Suppression of cell adhesion and spreading activities of fibronectin by arginine-specific ADP-ribosyltransferase from chicken polymorphonuclear leukocytes.
Arginine-specific ADP-ribosyltransferase present in secretory granules of chicken polymorphonuclear leukocytes (so-called heterophils) was shown to be released into the extracellular space by secretagogues (Terashima et al., J. Biochem. 120 (1996) 1209-1215). In the present work, we examined fibronectin as an extracellular target protein of the released transferase. Fibronectin was ADP-ribosylated by purified transferase and stoichiometry of ADP-ribose incorporation into fibronectin was 1.0 mol/mol of fibronectin. Cell adhesion and spreading assays revealed that ADP-ribosylation of fibronectin markedly inhibited the adhesion activity of fibronectin. A proteolytic peptide map of ADP-ribosylated fibronectin demonstrated that the modification occurs in the cell binding domain of fibronectin. ADP-ribosylation of the RGD peptide suggests that the RGD sequence is the modification site in the domain. ADP-ribosylation of fibronectin in plasma means that fibronectin can probably serve as the substrate for extracellularly released ADP-ribosyltransferase in vivo. Thus, in the extracellular space, ADP-ribosyltransferase released from polymorphonuclear leukocytes may perhaps be involved in regulation of cell adhesion process by interfering with the activity of fibronectin.
Terashima
M
M
Department of Biochemistry, Shimane Medical University, Izumo 693-8501, Japan.
Yamamori
C
C
Shimoyama
M
M
Tsuchiya
M
M
D036002:ADP Ribose Transferases / Q000378:metabolism*; D000818:Animals; D002448:Cell Adhesion; D002645:Chickens; D005353:Fibronectins / Q000737:chemistry* / Q000378:metabolism*; D009504:Neutrophils / Q000201:enzymology*; D009842:Oligopeptides / Q000737:chemistry; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism
D005353:Fibronectins; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases