(Q27631417)

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The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1

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The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1 (English)

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author name string

J Rotonda

1

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M Garcia-Calvo

2

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H G Bull

3

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W M Geissler

4

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B M McKeever

5

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C A Willoughby

6

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N A Thornberry

7

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J W Becker

8

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publication date

April 2001

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Chemistry and Biology

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8

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4

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357-68

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Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells.

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The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism.

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Target cell lysis by CTL granule exocytosis is independent of ICE/Ced-3 family proteases

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Granzyme B directly and efficiently cleaves several downstream caspase substrates: implications for CTL-induced apoptosis

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DFF45/ICAD can be directly processed by granzyme B during the induction of apoptosis

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10.1016/S1074-5521(01)00018-7

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