaryotic protease, interleukin-lp-convertingenzyme allogeneic cells, or aCD3, suggesting

A J Darmon; N Ehrman; A Caputo; J Fujinaga; R C Bleackley

2021

Scholarcy highlights

  • Alison J.Damon$,Nancy Ehrman, Antonio CaputoB, Jocelyne Fujinaga, and R
  • The results revealed that acid residue astite P1, is unique among eukaryotic ser- only granzyme B expression is correlated with thdeevelopment ine proteases andis shared with only one othekrnown of cytotoxicity in T cells in response to stimulatiobny mitogen, eukaryotic protease, interleukin-lp-convertingenzyme allogeneic cells, or aCD3, suggesting
  • Recent kin-lpto produce biologically active interleukin-la anedvidence has suggested a role for granzyme B in target cell is itself synthesized aasn inactive precursor
  • The results clearly show that pre-murine ICE is not cleaved by granzyme B but is cleaved to a certain extent by human recombinant ICE
  • Even after a 16-h incubation, granzymeB does not cleave pre-mICE. These results suggest that pre-mICE is not a substrate for 6 granzyme B
  • The accepted model for CTL-mediated cytotoxicity proposes that CTLs recognize and bind target cells resulting in CTL activation and the release of granule contents into the intertransfected COS cell lysates, assayin the presence of mICE; 6, lysate of COS cells transfected with granzyme B expression vector, assay in the presence of mICE
  • 149, that granzyme B and ICE infact are able tocleave the same or related substrate within a cell and thereby induce DNA fragmentation and apoptosis

Need more features? Save interactive summary cards to your Scholarcy Library.