Matrix metalloproteinases generate angiostatin: effects on neovascularization

J Immunol. 1998 Dec 15;161(12):6845-52.

Abstract

Angiostatin, a cleavage product of plasminogen, has been shown to inhibit endothelial cell proliferation and metastatic tumor cell growth. Recently, the production of angiostatin has been correlated with tumor-associated macrophage production of elastolytic metalloproteinases in a murine model of Lewis lung cell carcinoma. In this report we demonstrate that purified murine and human matrix metalloproteinases generate biologically functional angiostatin from plasminogen. Macrophage elastase (MMP-12 or MME) proved to be the most efficient angiostatin-producing MMP. MME was followed by gelatinases and then the stomelysins in catalytic efficiency; interstitial collagenases had little capacity to generate angiostatin. Both recombinant angiostatin and angiostatin generated from recombinant MME-treated plasminogen inhibited human microvascular endothelial cell proliferation and differentiation in vitro. Finally, employing macrophages isolated from MME-deficient mice and their wild-type littermates, we demonstrate that MME is required for the generation of angiostatin that inhibits the proliferation of human microvascular endothelial cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amides / pharmacology
  • Angiostatins
  • Animals
  • Cells, Cultured
  • Culture Media, Conditioned / pharmacology
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / drug effects
  • Fibroblast Growth Factor 2 / pharmacology
  • Gelatinases / pharmacology
  • Gene Expression Regulation / drug effects*
  • Humans
  • Macrophages, Peritoneal / metabolism
  • Matrix Metalloproteinase 12
  • Matrix Metalloproteinase 3 / pharmacology
  • Metalloendopeptidases / antagonists & inhibitors
  • Metalloendopeptidases / deficiency
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / pharmacology*
  • Mice
  • Mice, Knockout
  • Neovascularization, Physiologic / drug effects*
  • Peptide Fragments / biosynthesis*
  • Peptide Fragments / genetics
  • Plasminogen / biosynthesis*
  • Plasminogen / drug effects
  • Plasminogen / genetics
  • Plasminogen / metabolism
  • Plasminogen / pharmacology
  • Protease Inhibitors / pharmacology
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Tyrosine / analogs & derivatives
  • Tyrosine / pharmacology

Substances

  • Amides
  • Culture Media, Conditioned
  • Peptide Fragments
  • Protease Inhibitors
  • Recombinant Fusion Proteins
  • Fibroblast Growth Factor 2
  • N-(2-isobutyl-3-(N'-hydroxycarbonylamido)propanoyl)-O-methyltyrosinemethylamide
  • Tyrosine
  • Angiostatins
  • Plasminogen
  • Gelatinases
  • Metalloendopeptidases
  • Matrix Metalloproteinase 3
  • MMP12 protein, human
  • Matrix Metalloproteinase 12