| pubmed-article:8573103 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C0128897 | lld:lifeskim |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:8573103 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:8573103 | pubmed:dateCreated | 1996-3-1 | lld:pubmed |
| pubmed-article:8573103 | pubmed:abstractText | Monocyte chemoattractant protein-1 (MCP-1) mediates monocyte migration into tissues in inflammatory diseases and atherosclerosis. We have investigated structure-activity relationships for human MCP-1. Mutations were introduced based upon differences between MCP-1 and the structurally related but functionally distinct molecule interleukin-8 (IL-8). Mutant proteins produced using the baculovirus/insect cell expression system were purified and their ability to stimulate monocyte chemotaxis and elevation of intracellular calcium in THP-1 monocytic leukaemia cells was measured. Two regions in MCP-1 were identified as important for its biological activity. One region consists of the sequence Thr-Cys-Cys-Tyr (amino acids 10-13). Point mutations of Thr-10 to Arg and Tyr-13 to Ile greatly lowered MCP-1 activity. The second functionally important region is formed by Ser-34 and Lys-35. Insertion of a Pro between these two residues, or their substitution by the sequence Gly-Pro-His, caused nearly complete loss of MCP-1 activity. Competition binding experiments showed that the mutations that affected activity also lowered the ability to compete with wild-type MCP-1 for receptors on THP-1 cells. Point mutations at positions 8, 15, 30, 37, 38 and 68 had little effect on MCP-1 activity. The important regions that we have identified in MCP-1 correspond with previously identified functionally important regions of IL-8, suggesting that the two molecules bind to their respective receptors by similar contacts. | lld:pubmed |
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| pubmed-article:8573103 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8573103 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8573103 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8573103 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8573103 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8573103 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8573103 | pubmed:author | pubmed-author:KolattukudyP... | lld:pubmed |
| pubmed-article:8573103 | pubmed:author | pubmed-author:MahajanSS | lld:pubmed |
| pubmed-article:8573103 | pubmed:author | pubmed-author:KoppJ SJS | lld:pubmed |
| pubmed-article:8573103 | pubmed:author | pubmed-author:BehunMM | lld:pubmed |
| pubmed-article:8573103 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8573103 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8573103 | pubmed:volume | 313 ( Pt 2) | lld:pubmed |
| pubmed-article:8573103 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8573103 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8573103 | pubmed:pagination | 633-40 | lld:pubmed |
| pubmed-article:8573103 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8573103 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8573103 | pubmed:articleTitle | Site-directed mutagenesis of monocyte chemoattractant protein-1 identifies two regions of the polypeptide essential for biological activity. | lld:pubmed |
| pubmed-article:8573103 | pubmed:affiliation | Neurobiotechnology Center, Ohio State University, Columbus 43210, USA. | lld:pubmed |
| pubmed-article:8573103 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8573103 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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