PMID: 9173879Apr 1, 1997Paper

Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase

The Biochemical Journal
E M Jones, A Baird

Abstract

Basic fibroblast growth factor (FGF-2) appeared to be ADP-ribosylated on the surface of adult bovine aortic arch endothelial and human hepatoma cells. Further characterization of this reaction with cells expressing an arginine-specific, glycosylphosphatidylinositol-anchored, mono-ADP-ribosyltransferase demonstrated that FGF-2 is ADP-ribosylated on arginine. Incubation of transformed cells with FGF-2 and [adenylate-32P]nicotinamide-adenine dinucleotide (NAD) resulted in the rapid incorporation of [32P]ADP-ribose into FGF-2 in a time- and concentration-dependent manner, with labelling averaging 3 mol of ADP-ribose/mol of FGF-2. Excess ADP-ribose had no effect on these reactions, whereas excess NAD inhibited the ADP-ribosylation of FGF-2, consistent with an enzymic rather than a non-enzymic ADP-ribosylation reaction. Heparin also inhibited the ADP-ribosylation reaction, whereas a neutralizing polyclonal anti-peptide antibody had no effect. Furthermore, the addition of putative receptor binding domain peptide analogues of FGF-2 reduced the maximal ADP-ribosylation of FGF-2. These results identify the cell-surface ADP-ribosylation of FGF-2 as a potentially ubiquitous event.

Citations

Jul 29, 2016·The Tohoku Journal of Experimental Medicine·Zhen LiXiaoqing Yang
Aug 11, 2001·British Journal of Pharmacology·B A SaxtyJ MacDermot
Nov 21, 2007·Organic & Biomolecular Chemistry·Hening Lin
Nov 16, 2018·JCI Insight·Hiroko Ishiwata-EndoJoel Moss
Sep 15, 2005·The FEBS Journal·Maria Di GirolamoDaniela Corda
Jul 10, 2019·Biochemical Pharmacology·Maria Di Girolamo, Gaia Fabrizio

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