PMID: 9553724Apr 29, 1998Paper

Proteolytic cleavage of retinoblastoma protein upon DNA damage and Fas-mediated apoptosis

Cell Biology and Toxicology
L DiederichR Fotedar

Abstract

Proteolytic cleavage of key cellular proteins by caspases (ICE, CPP32, and Ich-1/Nedd2) may be crucial to the apoptotic process. The retinoblastoma tumor suppressor gene is a negative regulator of cell growth and the retinoblastoma protein (pRb) exhibits anti-apoptotic function. We show that pRb is cleaved during apoptosis induced by either UV irradiation or anti-Fas antibody. Our studies implicate CPP32-like activity in the proteolytic cleavage of pRb. The kinetics of proteolytic cleavage of pRb during apoptosis differ from that observed for other cellular proteins, suggesting that the specific cleavage of pRb during apoptosis may be an important event.

Citations

Sep 26, 2002·The Journal of Biological Chemistry·Cai BowenEdward P Gelmann
May 6, 2019·European Journal of Pharmacology·Shiva Akbari-BirganiParviz Davoodi-Monfared

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