Apparent cleavage of poly(ADP-ribose) polymerase in non-apoptotic mouse LTA cells: an artifact of cross-reactive secondary antibody

Proteolytic cleavage of the nuclear enzyme poly(ADP-ribose) polymerase (PARP) to fragments of 89 kD and 24 kD is widely observed during apoptotic cell death. In the present study, labelling of a Mr approximately 89000 polypeptide was demonstrated in untreated mouse LTA cells during probing of immuno...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1998-01, Vol.178 (1-2), p.245-249
Main Authors: Budihardjo, I I, Poirier, G G, Kaufmann, S H
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - immunology
Apoptosis
Bisbenzimidazole - metabolism
Cell Line
Cellular biology
Cross Reactions
Fibroblasts - cytology
Fibroblasts - enzymology
Fluorescent Dyes - metabolism
Humans
Mice
Microscopy, Fluorescence
Molecular Weight
Peptide Fragments - immunology
Peptide Fragments - metabolism
Poly(ADP-ribose) Polymerases - immunology
Poly(ADP-ribose) Polymerases - metabolism
Polypeptides
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Summary:Proteolytic cleavage of the nuclear enzyme poly(ADP-ribose) polymerase (PARP) to fragments of 89 kD and 24 kD is widely observed during apoptotic cell death. In the present study, labelling of a Mr approximately 89000 polypeptide was demonstrated in untreated mouse LTA cells during probing of immunoblots with C-2-10 monoclonal anti-PARP antibody. The source of the labeling was traced to the secondary antibody preparation, which labeled a Mr approximately 89000 polypeptide in murine LTA cells but not in human cells. These observations indicate that assessment of PARP cleavage must be (1) performed with appropriate controls when new cell lines are investigated and (2) carefully interpreted in light of additional biochemical or morphological data demonstrating apoptotic changes.
ISSN:0300-8177
1573-4919
DOI:10.1023/A:1006808001462