TY - JOUR
T1 - Molecular composition and regulation of the Nox family NAD(P)H oxidases
AU - Sumimoto, Hideki
AU - Miyano, Kei
AU - Takeya, Ryu
N1 - Funding Information:
This work was supported in part by Grants-in-Aid for Scientific Research and National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by CREST of JST (Japan Science and Technology Agency) and BIRD of JST.
PY - 2005/12/9
Y1 - 2005/12/9
N2 - Reactive oxygen species (ROS) are conventionally regarded as inevitable deleterious by-products in aerobic metabolism with a few exceptions such as their significant role in host defense. The phagocyte NADPH oxidase, dormant in resting cells, becomes activated during phagocytosis to deliberately produce superoxide, a precursor of other microbicidal ROS, thereby playing a crucial role in killing pathogens. The catalytic center of this oxidase is the membrane-integrated protein gp91phox, tightly complexed with p22 phox, and its activation requires the association with p47 phox, p67phox, and the small GTPase Rac, which normally reside in the cytoplasm. Since recent discovery of non-phagocytic gp91 phox-related enzymes of the NAD(P)H oxidase (Nox) family-seven homologues identified in humans-deliberate ROS production has been increasingly recognized as important components of various cellular events. Here, we describe a current view on the molecular composition and post-translational regulation of Nox-family oxidases in animals.
AB - Reactive oxygen species (ROS) are conventionally regarded as inevitable deleterious by-products in aerobic metabolism with a few exceptions such as their significant role in host defense. The phagocyte NADPH oxidase, dormant in resting cells, becomes activated during phagocytosis to deliberately produce superoxide, a precursor of other microbicidal ROS, thereby playing a crucial role in killing pathogens. The catalytic center of this oxidase is the membrane-integrated protein gp91phox, tightly complexed with p22 phox, and its activation requires the association with p47 phox, p67phox, and the small GTPase Rac, which normally reside in the cytoplasm. Since recent discovery of non-phagocytic gp91 phox-related enzymes of the NAD(P)H oxidase (Nox) family-seven homologues identified in humans-deliberate ROS production has been increasingly recognized as important components of various cellular events. Here, we describe a current view on the molecular composition and post-translational regulation of Nox-family oxidases in animals.
UR - http://www.scopus.com/inward/record.url?scp=27544443327&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=27544443327&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2005.08.210
DO - 10.1016/j.bbrc.2005.08.210
M3 - Review article
C2 - 16157295
AN - SCOPUS:27544443327
SN - 0006-291X
VL - 338
SP - 677
EP - 686
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -