Linked Life Data

1847072

Source:http://linkedlifedata.com/resource/pubmed/id/1847072

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-3-15
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1682-91
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:1847072-Amino Acid Sequence, pubmed-meshheading:1847072-Binding, Competitive, pubmed-meshheading:1847072-Carboxypeptidase B, pubmed-meshheading:1847072-Carboxypeptidases, pubmed-meshheading:1847072-Cell Line, pubmed-meshheading:1847072-Cell Membrane, pubmed-meshheading:1847072-Flow Cytometry, pubmed-meshheading:1847072-Humans, pubmed-meshheading:1847072-Kinetics, pubmed-meshheading:1847072-Ligands, pubmed-meshheading:1847072-Lysine, pubmed-meshheading:1847072-Molecular Sequence Data, pubmed-meshheading:1847072-Molecular Weight, pubmed-meshheading:1847072-Peptides, pubmed-meshheading:1847072-Phosphopyruvate Hydratase, pubmed-meshheading:1847072-Plasminogen, pubmed-meshheading:1847072-Receptors, Cell Surface, pubmed-meshheading:1847072-Receptors, Urokinase Plasminogen Activator, pubmed-meshheading:1847072-Sequence Homology, Nucleic Acid
pubmed:year
1991
pubmed:articleTitle
Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor.
pubmed:affiliation
Committee on Vascular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.