Human prostate carcinoma cells express enzymatic activity that converts human plasminogen to the angiogenesis inhibitor, angiostatin

Stephen Gately, Przemyslaw Twardowski, M. Sharon Stack, Matthew Patrick, Lisa Boggio, Deborah L. Cundiff, H. William Schnaper, Laird Madison, Olga Volpert, Noel Bouck, Jan Enghild, Hau C. Kwaan, Gerald A. Soff*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

196 Scopus citations

Abstract

Angiostatin is an inhibitor of angiogenesis and metastatic growth that is found in tumor-bearing animals and can be generated in vitro by the proteolytic cleavage of plasminogen. The mechanism by which angiostatin is produced in vivo has not been defined. We now demonstrate that human prostate carcinoma cell lines (PC-3, DU-145, and LN-CaP) express enzymatic activity that can generate bioactive angiostatin from purified human plasminogen or plasmin. Affinity purified PC-3-derived angiostatin inhibited human endothelial cell proliferation, basic fibroblast growth factor-induced migration, endothelial cell tube formation, and basic fibroblast growth factor-induced corneal angiogenesis. Studies with proteinase inhibitors demonstrated that a serine proteinase is necessary for angiostatin generation. These data indicate that bioactive angiostatin can be generated directly by human prostate cancer cells and that serine proteinase activity is necessary for angiostatin generation.

Original languageEnglish (US)
Pages (from-to)4887-4890
Number of pages4
JournalCancer Research
Volume56
Issue number21
StatePublished - Nov 1 1996

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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