The alpha 7 integrin as a target protein for cell surface mono-ADP-ribosylation in muscle cells

Advances in Experimental Medicine and Biology
A Zolkiewska, J Moss

Abstract

A membrane-associated arginine-specific mono-ADP-ribosyltransferase was purified 215,000-fold from rabbit skeletal muscle and its gene was isolated from a skeletal muscle cDNA library. The enzyme was a glycosylphosphatidyl-inositol-linked protein, present on the surface of differentiated skeletal muscle myoblasts (myotubes). Following incubation of cultured, intact myotubes with [adenylate-32P]NAD and analysis by SDS-PAGE, a major radiolabeled protein of 97/140 kDa (reduced/nonreduced conditions) was observed. It was identified as integrin alpha 7 based on its size, binding to a laminin affinity column, immunoprecipitation with a monoclonal antibody, and partial amino acid sequencing. Since ADP-ribosylarginine hydrolase, the enzyme responsible for cleavage of the ADP-ribosylarginine bond and a component with the transferase of a putative ADP-ribosylation cycle, is cytosolic, whereas the transferase is attached via a GPI-anchor to the cell surface, the processing of ADP-ribosylated integrin alpha 7 was investigated. 32P label was rapidly removed from [32P]ADP-ribosylated integrin alpha 7, a process inhibited by free ADP-ribose or p-nitrophenylthymidine-5'-monophosphate, alternative substrates for 5'-nucleotide phosphodiesterase....Continue Reading

Citations

Jun 23, 2004·Development, Growth & Differentiation·Nikolas ZagrisAnastasia Giakoumaki
Oct 20, 2007·The Journal of Immunology : Official Journal of the American Association of Immunologists·Shiyuan HongGeorge R Dubyak
Mar 9, 2018·Skeletal Muscle·Michelle F Goody, Clarissa A Henry
Oct 23, 2008·The Journal of Biological Chemistry·Jianming LiuStephen J Kaufman

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