TY - JOUR
T1 - Regulation of superoxide-producing NADPH oxidases in nonphagocytic cells
AU - Takeya, Ryu
AU - Ueno, Noriko
AU - Sumimoto, Hideki
N1 - Funding Information:
We are grateful to Yohko Kage (Kyushu University and JST), Miki Matsuo (Kyushu University), and Natsuko Yoshiura (Kyushu University) for technical assistance, and Minako Nishino (Kyushu University and JST) for secretarial assistance. 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 CREST and BIRD projects of JST (Japan Science and Technology Agency).
PY - 2006
Y1 - 2006
N2 - The membrane-integrated protein gp91phox functions as the catalytic center of the superoxide-producing phagocyte NADPH oxidase. Recent studies have identified homologs of gp91phox in nonphagocytic cells, which constitute the NADPH oxidase (Nox) family. Activation of the Nox oxidases leads to production of reactive oxygen species (ROS), thereby participating in a variety of biological events, such as host defense, hormone biosynthesis, and signal transduction. The activity of the Nox enzymes is regulated by various proteins, including the small GTPase Rac; regulatory mechanisms differ dependent on the type of the Nox proteins. For example, an oxidase activator (p47 phox or Noxo1) and an oxidase activator (p67phox or Noxa1) are absolutely required for superoxide production by gp91phox and Nox1, but not by Nox3. Rac, albeit probably dispensable to the Nox3 activity, plays an essential role in activation of gp91phox. Thus, functional reconstitution of Nox systems is crucial for the study of Nox regulation. Here we describe a basic method for the reconstitution of Nox systems by expression of oxidase proteins in transfectable cells.
AB - The membrane-integrated protein gp91phox functions as the catalytic center of the superoxide-producing phagocyte NADPH oxidase. Recent studies have identified homologs of gp91phox in nonphagocytic cells, which constitute the NADPH oxidase (Nox) family. Activation of the Nox oxidases leads to production of reactive oxygen species (ROS), thereby participating in a variety of biological events, such as host defense, hormone biosynthesis, and signal transduction. The activity of the Nox enzymes is regulated by various proteins, including the small GTPase Rac; regulatory mechanisms differ dependent on the type of the Nox proteins. For example, an oxidase activator (p47 phox or Noxo1) and an oxidase activator (p67phox or Noxa1) are absolutely required for superoxide production by gp91phox and Nox1, but not by Nox3. Rac, albeit probably dispensable to the Nox3 activity, plays an essential role in activation of gp91phox. Thus, functional reconstitution of Nox systems is crucial for the study of Nox regulation. Here we describe a basic method for the reconstitution of Nox systems by expression of oxidase proteins in transfectable cells.
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U2 - 10.1016/S0076-6879(06)06034-4
DO - 10.1016/S0076-6879(06)06034-4
M3 - Review article
C2 - 16472678
AN - SCOPUS:32144436424
VL - 406
SP - 456
EP - 468
JO - Methods in Enzymology
JF - Methods in Enzymology
SN - 0076-6879
M1 - 34
ER -