Linked Life Data

8663389

Source:http://linkedlifedata.com/resource/pubmed/id/8663389

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1996-9-3
pubmed:abstractText
Neutrophils exhibit a dramatic enhancement of integrin-mediated cell adhesion in response to lipopolysaccharide (LPS). This response requires CD14 on the neutrophil and plasma proteins in solution. We have purified the factor from plasma that facilitates the adhesive response of neutrophil to LPS by using a combination of affinity and ion-exchange chromatography. Previous work has shown that the activity is associated with apolipoprotein A-I (apoA-I), and here we show that this activity is associated with an apoA-I-bearing complex of protein and phospholipid. Native polyacrylamide gel electrophoresis (PAGE) analysis showed a ladder of bands in the Mr 200,000 region, and electron microscopy revealed round, indented particles of 11.4 +/- 0.12 nm in diameter. Characterization of these particles revealed a density of 1.219-1.264 g/ml and approximately 10 molecules of lipid phosphate per Mr 200,000 complex. SDS-PAGE showed that each of the bands seen in native PAGE was composed of several polypeptides. These were identified as apoA-I, LPS binding protein (LBP), and factor H-related proteins (FHRPs). Physical association of apoA-I, LBP, and FHRP in these particles was further confirmed using double immunodiffusion, and association of LBP and FHRP in plasma was confirmed by coimmunoprecipitation. FHRPs are the numerically dominant protein components in these particles, and all plasma FHRP-1 appears to be associated with these particles. We suggest that FHRPs may be the defining constituent of this novel "lipoprotein" particle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acute-Phase Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14, http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I, http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Complement Factor H, http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids, http://linkedlifedata.com/resource/pubmed/chemical/complement factor H, human, http://linkedlifedata.com/resource/pubmed/chemical/lipopolysaccharide-binding protein, http://linkedlifedata.com/resource/pubmed/chemical/very high density lipoproteins
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18054-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Plasma lipopolysaccharide-binding protein is found associated with a particle containing apolipoprotein A-I, phospholipid, and factor H-related proteins.
pubmed:affiliation
Laboratory of Cellular Physiology and Immunology, The Rockefeller University, New York, New York 10021, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.