Linked Life Data

8605924

Source:http://linkedlifedata.com/resource/pubmed/id/8605924

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-5-20
pubmed:abstractText
The human cell surface complement regulatory proteins CD46 (MCP), CD55 (DAF) and CD35 (CR1) protect autologous cells from complement-mediated damage by inhibiting C3 and C5 convertases. This regulatory potential has previously been exploited in the treatment of some models of inflammatory injury by the generation of recombinant soluble (rs) proteins, such as rsCD55 and rsCD35 . More recently, we have shown that rsCD46 inhibits complement activation in the fluid phase. In this report, the ability of rsCD46, rsD55 and rsCD35 to regulate human complement activation mediated by the classical pathway in vitro was clearly demonstrated by all three soluble proteins; however, rsCD35 was a more effective inhibitor than either rsCD46 or rsCD55. A combination of rsCD46+ rsCD55 was more potent than either of these proteins alone. Cell lysis via alternative pathway activation in vitro was efficiently regulated by rsCD46 and rsCD35 to a similar extent, whereas rsCD55 was not effective. Assays of rsCD46 in vivo have previously not been possible due to difficulties in expressing sufficient quantities of protein. This limitation has been overcome and now we report the ability of rsCD46 to inhibit immune complex-mediated inflammation in a rat using the reverse passive Arthus reaction model. Administration of rsCD46 significantly reduced the size of lesion, and histological examination showed a reduction in inflammatory infiltrate and edema. These data suggest that rsCD46, in addition to rsCd55 and rsCD35, may be useful a therapeutic agent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
578-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8605924-Animals, pubmed-meshheading:8605924-Antigens, CD, pubmed-meshheading:8605924-Antigens, CD46, pubmed-meshheading:8605924-Antigens, CD55, pubmed-meshheading:8605924-Arthus Reaction, pubmed-meshheading:8605924-Base Sequence, pubmed-meshheading:8605924-Cell Line, pubmed-meshheading:8605924-Complement Inactivator Proteins, pubmed-meshheading:8605924-Complement Pathway, Alternative, pubmed-meshheading:8605924-Complement Pathway, Classical, pubmed-meshheading:8605924-Drug Combinations, pubmed-meshheading:8605924-Humans, pubmed-meshheading:8605924-Membrane Glycoproteins, pubmed-meshheading:8605924-Molecular Sequence Data, pubmed-meshheading:8605924-Rats, pubmed-meshheading:8605924-Receptors, Complement 3b, pubmed-meshheading:8605924-Recombinant Proteins, pubmed-meshheading:8605924-Solubility
pubmed:year
1996
pubmed:articleTitle
A functional analysis of recombinant soluble CD46 in vivo and a comparison with recombinant soluble forms of CD55 and CD35 in vitro.
pubmed:affiliation
The Austin Research Institute, Heidelberg, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't