Endostatin binds to the catalytic domain of matrix metalloproteinase-2

Seo Jin Lee, Jin Wook Jang, Young Mi Kim, Hyun Ick Lee, Jun Yung Jeon, Young Guen Kwon, Seung Taek Lee

Research output: Contribution to journalArticle

105 Citations (Scopus)


We previously reported that endostatin inhibits endothelial and tumor cellular invasion by blocking activation and catalytic activity of matrix metalloproteinase (MMP)-2. Here we have examined the domain of proMMP-2 responsible for the binding of endostatin using surface plasmon resonance. ProMMP-2 and proMMP-2ΔHP lacking the hinge and hemopexin-like (HP) domains bound little to the immobilized endostatin. The active MMP-2 and MMP-2ΔHP, but not the HP domain of MMP-2, bound to endostatin at similar levels. In addition, preincubation of MMP-2 and MMP-2ΔHP with the MMP inhibitor actinonin, which binds to the active site of MMP-2, abolished their bindings to endostatin. These results indicate that endostatin binds to neither the latent proMMP-2 nor the HP domain but to the catalytic domain of MMP-2.

Original languageEnglish
Pages (from-to)147-152
Number of pages6
JournalFEBS Letters
Issue number1-3
Publication statusPublished - 2002 May 22

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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