Linked Life Data

16987008

Source:http://linkedlifedata.com/resource/pubmed/id/16987008

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9-10
pubmed:dateCreated
2006-9-21
pubmed:abstractText
Deliberate production of reactive oxygen species (ROS) are catalyzed by enzymes that belong to the NAD(P)H oxidase (Nox) family. The human genome contains seven members of the Nox family: the superoxide-producing enzymes Nox1 through Nox5 and the dual oxidases Duox1 and Duox2 that release hydrogen peroxide but not superoxide. Among them, the classical member gp91( phox )/Nox2 functions as the phagocyte NADPH oxidase, playing a crucial role in host defense. Although Nox2, heterodimerized with its membrane-spanning partner p22( phox ), is inactive in resting cells, during phagocytosis it forms an active complex with soluble regulatory proteins such as the organizer p47( phox ), the activator p67( phox ), and the small GTPase Rac. Here the authors describe how the novel superoxide-producing Nox oxidases (Nox1, 3, 4, and 5) with different functions are regulated by p22( phox ), the Nox organizers, the Nox activators, and Rac, and how their expression is controlled at the transcriptional level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1523-0864
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1523-32
pubmed:meshHeading
pubmed:articleTitle
Regulation of novel superoxide-producing NAD(P)H oxidases.
pubmed:affiliation
Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't