| pubmed-article:1847072 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C0032140 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C2364020 | lld:lifeskim |
| pubmed-article:1847072 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1847072 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:1847072 | pubmed:dateCreated | 1991-3-15 | lld:pubmed |
| pubmed-article:1847072 | pubmed:abstractText | Plasminogen binding to cell surfaces results in enhanced plasminogen activation, localization of the proteolytic activity of plasmin on cell surfaces, and protection of plasmin from alpha 2-antiplasmin. We sought to characterize candidate plasminogen binding sites on nucleated cells, using the U937 monocytoid cell as a model, specifically focusing on the role of cell-surface proteins with appropriately placed lysine residues as candidate plasminogen receptors. Lysine derivatives with free alpha-carboxyl groups and peptides with carboxy-terminal lysyl residues were effective inhibitors of plasminogen binding to the cells. One of the peptides, representing the carboxy-terminal 19 amino acids of alpha 2-antiplasmin, was approximately 5-fold more effective than others with carboxy-terminal lysines. Thus, in addition to a carboxy-terminal lysyl residue, other structural features of the cell-surface proteins may influence their affinity for plasminogen. Affinity chromatography has been used to isolate candidate plasminogen receptors from U937 cells. A major protein of Mr 54,000 was recovered and identified as alpha-enolase by immunochemical and functional criteria. alpha-Enolase was present on the cell surface and was capable of binding plasminogen in ligand blotting analyses. Plasminogen binding activity of a molecular weight similar to alpha-enolase also was present in a variety of other cell types. Carboxypeptidase B treatment of alpha-enolase abolished its ability to bind plasminogen, consistent with the presence of a C-terminal lysyl residue. Thus, cell-surface proteins with carboxy-terminal lysyl residues appear to function as plasminogen binding sites, and alpha-enolase has been identified as a prominent representative of this class of receptors. | lld:pubmed |
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| pubmed-article:1847072 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1847072 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1847072 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1847072 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1847072 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1847072 | pubmed:author | pubmed-author:KatoKK | lld:pubmed |
| pubmed-article:1847072 | pubmed:author | pubmed-author:PlowE FEF | lld:pubmed |
| pubmed-article:1847072 | pubmed:author | pubmed-author:FelezJJ | lld:pubmed |
| pubmed-article:1847072 | pubmed:author | pubmed-author:MilesL ALA | lld:pubmed |
| pubmed-article:1847072 | pubmed:author | pubmed-author:PlesciaJJ | lld:pubmed |
| pubmed-article:1847072 | pubmed:author | pubmed-author:DahlbergC MCM | lld:pubmed |
| pubmed-article:1847072 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1847072 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:1847072 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:1847072 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1847072 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1847072 | pubmed:pagination | 1682-91 | lld:pubmed |
| pubmed-article:1847072 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:1847072 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1847072 | pubmed:articleTitle | Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. | lld:pubmed |
| pubmed-article:1847072 | pubmed:affiliation | Committee on Vascular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037. | lld:pubmed |
| pubmed-article:1847072 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1847072 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1847072 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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