Arginine-specific mono(ADP-ribosyl)transferase activity in human neutrophil polymorphs. A possible link with the assembly of filamentous actin and chemotaxis.
Mono(ADP-ribosyl)transferase activity has been detected on the external surface of human polymorphonuclear neutrophil leucocytes (PMNs). The corresponding cDNA has been cloned and shown to be identical to that derived from human skeletal muscle. Our results suggest that mono(ADP-ribosyl)transferase is involved in the transduction pathway mediating (i) receptor-dependent re-alignment of cytoskeletal actin and (ii) chemotaxis of PMNs.
Kefalas
P
P
Department of Clinical Pharmacology, Royal Postgraduate Medical School, London, United Kingdom.
Allport
J R
JR
Donnelly
L E
LE
Rendell
N B
NB
Murray
S
S
Taylor
G W
GW
Lo
G
G
Yadollahi-Farsani
M
M
MacDermot
J
J
D036002:ADP Ribose Transferases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002634:Chemotaxis, Leukocyte; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D006801:Humans; D009504:Neutrophils / Q000201:enzymology*
D017261:Glycosylphosphatidylinositols; D036002:ADP Ribose Transferases