Biomaterial Database

Suppression of cell adhesion and spreading activities of fibronectin by arginine-specific ADP-ribosyltransferase from chicken polymorphonuclear leukocytes. 1998

M Terashima, and C Yamamori, and M Shimoyama, and M Tsuchiya

Department of Biochemistry, Shimane Medical University, Izumo 693-8501, Japan.

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.

UI	MeSH Term	Description	Entries
D009504	Neutrophils	Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.	LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D009842	Oligopeptides	Peptides composed of between two and twelve amino acids.	Oligopeptide
D011065	Poly(ADP-ribose) Polymerases	Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE.	ADP-Ribosyltransferase (Polymerizing),Poly ADP Ribose Polymerase,Poly(ADP-Ribose) Synthase,Poly(ADP-ribose) Polymerase,PARP Polymerase,Poly ADP Ribose Transferase,Poly ADP-Ribose Synthase,Poly(ADP-Ribose) Transferase,Poly(ADPR) Polymerase,Poly(ADPribose) Polymerase,Poly ADP Ribose Synthase,Polymerase, PARP,Synthase, Poly ADP-Ribose
D002448	Cell Adhesion	Adherence of cells to surfaces or to other cells.	Adhesion, Cell,Adhesions, Cell,Cell Adhesions
D002645	Chickens	Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.	Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D005353	Fibronectins	Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.	Cold-Insoluble Globulins,LETS Proteins,Fibronectin,Opsonic Glycoprotein,Opsonic alpha(2)SB Glycoprotein,alpha 2-Surface Binding Glycoprotein,Cold Insoluble Globulins,Globulins, Cold-Insoluble,Glycoprotein, Opsonic,Proteins, LETS,alpha 2 Surface Binding Glycoprotein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D036002	ADP Ribose Transferases	Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.	ADP-Ribosyltransferase,Mono(ADP-Ribose) Transferases,NAD(P)(+)-Arginine ADP-Ribosyltransferase,NAD+ ADP-Ribosyltransferase,ADP Ribose Transferase,ADPRT,ADPRTs,ART Transferase,ART Transferases,ARTase,ARTases,Mono ADP-ribose Transferases,Mono ADPribose Transferase,Mono ADPribose Transferases,Mono(ADP-Ribose) Transferase,Mono(ADP-Ribosyl)transferase,Mono(ADPribosyl)transferase,Mono-ADP-Ribosyltransferase,MonoADPribosyltransferase,NAD ADP-Ribosyltransferase,NAD(+)-L-arginine ADP-D-ribosyltransferase,NAD-Agmatine ADP-Ribosyltransferase,NAD-Arginine ADP-Ribosyltransferase,NADP-ADPRTase,NADP-Arginine ADP-Ribosyltransferase,ADP Ribosyltransferase,ADP-Ribosyltransferase, NAD,ADP-Ribosyltransferase, NAD+,ADP-Ribosyltransferase, NAD-Agmatine,ADP-Ribosyltransferase, NAD-Arginine,ADP-Ribosyltransferase, NADP-Arginine,ADP-ribose Transferases, Mono,ADPribose Transferase, Mono,ADPribose Transferases, Mono,Mono ADP Ribosyltransferase,Mono ADP ribose Transferases,NAD ADP Ribosyltransferase,NAD Agmatine ADP Ribosyltransferase,NAD Arginine ADP Ribosyltransferase,NAD+ ADP Ribosyltransferase,NADP ADPRTase,NADP Arginine ADP Ribosyltransferase,Ribose Transferase, ADP,Ribose Transferases, ADP,Transferase, ADP Ribose,Transferase, ART,Transferase, Mono ADPribose,Transferases, ADP Ribose,Transferases, ART,Transferases, Mono ADP-ribose,Transferases, Mono ADPribose