| pubmed-article:2430040 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2430040 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2430040 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:2430040 | lifeskim:mentions | umls-concept:C1413694 | lld:lifeskim |
| pubmed-article:2430040 | lifeskim:mentions | umls-concept:C0034793 | lld:lifeskim |
| pubmed-article:2430040 | lifeskim:mentions | umls-concept:C1413000 | lld:lifeskim |
| pubmed-article:2430040 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2430040 | pubmed:dateCreated | 1986-12-3 | lld:pubmed |
| pubmed-article:2430040 | pubmed:abstractText | Activation of the classical complement pathway on the membrane of autologous cells results in the deposition of C4b on their surface and in the assembly of the C3 convertase C4b2a, one of the amplifying enzymes of the cascade. Here we study the sequence of events leading to irreversible inactivation of the potentially harmful C4b bound to human red cells. We show that deposited C4b interacts endogenously with complement receptor type 1 (CR1) present on the membrane of the same red cell. Complexes containing CR1 and C4b are found in extracts of membranes of C4b-bearing red cells after treatment of the intact cells with a bifunctional crosslinking reagent. The amount of complexed CR1 increases with the number of deposited C4b molecules. Only small amounts of free CR1 are observed on red cells bearing as few as 1,900 molecules of C4b, suggesting that the binding avidity between C4b and endogenous CR1 is high. In agreement with this observation, we find that the deposited C4b inhibits the exogenous cofactor activity of the red cell CR1 for the factor I-mediated cleavage of target-bound clustered C3b. The C4b bound to the human red cells is cleaved by the serum enzyme C3b/C4b inactivator (factor I) and a large fragment (C4c) is released in the incubation medium. The cleavage is totally inhibited by mAbs against CR1, showing that the complement receptor is an essential cofactor for the activity of I. When the number of bound C4b per red cell is relatively small (less than 1,000 molecules) the substrate for the enzymatic activity of factor I is mostly or exclusively the C4b bound endogenously to CR1. Indeed, the kinetics or the extent of cleavage of C4b are not affected by greatly augmenting the concentration of exogenous CR1 or of C4b-bearing red cells in the incubation mixture, thereby increasing the frequency of collisions between CR1 on the surface of one cell with C4b deposited on the membrane of a different cell. On the basis of the present and prior observations, we speculate that both DAF and CR1 act endogenously to inactivate the function of autologous red cell-bound C4b and prevent the progression of the cascade. DAF binding prevents the formation of the C3 convertase, C4b2a. The cleavage and irreversible inactivation of C4b only occurs after the concerted activities of endogenous CR1 and serum factor I.(ABSTRACT TRUNCATED AT 400 WORDS) | lld:pubmed |
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| pubmed-article:2430040 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2430040 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2430040 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2430040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2430040 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2430040 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2430040 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:2430040 | pubmed:author | pubmed-author:MedofM EME | lld:pubmed |
| pubmed-article:2430040 | pubmed:author | pubmed-author:HoodWW | lld:pubmed |
| pubmed-article:2430040 | pubmed:author | pubmed-author:NussenzweigVV | lld:pubmed |
| pubmed-article:2430040 | pubmed:author | pubmed-author:KinoshitaTT | lld:pubmed |
| pubmed-article:2430040 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2430040 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2430040 | pubmed:volume | 164 | lld:pubmed |
| pubmed-article:2430040 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2430040 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2430040 | pubmed:pagination | 1377-88 | lld:pubmed |
| pubmed-article:2430040 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2430040 | pubmed:meshHeading | pubmed-meshheading:2430040-... | lld:pubmed |
| pubmed-article:2430040 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2430040 | pubmed:articleTitle | Membrane-bound C4b interacts endogenously with complement receptor CR1 of human red cells. | lld:pubmed |
| pubmed-article:2430040 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2430040 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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