Actin enhances the activation of human neutrophil NADPH oxidase in a cell-free system.
The cell-free activation of human neutrophil NADPH oxidase (02- generating enzyme) was enhanced by exogenously added G-actin (actin monomer). When cytosol, a constituent of the system, was pretreated with DNase I, which may bind to G-actin (endogenous) to block polymerization, the activation of NADPH oxidase was significantly suppressed. The activation was also impaired when cytosol G-actin was removed by DNase I-linked resin, being completely restored by the addition of G-actin. These results suggest a role of actin and its polymerization in the activation of NADPH oxidase of human neutrophils.
Morimatsu
T
T
Department of Applied Biochemistry, Faculty of Engineering, Ehime University, Matsuyama, Japan.
Kawagoshi
A
A
Yoshida
K
K
Tamura
M
M
D000199:Actins / Q000494:pharmacology*; D000818:Animals; D002458:Cell Fractionation; D002474:Cell-Free System; D003600:Cytosol / Q000201:enzymology; D003850:Deoxyribonuclease I / Q000494:pharmacology; D004789:Enzyme Activation; D006801:Humans; D007700:Kinetics; D019255:NADPH Oxidases / Q000097:blood*; D009504:Neutrophils / Q000201:enzymology*; D010047:Ovalbumin / Q000494:pharmacology; D011817:Rabbits; D013481:Superoxides / Q000097:blood
D000199:Actins; D013481:Superoxides; D010047:Ovalbumin; D019255:NADPH Oxidases; D003850:Deoxyribonuclease I