| pubmed-article:2481448 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2481448 | lifeskim:mentions | umls-concept:C0009498 | lld:lifeskim |
| pubmed-article:2481448 | lifeskim:mentions | umls-concept:C0285488 | lld:lifeskim |
| pubmed-article:2481448 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:2481448 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:2481448 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2481448 | pubmed:dateCreated | 1990-2-6 | lld:pubmed |
| pubmed-article:2481448 | pubmed:abstractText | Membrane cofactor protein (MCP or gp45-70) of the complement system is a cofactor for factor I-mediated cleavage of fluid-phase C3b and C3b-like C3, which opens the thioester bond. In the present study the activity of MCP was further characterized. Unexpectedly, in the absence of factor I, MCP stabilized the alternative- and, to a lesser extent, the classical-pathway cell-bound C3 convertases and thereby enhanced C3b deposition. Soluble MCP, if added exogenously, hardly functioned as cofactor for the cleavage of erythrocyte-bound C3b to iC3b; i.e. its activity, compared with the cofactor activity of factor H, was inefficient, since less than 10% of the bound C3b was MCP-sensitive. Further, exogenously added soluble MCP was also a weak cofactor for the cleavage of C3b bound to zymosan. Likewise, factor I, in the presence of cells bearing MCP, cleaved fluid-phase C3b inefficiently. These results imply that MCP has very little extrinsic cofactor activity for factor I. In contrast, exogenously added MCP and factor I mediated efficient cleavage of erythrocyte-bound C3b if the concentration of Nonidet P40 was sufficient to solubilize the cells. Interestingly, soluble MCP and factor I degraded C3b attached to certain solubilized acceptor membrane molecules more readily than others. The cleavage reaction of fluid-phase and cell-bound C3b by soluble MCP and factor I produced iC3b, but no C3c and C3dg. These and prior data indicate that soluble MCP has potent cofactor activity for fluid-phase C3b or C3b bound to solubilized molecules, but acts inefficiently towards C3b on other cells. This functional profile is unique for a C3b/C4b binding protein and, taken together with its wide tissue distribution, suggests an important role for MCP in the regulation of the complement system. | lld:pubmed |
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| pubmed-article:2481448 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2481448 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2481448 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2481448 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2481448 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2481448 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2481448 | pubmed:author | pubmed-author:AtkinsonJ PJP | lld:pubmed |
| pubmed-article:2481448 | pubmed:author | pubmed-author:SeyaTT | lld:pubmed |
| pubmed-article:2481448 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2481448 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2481448 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2481448 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2481448 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2481448 | pubmed:pagination | 581-8 | lld:pubmed |
| pubmed-article:2481448 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2481448 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2481448 | pubmed:articleTitle | Functional properties of membrane cofactor protein of complement. | lld:pubmed |
| pubmed-article:2481448 | pubmed:affiliation | Department of Immunology, Center for Adult Diseases, Osaka, Japan. | lld:pubmed |
| pubmed-article:2481448 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2481448 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2481448 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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