DNA-regulated arginine-specific mono(ADP-ribosyl)ation and de-ADP-ribosylation of endogenous acceptor proteins in human neutrophils

Biochemical and Biophysical Research Communications
S ObaraM Shimoyama

Abstract

Arginine-specific mono(ADP-ribosyl)ation and de-ADP-ribosylation reactions of endogenous acceptor proteins were examined using human neutrophils. The cells contained arginine-specific ADP-ribosyltransferase, acceptor proteins and hydrolase catalyzing the release of ADP-ribose from the ADP-ribose/acceptor conjugate. One major acceptor protein with an apparent molecular mass of 27 kDa was detected in the neutrophils. The ADP-ribosylation of this protein was greatly enhanced when double-stranded DNA was added. The release of ADP-ribose from the ADP-ribosyl core-histones was suppressed. These findings provide clues as to the physiological function of neutrophil ADP-ribosyltransferase.

References

Feb 1, 1989·European Journal of Biochemistry·K MishimaM Shimoyama
Dec 30, 1988·Biochemical and Biophysical Research Communications·L Molina y VediaE G Lapetina
Sep 30, 1986·Biochemical and Biophysical Research Communications·Y C ChangD J Graves
Aug 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·J Moss, S J Stanley
May 16, 1984·Biochemical and Biophysical Research Communications·G SomanD J Graves

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Citations

Jul 1, 1996·Journal of Cellular Physiology·F L MoffatL Y Bourguignon
Sep 1, 1994·Molecular and Cellular Biochemistry·M Tsuchiya, M Shimoyama
Feb 15, 1992·European Journal of Biochemistry·M TerashimaM Shimoyama
Feb 8, 2020·Genes & Development·Kameron Azarm, Susan Smith
Feb 8, 2020·Genes & Development·Dea Slade
Apr 15, 1991·Biochemical and Biophysical Research Communications·G SomanR W Finberg

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