Natural inhibitors of metalloproteinases from fungi and herbs – new bioactive extracts of pharmacological potential

Authors

  • Krzysztof Grzywnowicz Department of Biochemistry, Maria Curie-Skłodowska University Author
  • Daniel Załuski Chair and Department of Pharmaceutical Botany, Medical University of Lublin Author
  • Tadeusz Walczyński Department of Biochemistry, Maria Curie-Skłodowska University Author
  • Monika Prendecka Department of Biochemistry, Maria Curie-Skłodowska University Author
  • Helena Smolarz Chair and Department of Pharmaceutical Botany, Medical University of Lublin Author

Keywords:

wood rotting fungi, herbs, metalloproteinase inhibitors, matrix metalloproteinases, MMPs

Abstract

Novel metalloproteinase inhibitors were extracted from the fruit bodies of a few wood rotting fungi and some herbs. Fractions active against metalloproteases was extracted with chloroform and, for comparison, with other organic solvents. Their inhibitory parameters were characterized against gelatinase and collagenase activities. In the course of searching for potential pharmacological activities, inhibition of MMP1, MMP2, MMP3 and MMP9 were analyzed. The obtained results suggest that isolated substances are similar to berberine (substances from herbs) and polyporenic acids from Piptoporus betulinus (substances from wood rotting fungi). They are very promising bioactive substances (few extracts are really very active, in comparison with literature data).

References

1. Baker A.H., Edwards D.R., Murphy G.: Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci., 115, 3719, 2002.

2. Barros I.F.M., Barros P.S.M., Ropke C.D. et al.: Dose dependent in vitro inhibition of rabbit corneal matrix metalloproteinases by an extract of Pothomorphe umbellata after alkali injury. Brazil. J. Med. Biol. Res., 40, 1129, 2007.

3. Bode W., Huber R.: Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem., 204, 433, 1992.

4. Bode W., Huber R.: Structural basis of the endoproteinase-protein inhibitor interaction. Biochim. Biophys. Acta, 1477, 241, 2000.

5. Frederics W.M., Mook O.R.F.: Metabolic mapping of proteinase activity with emphasis on in situ zymography of gelatinases: review and protocols. J. Histochem., 52, 711, 2004.

6. Grimm T., Schafer A., Hogger P.: Antioxidant activity and inhibition of matrix metalloproteinases by metabolites of maritime pine bark extract. Free Radic. Biol. Med., 36, 811, 2004.

7. Kawagishi H., Hamajima K., Inoue Y.: Novel hydroquinone as a matrix metallo-proteinase inhibitor from the mushroom Piptoporus betulinus. Biosci. Biotechnol. Biochem., 66, 2748, 2002.

8. Kim W.J., Hong S.C., Do E.J. et al.: Keumsa linteusan suppresses invasion of cancer cells through the inhibition of cellular adhesion and MMP-9 expression. Animal Cells Systems, 13, 113, 2009.

9. Lee T-M., Lin Y-H.: Trypsin inhibitor and trypsin-like protease activity in air- or submergence-grown rice (Oryza sativa L.) coleoptiles. Plant Sci., 106, 43, 1995.

10. Lombard C., Saulnier J., Wallach J.: Assays of matrix metalloproteinases (MMPs) activities: a review. Biochimie, 87, 265, 2005.

11. Rawlings N.D., Tolle D.P., Barrett A.J.: Evolutionary families of peptidase inhibitors. Biochem. J., 378, 705, 2004.

12. Vayalil P.K., Mittal A., Hara Y. et al.: Green tea polyphenols prevent ultraviolet-induced oxidative damage and matrix metalloproteinase expression in mouse skin. J. Invest. Dermatol., 122,1480, 2004.

13. Weng C.J., Chau C.F., Yen, G.C. et al.: Inhibitory effects of Ganoderma lucidum on tumorigenesis and metastasis of human hepatoma cells in cells and animal models. J. Food Agricult. Food Chem., 5049, 2009.

Downloads

Published

2025-04-09

How to Cite

Grzywnowicz, K., Załuski, D., Walczyński, T., Prendecka, M., & Smolarz, H. (2025). Natural inhibitors of metalloproteinases from fungi and herbs – new bioactive extracts of pharmacological potential. Current Issues in Pharmacy and Medical Sciences, 23(2), 41-45. https://czasopisma.umlub.pl/curipms/article/view/2862