Interaction of plasminogen-related protein B with endothelial and smooth muscle cells in vitro

Hideo Morioka, Takeshi Morii, Tikva Vogel, Francis J. Hornicek, Lawrence Weissbach

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Plasminogen-related protein B (PRP-B) closely resembles the N-terminal plasminogen activation peptide, which is released from plasminogen during conversion to plasmin. We have previously demonstrated that the steady-state level of mRNA encoding PRP-B is increased within tumor tissues, and that recombinant PRP-B antagonizes neoplastic growth when administered systemically to mice harboring tumors, but no insights into the cell targets of PRP-B have been presented. Employing serum-free medium optimized for culturing human endothelial or smooth muscle cells, we show that recombinant PRP-B inhibits basic fibroblast growth factor-dependent cell migration for both cell types, as well as tube formation of endothelial cells. Comparison with the angiogenesis inhibitors angiostatin and endostatin revealed similar results. Recombinant PRP-B is effective in promoting cell attachment of endothelial and smooth muscle cells, and antibody interference experiments reveal that the interaction of recombinant PRP-B with endothelial cells is mediated at least in part by αv-containing integrins. Inhibition of angiogenesis in vivo by PRP-B was demonstrated in the chicken chorioallantoic membrane assay. PRP-B and other antiangiogenic molecules may elicit metabolic perturbations in endothelial cells as well as perivascular mesenchymal cells such as smooth muscle cells and pericytes.

Original languageEnglish
Pages (from-to)166-177
Number of pages12
JournalExperimental Cell Research
Issue number1
Publication statusPublished - 2003 Jul 1


  • Antiangiogenesis
  • Basic fibroblast growth factor
  • Endothelial cell
  • Mural cell
  • Plasminogen-related protein B

ASJC Scopus subject areas

  • Cell Biology


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