Purification of the plasmin receptor from human carcinoma cells and comparison to alpha-enolase.
We have characterized a receptor for plasmin (Pli-R) from a human tumor cell line, MCF7MF. The Pli-R was purified from a MCF7 0.1% Triton X-100 solubilisate by affinity chromatography. A protein of 55-60 kDa was obtained, which bound plasminogen and plasmin specifically. Chemical cross-linking of M(r) 90 kDa [125I]-Pli to the surface of MCF7 cells with DSP results in the formation of a labelled complex of M(r) 145 kDa, suggesting a M(r) of 55-60 kDa for the receptor. Comparing Pli-R with alpha-enolase (a candidate for plasminogen receptor in U937 cells) we have found a high homology between both proteins, but not an identity.
Lopez-Alemany
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Immunopathologie de l'oeil, INSERM U 86, Paris, France.
Correc
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P
Camoin
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Burtin
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001943:Breast Neoplasms / Q000097:blood* / Q000201:enzymology; D003432:Cross-Linking Reagents; D006801:Humans; D008969:Molecular Sequence Data; D010751:Phosphopyruvate Hydratase / Q000032:analysis*; D018000:Receptors, Peptide / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid; D014407:Tumor Cells, Cultured
D000596:Amino Acids; D003432:Cross-Linking Reagents; D018000:Receptors, Peptide; C065181:plasmin receptor; D010751:Phosphopyruvate Hydratase