Linked Life Data

7616102

Source:http://linkedlifedata.com/resource/pubmed/id/7616102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-8-22
pubmed:abstractText
Cytosolic components of the phagocyte NADPH oxidase (p47phox, p67phox, and Rac2) translocate to the plasma membrane on cell activation where they interact with a membrane-bound cytochrome b to generate superoxide anion. Phosphorylation reactions are known to be important for activity of NADPH oxidase. Translocation of Rac2, p47phox, and p67phox were all enhanced in formyl-Met-Leu-Phe-stimulated neutrophils treated with 50 nM of the protein phosphatase 1/2A inhibitor calyculin A. Rac translocation was blocked by the tyrosine kinase inhibitors genistein (50 microM) and herbimycin (17 microM), whereas movement of p47phox and p67phox were not inhibited. Cell-free analysis of Rac translocation also demonstrated that translocation of p47phox and p67phox were not linked to the movement or availability of Rac2. Thus, Rac2 does not appear to regulate NADPH oxidase by controlling movements of the cytosolic components to the membrane-associated enzyme but may exert its effect at the level of the assembled complex. Tyrosine kinase activity is required for translocation of Rac in the chemoattractant-stimulated human neutrophil.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine..., http://linkedlifedata.com/resource/pubmed/chemical/NADPH Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine, http://linkedlifedata.com/resource/pubmed/chemical/Superoxides, http://linkedlifedata.com/resource/pubmed/chemical/neutrophil cytosol factor 67K, http://linkedlifedata.com/resource/pubmed/chemical/neutrophil cytosolic factor 1, http://linkedlifedata.com/resource/pubmed/chemical/rac GTP-Binding Proteins
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0741-5400
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
108-13
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7616102-Alkaloids, pubmed-meshheading:7616102-Amino Acid Sequence, pubmed-meshheading:7616102-Cell Compartmentation, pubmed-meshheading:7616102-Cell Membrane, pubmed-meshheading:7616102-Cytosol, pubmed-meshheading:7616102-GTP-Binding Proteins, pubmed-meshheading:7616102-Humans, pubmed-meshheading:7616102-Molecular Sequence Data, pubmed-meshheading:7616102-N-Formylmethionine Leucyl-Phenylalanine, pubmed-meshheading:7616102-NADPH Dehydrogenase, pubmed-meshheading:7616102-NADPH Oxidase, pubmed-meshheading:7616102-Neutrophils, pubmed-meshheading:7616102-Phosphoprotein Phosphatases, pubmed-meshheading:7616102-Phosphoproteins, pubmed-meshheading:7616102-Protein Phosphatase 1, pubmed-meshheading:7616102-Protein-Tyrosine Kinases, pubmed-meshheading:7616102-Staurosporine, pubmed-meshheading:7616102-Superoxides, pubmed-meshheading:7616102-rac GTP-Binding Proteins
pubmed:year
1995
pubmed:articleTitle
Dissociation of Rac translocation from p47phox/p67phox movements in human neutrophils by tyrosine kinase inhibitors.
pubmed:affiliation
Department of Immunology, Scripps Research Institute, La Jolla, California 92037, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't