Human glioma cell BT325 expresses a proteinase that converts human plasminogen to kringle 1-5-containing fragments

Fuyang Li, Jinghua Yang, Xinping Liu, Peng He, Shaoping Ji, Jicun Wang, Jiong Han, Nanchun Chen, Libo Yao

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Angiostatin, a specific angiogenesis inhibitor, is an internal fragment of plasminogen, and can be generated in many systems mediated by different enzymes in vitro. The mechanism of angiostatin generation in vivo has not been well defined. Here we demonstrated that human glioma cell line BT325 can express an enzyme that can convert purified plasminogen to angiostatin-like fragments with molecular masses of 65, 60, and 58 kDa, respectively. These fragments have an identical N-terminal as KVYLS, which starts from Lys98 of the plasminogen precusor. According to their molecular mass, the three fragments should comprise kringle domain 1 to kringle domain 5 (kringle 1-5). The proteolytic fragments obtained as above can inhibit the growth of bovine aortic endothelial (BAE) cells specifically. The proteolysis process can be completely inhibited by serine proteinase inhibitors, and partially inhibited by EDTA. The molecular weight of the peptide, which contains an enzymatic activity responsible for the proteolysis, was 13 kD determined by gel filtration and SDS-PAGE. The present data suggest that glioma cell BT325 can produce a novel proteinase to generate kringle 1-5 of plasminogen as an angiogenesis inhibitor. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)821-825
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Nov 30 2000


  • Angiogenesis
  • Angiogenesis inhibitor
  • Angiostatin
  • BT325
  • Glioma cell
  • Plasminogen
  • Protease
  • Tumor cell

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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