Regulatory role of arginine-specific mono(ADP-ribosyl)transferase in muscle cells

Advances in Experimental Medicine and Biology
D J GravesK K McMahon

Abstract

Earlier we demonstrated that meta-iodobenzylguanidine (MIBG), a specific inhibitor of arginine mono-ADP-ribosylation blocks proliferation and differentiation of chick skeletal myogenic cells in culture (Exp. Cell Res., 1992, 201:33-42). Membrane fractions from 4-day, myotube cultures of embryonic chick muscle cells were incubated with 32P-NAD+. Several proteins were labeled, but labeling of two hands of about 53 and 36 kDa appeared to be due to arginyl ADP-ribosylation. Immunoprecipitation with D3 monoclonal antibody to the intermediate filament protein desmin, SDS-PAGE and autoradiography demonstrated that the 53 kDa band contained desmin, and that this desmin is ADP-ribosylated by the endogenous arginine-specific mono(ADP-ribosyl)transferase (Exp. Cell Res., 1996, in press). Desmin is the muscle-specific intermediate filament protein, and it appears to be one of the first muscle-specific proteins expressed during terminal myogenic differentiation. We have examined whether desmin can be ADP-ribosylated in muscle cells by use of polyclonal antibodies for ADP-ribosylated arginyl residues. We have found that soluble desmin is present in 5-6 day myogenic cell cultures and that this desmin contains ADP-ribose, demonstrating that de...Continue Reading

Citations

Mar 18, 2000·Proceedings of the Society for Experimental Biology and Medicine·C J SchwabK K McMahon
Oct 5, 2013·Histochemistry and Cell Biology·Daniel L WinterZhenlin Li
Sep 14, 2002·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Ilona A BarashRichard L Lieber
Mar 9, 1999·Archives of Biochemistry and Biophysics·J YuanD J Graves

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