Linked Life Data

19536508

Source:http://linkedlifedata.com/resource/pubmed/id/19536508

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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-6-18
pubmed:abstractText
In pulmonary neuroepithelial bodies (NEB), presumed airway chemoreceptors, classical NADPH oxidase (gp91 phox, NOX2) is co-expressed with O(2) sensitive K(+) channels (K(+)O(2)) and functions as an O(2) sensor. Here we examined related NADPH oxidase homologues "novel oxidases "(NOX 1, 3&4) and their possible involvement in O(2) sensing. For immunolocalization we used specific antibodies against various NADPH components and K(+) (O(2)) subunits to label NEB in rat /rabbit lung and NEB related H146 tumor cell line. For gene expression profiling of NEB cells microdissected from human lung, and H146 cells, we used custom MultiGene-12TM RT-PCR array that included NADPH oxidase components and homologues /accessory proteins (NOX1-4, phox-p22, p40, p47, p67, Rac1, NOXO1 and NOXA1) and K(+)O(2) channels (Kv -1.2, 1.5, 2.1, 3.1, 3.3, 3.4, 4.2, 4.3;TASK1-3). In rat lung, NOX2, NOX4, p22phox, Kv3.3 (and Kv3.4 in rabbit) and TASK1 localized to the apical plasma membrane of NEB cells, and membrane or sub-membrane regions in H146 cells. NEB and H146 cells expressed all NOX proteins except NOX3, as well as all K(+)O(2) channels, except Kv1.5 and Kv4.3. Co-immunoprecipitation using Western blot multicolor Quantum dot labeling showed NOX2 molecular complexes with Kv but not with TASK, while NOX4 associated with TASK1 but not with Kv channel proteins. Hypoxia -induced serotonin release was inhibited in H 146 cells by siRNA to NOX2, while siRNA to NOX4 had only a partial effect, implicating NOX 2 as the predominant NEB cell O(2) sensor. Present findings support NEB cell specific plasma membrane model of O(2) sensing, and suggest unique NOX/K(+)O(2) channel combinations for diverse physiological NEB functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
648
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
427-38
pubmed:meshHeading
pubmed-meshheading:19536508-Animals, pubmed-meshheading:19536508-Anoxia, pubmed-meshheading:19536508-Base Sequence, pubmed-meshheading:19536508-Cell Line, pubmed-meshheading:19536508-Epitopes, pubmed-meshheading:19536508-Gene Expression Profiling, pubmed-meshheading:19536508-Humans, pubmed-meshheading:19536508-Immunohistochemistry, pubmed-meshheading:19536508-Infant, pubmed-meshheading:19536508-Lung, pubmed-meshheading:19536508-Male, pubmed-meshheading:19536508-Membrane Glycoproteins, pubmed-meshheading:19536508-NADPH Oxidase, pubmed-meshheading:19536508-Neuroepithelial Bodies, pubmed-meshheading:19536508-Oxygen, pubmed-meshheading:19536508-Potassium Channels, pubmed-meshheading:19536508-Protein Transport, pubmed-meshheading:19536508-RNA, Messenger, pubmed-meshheading:19536508-RNA, Small Interfering, pubmed-meshheading:19536508-RNA Interference, pubmed-meshheading:19536508-Serotonin
pubmed:year
2009
pubmed:articleTitle
The role of NOX2 and "novel oxidases" in airway chemoreceptor O(2) sensing.
pubmed:affiliation
Division of Pathology, Department of Pediatric Laboratory Medicine, The Research Institute, The Hospital for Sick Children and University of Toronto, Toronto, Ontario, Canada. ernest.cutz@sickkids.ca
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't