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[Cancer Research 59, 2190-2194, May 1, 1999]
© 1999 American Association for Cancer Research
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[Cancer Research 59, 2190-2194, May 1, 1999]
© 1999 American Association for Cancer Research

Molecular Biology and Genetics

Poly(ADP-ribosyl)ation of p53 during Apoptosis in Human Osteosarcoma Cells1

Cynthia M. Simbulan-Rosenthal, Dean S. Rosenthal, RuiBai Luo and Mark E. Smulson2

Department of Biochemistry and Molecular Biology, Georgetown University School of Medicine, Washington, DC 20007

Spontaneous apoptosis in human osteosarcoma cells was observed to be associated with a marked increase in the intracellular abundance of p53. Immunoprecipitation and immunoblot analysis revealed that, together with a variety of other nuclear proteins, p53 undergoes extensive poly(ADP-ribosyl)ation early during the apoptotic program in these cells. Subsequent degradation of poly(ADP-ribose) (PAR), attached to p53 presumably by PAR glycohydrolase, the only reported enzyme to degrade PAR, was apparent concomitant with the onset of proteolytic processing and activation of caspase-3, caspase-3-mediated cleavage of poly(ADP-ribose) polymerase (PARP), and internucleosomal DNA fragmentation during the later stages of cell death. The decrease in PAR covalently bound to p53 also coincided with the marked induction of expression of the p53-responsive genes bax and Fas. These results suggest that poly(ADP-ribosyl)ation may play a role in the regulation of p53 function and implies a regulatory role for PARP and/or PAR early in apoptosis.




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HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
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Molecular Cancer Research Cancer Prevention Research
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Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1999 by the American Association for Cancer Research.