Title page for etd-0701109-185811


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URN etd-0701109-185811
Author Wen-min Chou
Author's Email Address No Public.
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Department Institute of Biomedical Sciences
Year 2008
Semester 2
Degree Master
Type of Document
Language zh-TW.Big5 Chinese
Title Studies on the inhibitory activity of Bungarus multicinctus PILPs on matrix metalloproteinase-2 (MMP-2)
Date of Defense 2009-06-29
Page Count 65
Keyword
  • migration
  • matrix metalloproteinase 2
  • Kunitz-type proteinase inhibitor
  • invasion
  • Protease inhibitor-like protein
  • Abstract Three protease inhibitor-like proteins (PILPs) identified from Bungarus multicinctus genome are structurally homologous with Kunitz-type proteinase inhibitor. The goal of the present study is to explore whether PILPs exhibit an inhibitory action on matrix metalloproteinase 2 (MMP-2) activity. Unlike PILP-1 and PILP-2, PILP-3 was found to inhibit MMP-2 activity as evidenced by specific substrate assay. Moreover, in vitro migration and invasion assays, and wound-healing assay showed that PILP-3 suppressed the migration and invasion of human neuroblastoma SK-N-SH cells.  Pull-down assay and dot blotting-binding assay proved an interaction between PILP-3 and MMP-2. Nevertheless, PILP-3 did not affect either expression or secretion of MMP-2 in SK-N-SH cells. In terms of highly structural similarity between PILP-2 and PILP-3, two chimeric mutants in which amino acids at N-terminus and C-terminus of PILP-3 were substituted by those of PILP-2 were prepared. In contrast to N-terminus chimera, C-terminus mutant of PILP-3 was unable to inhibit MMP-2 activity and showed a reduction in binding with MMP-2. Taken together, our data suggest that PILP-3 may be a useful template for rational designing pharmaceutical agent in inhibiting MMP-2 activity.
    Advisory Committee
  • Chun-Chang Chang - chair
  • Shinne-Ren Lin - co-chair
  • Long-Sen Chang - advisor
  • Files
  • etd-0701109-185811.pdf
  • indicate accessible in a year
    Date of Submission 2009-07-01

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