Homeopathy 2012; 101(02): 92-98
DOI: 10.1016/j.homp.2012.02.003
Original Paper
Copyright © The Faculty of Homeopathy 2012

Effects of Calendula officinalis on human gingival fibroblasts

Pragtipal Saini
1   Department of Periodontics, Indiana University School of Dentistry, 1121 West Michigan Street, DS 423, Indianapolis, IN 46202, USA
,
Nouf Al-Shibani
2   Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan Street, DS 271, Indianapolis, IN 46202, USA
,
Jun Sun
2   Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan Street, DS 271, Indianapolis, IN 46202, USA
,
Weiping Zhang
2   Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan Street, DS 271, Indianapolis, IN 46202, USA
,
Fengyu Song
2   Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan Street, DS 271, Indianapolis, IN 46202, USA
,
Karen S. Gregson
2   Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan Street, DS 271, Indianapolis, IN 46202, USA
,
L. Jack Windsor
2   Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan Street, DS 271, Indianapolis, IN 46202, USA
› Institutsangaben

Verantwortlicher Herausgeber dieser Rubrik:
Weitere Informationen

Publikationsverlauf

Received14. Mai 2010
revised10. Januar 2012

accepted06. Februar 2012

Publikationsdatum:
29. Dezember 2017 (online)

Background: Calendula officinalis is commonly called the marigold. It is a staple topical remedy in homeopathic medicine. It is rich in quercetin, carotenoids, lutein, lycopene, rutin, ubiquinone, xanthophylls, and other anti-oxidants. It has anti-inflammatory properties. Quercetin, one of the active components in Calendula, has been shown to inhibit recombinant human matrix metalloproteinase (MMP) activity and decrease the expression of tumor necrosis factor-α, interleukin-1β (IL), IL-6 and IL-8 in phorbol 12-myristate 13-acetate and calcium ionophore-stimulated human mast cells.

Objectives: To examine the effects of Calendula on human gingival fibroblast (HGF) mediated collagen degradation and MMP activity.

Material and methods: Lactate dehydrogenate assays were performed to determine the non-toxic concentrations of Calendula, doxycycline and quercetin. Cell-mediated collagen degradation assays were performed to examine the inhibitory effect on cell-mediated collagen degradation. Gelatin zymography was performed to examine their effects on MMP-2 activity. The experiments were repeated three times and ANOVA used for statistical analyses.

Results: Calendula at 2–3% completely inhibited the MMP-2 activity in the zymograms. Doxycycline inhibited HGF-mediated collagen degradation at 0.005, 0.01, 0.02 and 0.05%, and MMP-2 activity completely at 0.05%. Quercetin inhibited HGF-mediated collagen degradation at 0.005, 0.01 and 0.02%, and MMP-2 activity in a dose-dependent manner. Calendula inhibited HGF-mediated collagen degradation and MMP-2 activity more than the same correlated concentration of pure quercetin.

Conclusion: Calendula inhibits HGF-mediated collagen degradation and MMP-2 activity more than the corresponding concentration of quercetin. This may be attributed to additional components in Calendula other than quercetin.

