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acetyl-asp-glu-val-asp-p-nitroanilide etoh nature portfolio permissions reprints β-n-acetyl-d-glucosaminidase caps privacy policy ice nature 371 nature advertising social media research full size image anti-peptide antibodies directed ice-cold hypotonic buffer monoclonal antibody 10h n-terminal protein sequencer isolated lysosomal rich-fractions performed devd-ase assays lysosomal enzyme β-nag potential active-site residues access human lysosomal-rich fractions author correspondence human lysosomal-rich extracts permissions 473a protein sequencer cells lysosomal-rich fractions monoclonal antibody mapping α-chymotrypsin sensitive sites c-terminal 55 kda active monoclonal antibody c-2–10 n-terminal 62 kda fragment associates published d'amours devd-ase activity personal data devd-ase caspases privacy demonstrating cell death cell death differ purified bovine parp-1 ice-cold pbs main active fragment lysosomal rich-fractions lysosomal-rich fractions cell organelles anal lysosomal-rich extract modified bradford assay purified lysosomal proteases human leukemia jurkat lysosomal rich-extracts

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         description:The poly(ADP-ribose) polymerase (PARP-1), a 113 kDa nuclear enzyme, is cleaved in fragments of 89 and 24 kDa during apoptosis. This cleavage has become a useful hallmark of apoptosis and has been shown to be done by DEVD-ase caspases, a family of proteases activated during apoptosis. Interestingly, PARP-1 is also processed during necrosis but a major fragment of 50 kDa is observed. This event is not inhibited by zVAD-fmk, a broad spectrum caspase inhibitor, suggesting that these proteases are not implicated in the necrotic cleavage of PARP-1. Since lysosomes release their content into the cytosol during necrosis, the proteases liberated could produce the cleavage of PARP-1. We therefore isolated lysosomal rich-fractions from Jurkat T cells. Our results reveal that the in vitro lysosomal proteolytic cleavage of affinity purified bovine PARP-1 is composed of fragments corresponding, in apparent molecular weight and function, to those found in Jurkat T cells treated with necrotic inducers like 0.1% H2O2, 10% EtOH or 100 μM HgCl2. Moreover, we used purified lysosomal proteases (cathepsins B, D and G) in an in vitro cleavage assay and found that cathepsins B and G cleaved PARP-1 in fragments also found with the lysosomal rich-fractions. These findings suggest that the necrotic cleavage of PARP-1 is caused in part or in totality by lysosomal proteases released during necrosis. Cell Death and Differentiation (2001) 8, 588–594
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      headline:Characterization of the necrotic cleavage of poly(ADP-ribose) polymerase (PARP-1): implication of lysosomal proteases
      description:The poly(ADP-ribose) polymerase (PARP-1), a 113 kDa nuclear enzyme, is cleaved in fragments of 89 and 24 kDa during apoptosis. This cleavage has become a useful hallmark of apoptosis and has been shown to be done by DEVD-ase caspases, a family of proteases activated during apoptosis. Interestingly, PARP-1 is also processed during necrosis but a major fragment of 50 kDa is observed. This event is not inhibited by zVAD-fmk, a broad spectrum caspase inhibitor, suggesting that these proteases are not implicated in the necrotic cleavage of PARP-1. Since lysosomes release their content into the cytosol during necrosis, the proteases liberated could produce the cleavage of PARP-1. We therefore isolated lysosomal rich-fractions from Jurkat T cells. Our results reveal that the in vitro lysosomal proteolytic cleavage of affinity purified bovine PARP-1 is composed of fragments corresponding, in apparent molecular weight and function, to those found in Jurkat T cells treated with necrotic inducers like 0.1% H2O2, 10% EtOH or 100 μM HgCl2. Moreover, we used purified lysosomal proteases (cathepsins B, D and G) in an in vitro cleavage assay and found that cathepsins B and G cleaved PARP-1 in fragments also found with the lysosomal rich-fractions. These findings suggest that the necrotic cleavage of PARP-1 is caused in part or in totality by lysosomal proteases released during necrosis. Cell Death and Differentiation (2001) 8, 588–594
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