Linked Life Data

10228028

Source:http://linkedlifedata.com/resource/pubmed/id/10228028

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1999-5-20
pubmed:abstractText
Inflammatory responses of myeloid cells to LPS are mediated through CD14, a glycosylphosphatidylinositol-anchored receptor that binds LPS. Since CD14 does not traverse the plasma membrane and alternatively anchored forms of CD14 still enable LPS-induced cellular activation, the precise role of CD14 in mediating these responses remains unknown. To address this, we created a transmembrane and a glycosylphosphatidylinositol-anchored form of LPS-binding protein (LBP), a component of serum that binds and transfers LPS to other molecules. Stably transfected Chinese hamster ovary (CHO) fibroblast and U373 astrocytoma cell lines expressing membrane-anchored LBP (mLBP), as well as separate CHO and U373 cell lines expressing membrane CD14 (mCD14), were subsequently generated. Under serum-free conditions, CHO and U373 cells expressing mCD14 responded to as little as 0.1 ng/ml of LPS, as measured by NF-kappaB activation as well as ICAM and IL-6 production. Conversely, the vector control and mLBP-expressing cell lines did not respond under serum-free conditions even in the presence of more than 100 ng/ml of LPS. All the cell lines exhibited responses to less than 1 ng/ml of LPS in the presence of the soluble form of CD14, demonstrating that they are still capable of LPS-induced activation. Taken together, these results demonstrate that mLBP, a protein that brings LPS to the cell surface, does not mediate cellular responses to LPS independently of CD14. These findings suggest that CD14 performs a more specific role in mediating responses to LPS than that of simply bringing LPS to the cell surface.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5483-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10228028-Acute-Phase Proteins, pubmed-meshheading:10228028-Amino Acid Sequence, pubmed-meshheading:10228028-Animals, pubmed-meshheading:10228028-Antigens, CD14, pubmed-meshheading:10228028-Astrocytoma, pubmed-meshheading:10228028-Base Sequence, pubmed-meshheading:10228028-CHO Cells, pubmed-meshheading:10228028-Carrier Proteins, pubmed-meshheading:10228028-Cell Membrane, pubmed-meshheading:10228028-Cricetinae, pubmed-meshheading:10228028-Dose-Response Relationship, Immunologic, pubmed-meshheading:10228028-Humans, pubmed-meshheading:10228028-Immunity, Cellular, pubmed-meshheading:10228028-Intercellular Adhesion Molecule-1, pubmed-meshheading:10228028-Interleukin-6, pubmed-meshheading:10228028-Lipopolysaccharides, pubmed-meshheading:10228028-Membrane Glycoproteins, pubmed-meshheading:10228028-Molecular Sequence Data, pubmed-meshheading:10228028-NF-kappa B, pubmed-meshheading:10228028-Recombinant Proteins, pubmed-meshheading:10228028-Tumor Cells, Cultured
pubmed:year
1999
pubmed:articleTitle
Membrane-anchored forms of lipopolysaccharide (LPS)-binding protein do not mediate cellular responses to LPS independently of CD14.
pubmed:affiliation
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't