Linked Life Data

10202042

Source:http://linkedlifedata.com/resource/pubmed/id/10202042

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1999-5-6
pubmed:abstractText
The complement inhibitor soluble complement receptor type 1 (sCR1) and a truncated form of sCR1, sCR1[desLHR-A], have been generated with expression of the selectin-reactive oligosaccharide moiety, sialyl Lewisx (sLex), as N-linked oligosaccharide adducts. These modified proteins, sCR1sLex and sCR1[desLHR-A]sLex, were assessed in the L-selectin- and P-selectin-dependent rat model of lung injury following systemic activation of complement by cobra venom factor and in the L-selectin-, P-selectin-, and E-selectin-dependent model of lung injury following intrapulmonary deposition of IgG immune complexes. In the cobra venom factor model, sCR1sLex and sCR1[desLHR-A]sLex caused substantially greater reductions in neutrophil accumulation and in albumin extravasation in lung when compared with the non-sLex-decorated forms. In this model, increased lung vascular binding of sCR1sLex and sCR1[desLHR-A]sLex occurred in a P-selectin-dependent manner, in contrast to the absence of any increased binding of sCR1 or sCR1[desLHR-A]. In the IgG immune complex model, sCR1[desLHR-A]sLex possessed greater protective effects relative to sCR1[desLHR-A], based on albumin extravasation and neutrophil accumulation. Enhanced protective effects correlated with greater lung vascular binding of sCR1[desLHR-A]sLex as compared with the non-sLex-decorated form. In TNF-alpha-activated HUVEC, substantial in vitro binding occurred with sCR1[desLHR-A]sLex (but not with sCR1[desLHR-A]). This endothelial cell binding was blocked by anti-E-selectin but not by anti-P-selectin. These data suggest that sLex-decorated complement inhibitors have enhanced antiinflammatory effects and appear to have enhanced ability to localize to the activated vascular endothelium.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4952-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10202042-Anti-Inflammatory Agents, Non-Steroidal, pubmed-meshheading:10202042-Cobra Venoms, pubmed-meshheading:10202042-Complement Inactivator Proteins, pubmed-meshheading:10202042-Endothelium, Vascular, pubmed-meshheading:10202042-Humans, pubmed-meshheading:10202042-Immune Complex Diseases, pubmed-meshheading:10202042-Immunohistochemistry, pubmed-meshheading:10202042-Infusions, Intravenous, pubmed-meshheading:10202042-Lewis Blood-Group System, pubmed-meshheading:10202042-Lung, pubmed-meshheading:10202042-Oligosaccharides, pubmed-meshheading:10202042-Protein Binding, pubmed-meshheading:10202042-Receptors, Complement 3b, pubmed-meshheading:10202042-Recombinant Proteins, pubmed-meshheading:10202042-Repetitive Sequences, Amino Acid, pubmed-meshheading:10202042-Sequence Deletion, pubmed-meshheading:10202042-Sequence Homology, Amino Acid
pubmed:year
1999
pubmed:articleTitle
Endothelial targeting and enhanced antiinflammatory effects of complement inhibitors possessing sialyl Lewisx moieties.
pubmed:affiliation
Department of Surgery and Pathology, University of Michigan Medical School, Ann Arbor 48109, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.