Linked Life Data

1512268

Source:http://linkedlifedata.com/resource/pubmed/id/1512268

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1992-9-25
pubmed:abstractText
Sodium dodecyl sulfate (SDS) treatment of a mixture of cytosol and plasma membranes from resting neutrophils resulted in the activation of the respiratory burst oxidase, a complicated enzyme that catalyzes the production of O2- from NADPH and oxygen. Activation was accompanied by translocation to the plasma membranes of the oxidase components p47phox and p67phox, which in resting cytosol were found in a M(r) approximately 240,000 complex. This translocation, which appeared to take place without a major change in the size of the cytosolic complex, did not occur if the membranes lacked cytochrome b558, and was inhibited by the peptide PRGV-HFIFNK, a sequence found near the carboxyl terminus of cytochrome b558 that was known from earlier work to inhibit O2- production by the cell-free system (Rotrosen, D., Kleinberg, M. E., Nunoi, H., Leto T., Gallin, J. I., and Malech H. L. (1990) J. Biol. Chem. 265, 8745-8750). Cytosols pretreated with the cross-linking agents 3,3'-dithiobis(sulfosuccinimidyl) propionate (DTSSP) (cleavable by 2-mercaptoethanol) and bis-(sulfosuccinimidyl) suberate (not cleavable by 2-mercaptoethanol) lost most of their ability to support O2- production in the cell-free system, and oxidase components from DTSSP-treated cytosol failed to translocate to the plasma membrane. When DTSSP-treated cytosols were incubated with 2-mercaptoethanol, however, both O2- production and translocation were partly restored, indicating that the functional impairment in DTSSP-treated cytosols was probably due at least in part to a restriction in the conformational mobility of the cross-linked peptide chains in the approximately 240,000 complex. These findings provide further support for the idea that the cytosolic components of the respiratory burst oxidase exist in the form of a approximately 240,000 complex, and suggest that the exposure of this complex to SDS induces a structural change that may or may not be associated with the loss of an inhibitory subunit too small to cause a detectable change in the size of the complex. This SDS-induced change allows translocation to take place by creating a membrane-binding site on the surface of the complex.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17327-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1512268-Adult, pubmed-meshheading:1512268-Binding Sites, pubmed-meshheading:1512268-Cell Membrane, pubmed-meshheading:1512268-Cell-Free System, pubmed-meshheading:1512268-Chromatography, Gel, pubmed-meshheading:1512268-Chromatography, Liquid, pubmed-meshheading:1512268-Cross-Linking Reagents, pubmed-meshheading:1512268-Cytosol, pubmed-meshheading:1512268-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1512268-Enzyme Activation, pubmed-meshheading:1512268-Humans, pubmed-meshheading:1512268-Immunoblotting, pubmed-meshheading:1512268-Macromolecular Substances, pubmed-meshheading:1512268-Mercaptoethanol, pubmed-meshheading:1512268-Molecular Weight, pubmed-meshheading:1512268-NADH, NADPH Oxidoreductases, pubmed-meshheading:1512268-NADPH Oxidase, pubmed-meshheading:1512268-Neutrophils, pubmed-meshheading:1512268-Succinimides
pubmed:year
1992
pubmed:articleTitle
The cytosolic components of the respiratory burst oxidase exist as a M(r) approximately 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system.
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.