| pubmed-article:9759896 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9759896 | lifeskim:mentions | umls-concept:C0009498 | lld:lifeskim |
| pubmed-article:9759896 | lifeskim:mentions | umls-concept:C0285488 | lld:lifeskim |
| pubmed-article:9759896 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9759896 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:9759896 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9759896 | pubmed:dateCreated | 1998-10-22 | lld:pubmed |
| pubmed-article:9759896 | pubmed:abstractText | Membrane cofactor protein (MCP; CD46) is a type 1 membrane glycoprotein that inhibits complement activation on host cells. It also is a measles virus (MV) receptor, an adherence factor for group A Streptococcus pyogenes, and a cellular pilus receptor for pathogenic Neisseria. The amino terminus of MCP consists of four complement control protein (CCP) repeats, three of which (CCP-1, -2, and -4) possess N-glycans. Immediately following the CCP modules is an alternatively spliced region for extensive O-glycosylation (termed the STP domain). Previous studies established that the N-glycan of CCP-2 is essential for MV binding and infection and that the splicing variants of the STP domain not only affect MV binding and fusion, but also differentially protect against complement-mediated cytolysis. In this report, we dissect the role of these carbohydrates on complement regulatory function. We constructed, expressed, and characterized proteins deleting these carbohydrates. For MCP-mediated protection against cytolysis, the N-glycans of CCP-2 and -4 were necessary, the STP segment influenced but was not essential, and the N-glycan of CCP-1 was not required. In addition, the rate and magnitude of cell surface cleavage of C4b to C4c and C4d by MCP and factor I correlated with cytoprotection. These studies expand the structure-function understanding of the active sites of MCP and elucidate an important role for carbohydrates in its function, a finding consistent with their conservation in the MCP of other species. | lld:pubmed |
| pubmed-article:9759896 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9759896 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9759896 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9759896 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:9759896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9759896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9759896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9759896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9759896 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9759896 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9759896 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:9759896 | pubmed:author | pubmed-author:AtkinsonJ PJP | lld:pubmed |
| pubmed-article:9759896 | pubmed:author | pubmed-author:LeungM KMK | lld:pubmed |
| pubmed-article:9759896 | pubmed:author | pubmed-author:LiszewskiM... | lld:pubmed |
| pubmed-article:9759896 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9759896 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9759896 | pubmed:volume | 161 | lld:pubmed |
| pubmed-article:9759896 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9759896 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9759896 | pubmed:pagination | 3711-8 | lld:pubmed |
| pubmed-article:9759896 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9759896 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9759896 | pubmed:articleTitle | Membrane cofactor protein: importance of N- and O-glycosylation for complement regulatory function. | lld:pubmed |
| pubmed-article:9759896 | pubmed:affiliation | Division of Rheumatology, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:9759896 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9759896 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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