 
  • References

  • 1 D’Huyvetter K., Cohrssen A. Homeopathy. Prim Care 2002; 29 (02) 407-418 viii.
  • 2 Basch E., Bent S., Foppa I. et al. Marigold (Calendula officinalis L.): an evidence-based systematic review by the Natural Standard Research Collaboration. J Herb Pharmacother 2006; 6 (03/04) 135-159.
  • 3 Ukiya M., Akihisa T., Yasukawa K. et al. Anti-inflammatory, anti-tumor-promoting, and cytotoxic activities of constituents of marigold (Calendula officinalis) flowers. J Nat Prod 2006; 69 (12) 1692-1696.
  • 4 Machado M.A., Contar C.M., Brustolim J.A. et al. Management of two cases of desquamative gingivitis with clobetasol and Calendula officinalis gel. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub 2010; 154 (04) 335-338.
  • 5 Preethi K.C., Kuttan G., Kuttan R. Anti-inflammatory activity of flower extract of Calendula officinalis Linn. and its possible mechanism of action. Indian J Exp Biol 2009; 47 (02) 113-120.
  • 6 Pommier P., Gomez F., Sunyack M.P. et al. Phase III randomized trial of Calendula officinalis compared with trolamine for the prevention of acute dermatitis during irradiation for breast cancer. J Clin Oncol 2004; 22 (08) 1447-1453.
  • 7 Lievre M., Marichy J., Baux S. Controlled study of three ointments for the local management of 2nd and 3rd degree burns. Clin Trials Metaanal 1992; 28: 9-12.
  • 8 Della Loggia R., Tubaro A., Sosa S. et al. The role of triterpenoids in the topical anti-inflammatory activity of Calendula officinalis flowers. Planta Med 1994; 60 (06) 516-520.
  • 9 Min Y.D., Choi C.H., Bark H. et al. Quercetin inhibits expression of inflammatory cytokines through attenuation of NF-kappaB and p38 MAPK in HMC-1 human mast cell line. Inflamm Res 2007; 56 (05) 210-215.
  • 10 Lim H., Kim H.P. Inhibition of mammalian collagenase, matrix metalloproteinase-1, by naturally-occurring flavonoids. Planta Med 2007; 73 (12) 1267-1274.
  • 11 Preethi K.C., Siveen K.S., Kuttan R. et al. Inhibition of metastasis of B16F-10 melanoma cells in C57BL/6 mice by an extract of Calendula officinalis L flowers. Asian Pac J Cancer Prev 2010; 11 (06) 1773-1779.
  • 12 Visse R., Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 2003; 92 (08) 827-839.
  • 13 Ejeil A.L., Igondjo-Tchen S., Ghomrasseni S. et al. Expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in healthy and diseased human gingiva. J Periodontol 2003; 74 (02) 188-195.
  • 14 Kubota T., Nomura T., Takahashi T. et al. Expression of mRNA for matrix metalloproteinases and tissue inhibitors of metalloproteinases in periodontitis-affected human gingival tissue. Arch Oral Biol 1996; 41 (03) 253-262.
  • 15 Soell M., Elkaim R., Tenenbaum H. Cathepsin C, matrix metalloproteinases, and their tissue inhibitors in gingiva and gingival crevicular fluid from periodontitis-affected patients. J Dent Res 2002; 81 (03) 174-178.
  • 16 Domeij H., Yucel-Lindberg T., Modeer T. Cell interactions between human gingival fibroblasts and monocytes stimulate the production of matrix metalloproteinase-1 in gingival fibroblasts. J Periodont Res 2006; 41 (02) 108-117.
  • 17 Hassell T.M. Tissues and cells of the periodontium. Periodontol 2000 1993; 3: 9-38.
  • 18 Sorsa T., Tjaderhane L., Salo T. Matrix metalloproteinases (MMPs) in oral diseases. Oral Dis 2004; 10 (06) 311-318.
  • 19 Uitto V.J., Overall C.M., McCulloch C. Proteolytic host cell enzymes in gingival crevice fluid. Periodontol 2000 2003; 31: 77-104.
  • 20 Golub L.M., Wolff M., Roberts S. et al. Treating periodontal diseases by blocking tissue-destructive enzymes. J Am Dent Assoc 1994; 125 (02) 163-169 discussion 169–71.
  • 21 Golub L.M., Lee H.M., Ryan M.E. et al. Tetracyclines inhibit connective tissue breakdown by multiple non-antimicrobial mechanisms. Adv Dent Res 1998; 12 (02) 12-26.
  • 22 Sorsa T., Ding Y., Salo T. et al. Effects of tetracyclines on neutrophil, gingival, and salivary collagenases. A functional and western-blot assessment with special reference to their cellular sources in periodontal diseases. Ann N Y Acad Sci 1994; 732: 112-131.
  • 23 Preshaw P.M., Hefti A.F., Jepsen S. et al. Subantimicrobial dose doxycycline as adjunctive treatment for periodontitis. A review. J Clin Periodontol 2004; 31 (09) 697-707.
  • 24 Caton J., Ryan M.E. Clinical studies on the management of periodontal diseases utilizing subantimicrobial dose doxycycline (SDD). Pharmacol Res 2011; 63 (02) 114-120.
  • 25 Golub L.M., Wolff M., Lee H.M. et al. Further evidence that tetracyclines inhibit collagenase activity in human crevicular fluid and from other mammalian sources. J Periodont Res 1985; 20 (01) 12-23.
  • 26 Golub L.M., Evans R.T., McNamara T.F. et al. A non-antimicrobial tetracycline inhibits gingival matrix metalloproteinases and bone loss in Porphyromonas gingivalis-induced periodontitis in rats. Ann N Y Acad Sci 1994; 732: 96-111.
  • 27 Al-Shibani N., Windsor L.J. Effects of Porphyromonas gingivalis on human gingival fibroblasts from healthy and inflamed tissues. J Periodont Res 2008; 43 (04) 465-470.
  • 28 Zhang W., Song F., Windsor L.J. Effects of tobacco and P. gingivalis on gingival fibroblasts. J Dent Res 2010; 89 (05) 527-531.
  • 29 Windsor L.J., Bodden M.K., Birkedal-Hansen B. et al. Mutational analysis of residues in and around the active site of human fibroblast-type collagenase. J Biol Chem 1994; 269 (42) 26201-26207.
  • 30 Duran V., Matic M., Jovanovć M. et al. Results of the clinical examination of an ointment with marigold (Calendula officinalis) extract in the treatment of venous leg ulcers. Int J Tissue React 2005; 27 (03) 101-106.