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The interaction of metal ions and Marimastat with matrix metalloproteinase 9

C K Underwood1, D Min, J G Lyons

  • 1Centre for Heavy Metals Research, School of Chemistry, University of Sydney NSW, 2006 Australia.

Journal of Inorganic Biochemistry
|May 24, 2003
PubMed

Insights

Metal ions do not affect Marimastat

Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Matrix metalloproteinase 9 (MMP-9) is a key enzyme in tissue remodeling.
  • Marimastat is a broad-spectrum inhibitor of matrix metalloproteinases.
  • The influence of metal ions on MMP-9 activity and drug inhibition is not fully understood.

Purpose of the Study:

  • To investigate the impact of various metal ions on the inhibitory activity of Marimastat against MMP-9.
  • To determine if metal ions modulate MMP-9's enzymatic function independently of Marimastat.

Main Methods:

  • A fluorescence-based proteolytic assay was employed.
  • The assay measured MMP-9 activity in the presence and absence of Marimastat and different metal ions.
  • Various concentrations of metal ions including Zn(II), Fe(II), Cd(II), and Co(II) were tested.

Main Results:

  • None of the tested metal ions significantly altered Marimastat's ability to inhibit MMP-9.
  • Zinc (Zn(II)) and Iron (Fe(II)) ions inhibited MMP-9 activity at 10 and 100 microM, respectively.
  • Cadmium (Cd(II)) inhibited MMP-9 at 100 microM, both with and without Marimastat.
  • Cobalt (Co(II)) at 1 mM significantly upregulated MMP-9 proteolytic activity.

Conclusions:

  • Marimastat's efficacy against MMP-9 is not compromised by the presence of common metal ions.
  • Specific metal ions can directly modulate MMP-9 activity, either inhibiting or upregulating its function.
  • These findings highlight the complex interplay between metal ions, MMP-9, and potential therapeutic inhibitors.

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