Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase
Year: 1997
Type: article
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.
Source: Biochemical Journal
DOI: 10.1042/bj3230173
Authors: Ellene M. JONES, Andrew BAIRD
Institution: Scripps Research Institute
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2344760053