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Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor

Academic Article
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Overview

authors

  • Miles, Lindsey
  • Dahlberg, C. M.
  • Plescia, J.
  • Felez, J.
  • Kato, K.
  • Plow, E. F.

publication date

  • February 1991

journal

  • Biochemistry  Journal

abstract

  • 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.

subject areas

  • Amino Acid Sequence
  • Binding, Competitive
  • Carboxypeptidase B
  • Carboxypeptidases
  • Cell Line
  • Cell Membrane
  • Flow Cytometry
  • Humans
  • Kinetics
  • Ligands
  • Lysine
  • Molecular Sequence Data
  • Molecular Weight
  • Peptides
  • Phosphopyruvate Hydratase
  • Plasminogen
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • Sequence Homology, Nucleic Acid
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00220a034

PubMed ID

  • 1847072
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Additional Document Info

start page

  • 1682

end page

  • 1691

volume

  • 30

issue

  • 6

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