Linked Life Data

17254389

Source:http://linkedlifedata.com/resource/pubmed/id/17254389

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-1-26
pubmed:abstractText
Using a combination of gel-exclusion chromatography and ligand binding with [(125)I]-lipopolysaccharide (LPS), we discovered two novel endotoxin-binding proteins, p31(LPB) and p34(LPB), in Kupffer cells. Their molecular masses suggest that these are previously undescribed LPS-binding proteins (LBPs). Evidence from detergent-based cell extractions shows that these proteins are probably transmembrane or located on the inner leaflet of the lipid bilayer. We have partially purified the proteins from detergent extracts of Kupffer cells and proven that they bind diphosphoryl lipid A, an interaction associated with TNF-alpha production. The proteins do not bind monophosphoryl lipid A. Diphosphoryl lipid A binding occurs in the absence of serum, suggesting a mechanism of cytokine production distinct from that involving CD14 and lipopolysaccharide-binding protein (LPB). The two proteins were not detectable in resident peritoneal macrophages or in a number of other cell lines of the macrophage/monocyte lineage, suggesting specificity towards terminally differentiated macrophages such as Kupffer cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0968-0519
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
352-7
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Identification of two novel LPS-binding proteins in Kupffer cells: implications in TNF-alpha production.
pubmed:affiliation
Laboratory of Cancer Biology, Department of Surgery, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, USA. peterthomas@creighton.edu
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural