Linked Life Data

10065760

Source:http://linkedlifedata.com/resource/pubmed/id/10065760

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-5-4
pubmed:abstractText
Endothelial-neutrophil adhesion is a critical step in acute inflammatory diseases, which is mediated in part by P-selectin and platelet-activating factor (PAF). Nitric oxide (NO) is well known as an endogenous second messenger derived from endothelial cells, and regulates many important physiological events, however, the direct effects of NO on endothelial-neutrophil adhesion is less well understood. The objective of this study was to examine whether, and how relatively high levels of exogenous NO increases neutrophil adhesion with respect to P-selectin and PAF. Endothelial monolayers were exposed to chemical agents for 30 min, and the adhesion of 51Cr-labeled neutrophils measured in a static adhesion assay. Spermine-NONOate (SNO), an NO donor, significantly increased neutrophil adhesion and expression of P-selectin at a concentration of 1 mM. SNO (1 mM)-mediated neutrophil adhesion was significantly inhibited by a protein kinase G inhibitor, KT5823 (0.5 microM), but not by a classical protein kinase C inhibitor, Gö6976 (10 nM), a tyrosine kinase inhibitor, genistein (1 microM), or a protein kinase A inhibitor, H-89 (0.1 microM). P-selectin surface expression induced by 1 mM SNO was also significantly inhibited by 0.5 microM KT5823. Conversely, a cytoplasm calcium chelator, TMB-8 (0.1 mM), significantly exacerbated both the neutrophil adhesion and P-selectin expression induced by SNO. WEB 2086 (10 microM), a PAF receptor antagonist, blocked neutrophil adhesion, but did not block P-selectin expression induced by SNO. These data suggest that NO increases endothelial-neutrophil adhesion through protein kinase G-mediated P-selectin mobilization to the cell surface and endothelial PAF synthesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Azepines, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Donors, http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Oxides, http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin, http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Spermine, http://linkedlifedata.com/resource/pubmed/chemical/Triazoles, http://linkedlifedata.com/resource/pubmed/chemical/WEB 2086, http://linkedlifedata.com/resource/pubmed/chemical/spermine nitric oxide complex
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0360-3997
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-50
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Exogenous nitric oxide increases neutrophil adhesion to cultured human endothelial monolayers through a protein kinase G dependent mechanism.
pubmed:affiliation
Department of Molecular and Cellular Physiology, Louisiana State University Medical Center, Shreveport 71130-3932, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.