Linked Life Data

1328185

Source:http://linkedlifedata.com/resource/pubmed/id/1328185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1992-11-16
pubmed:abstractText
The respiratory burst oxidase is a multimeric enzyme responsible for O2- production by stimulated neutrophils and a few other cell types. In the resting neutrophil, the oxidase is dormant, and its subunits are distributed between the cytosol, in which they appear to exist in the form of a multisubunit complex, and the plasma membrane; but, when the neutrophil is activated, the cytosolic complex translocates to the membrane to assemble the active enzyme. Using a cell-free system in which oxidase activity was elicited with SDS, we examined the effects of GTP gamma S and dioctanoylglycerol (DiC8) on both the activation of O2- production and the transfer of the cytosolic oxidase components p47phox and p67phox to the plasma membrane. GTP (added as undialyzed cytosol) and GTP gamma S augmented the transfer of the oxidase components to the plasma membrane and was essential for the acquisition of O2- producing activity by the oxidase. DiC8 also supported the SDS-mediated transfer of oxidase components to the membrane, but O2- production did not take place unless GTP or GTP gamma S was present. In the presence of these nucleotides, however, DiC8 augmented both translocation and O2- production. We interpreted these results in terms of a mechanism in which 2 membrane-binding sites are created during the activation of the cytosolic complex, one for diacylglycerol and the other for a second site on the membrane. Development of the second membrane-binding site depends upon the action of a G protein and is essential for the expression of oxidase activity. The results further suggested that the priming of the respiratory burst oxidase in intact neutrophils might be due to an increase in membrane diacylglycerol concentration that occurs in response to the priming stimulus. Because of the increased diacylglycerol content, a larger than usual amount of active respiratory burst oxidase could be assembled on the primed plasma membrane when the neutrophil is fully activated.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19901-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1328185-Adult, pubmed-meshheading:1328185-Biological Transport, pubmed-meshheading:1328185-Blotting, Western, pubmed-meshheading:1328185-Cations, Divalent, pubmed-meshheading:1328185-Cell Membrane, pubmed-meshheading:1328185-Cell-Free System, pubmed-meshheading:1328185-Cells, Cultured, pubmed-meshheading:1328185-Chromatography, Liquid, pubmed-meshheading:1328185-Cytosol, pubmed-meshheading:1328185-Diglycerides, pubmed-meshheading:1328185-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1328185-Guanine Nucleotides, pubmed-meshheading:1328185-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:1328185-Guanosine Triphosphate, pubmed-meshheading:1328185-Humans, pubmed-meshheading:1328185-Magnesium, pubmed-meshheading:1328185-NADH, NADPH Oxidoreductases, pubmed-meshheading:1328185-NADPH Oxidase, pubmed-meshheading:1328185-Neutrophils, pubmed-meshheading:1328185-Superoxides
pubmed:year
1992
pubmed:articleTitle
The translocation of respiratory burst oxidase components from cytosol to plasma membrane is regulated by guanine nucleotides and diacylglycerol.
pubmed:affiliation
Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.