PDF icon Download PDF
Planta Med 2003; 69(10): 899-904
DOI: 10.1055/s-2003-45097
Original Paper
Pharmacology
© Georg Thieme Verlag Stuttgart · New York

Antirheumatoid Arthritis Effect of Rhus verniciflua and of the Active Component, Sulfuretin

Jongwon Choi1 , Byung-Jae Yoon1 , Yong Nam Han2 , Kyung-Tae Lee3 , Joohun Ha4 , Hyun-Ju Jung5 , Hee-Juhn Park5
  • 1College of Pharmacy, Kyungsung University, Busan, Korea
  • 2Natural Products Research Institute, Seoul National University, Seoul, Korea
  • 3College of Pharmacy, Kyung-Hee University, Seoul, Korea
  • 4College of Medicine, Kyung-Hee University, Seoul, Korea
  • 5Division of Applied Plant Sciences, Sangji University, Wonju, Korea
This research was supported by a grant (PF002104-07) from the Plant Diversity Research Center of 21st Frontier Research Program funded by the Ministry of Science and Technology of the Korean Government
Further Information

Publication History

Received: February 13, 2003

Accepted: July 12, 2003

Publication Date:
02 December 2003 (online)

Also available ateRef
   Permissions and Reprints
Preview

Abstract

Oral administration of the MeOH extract of Rhus verniciflua or of an EtOAc fraction containing an EtOAc-soluble portion of the MeOH extract slightly decreased rheumatoid arthritis (RA) and C-reactive protein (CRP) factors in Freund's complete adjuvant reagent FCA-treated rats, indicating that they are active extracts for rheumatoid arthritis, the EtOAc extract being more active. Treatment with these two extracts prevented histological changes such as synovial cell proliferation, inflammatory cell infiltration and fat necrosis compared with an FCA-treated group. Oral administration (30 mg/kg) of sulfuretin and fustin, which were isolated from the EtOAc extract by activity-guided separation, significantly decreased RA and CRP factors, the former being more active than the latter. Treatment with the EtOAc fraction (p. o.) containing sulfuretin significantly decreased malondialdehyde (MDA) formation, and highly increased the activities of superoxide dismutase, catalase and glutathione peroxidase. Inhibition of xanthine oxidase and aldehyde oxidase in FCA-treated rats was also evident. Since treatment with sulfuretin and the EtOAc extract decreased the concentration of infiltrated mast cells in the rat knee exhibiting rheumatoid arthritis, we suggest that the Rhus verniciflua extract, which contains sulfuretin as an active component, may prevent rheumatoid syndromes by inhibiting reactive oxygen species.

Key words

Rhus verniciflua - Anacardiaceae - sulfuretin - fustin - aurones - rheumatoid arthritis - antioxidant

References

  • 1 Kim M J, Kim G T, Choi T B, Hyun J O. Effects of climatic factors and tapping date on yield and quality of lactree (Rhus verniciflua) sap.  Korean Journal of Plant Resources. 1998;  11 70-9
    PubMedSearch in Google Scholar
  • 2 Hirota S, Matsumoto H, Sakurai T, Kitagawa T, Yamaguchi O. Observation of Cu-N3-stretching bands for mono-oxide adduct of Rhus vernicifera laccase.  Biochemical and Biophysical Research Communication. 1998;  243 435-7
    PubMedSearch in Google Scholar
  • 3 Miller W C, Thielman N M, Swai N, Cegielski J P, Shao J, Ting D, Mlalasi J, Manyenga D, Lallinger G J. Delayed-type hypersensitivity testing in Tanzanian adults with HIV infection.  Journal of Acquired Immune Deficiency. 1996;  12 303-8
    PubMedSearch in Google Scholar
  • 4 Miesel R, Zuber M. Copper-dependent antioxidase defenses in inflammatory and autoimmune rheumatic diseases.  Inflammation. 1993;  17 283-94
    CrossrefPubMedSearch in Google Scholar
  • 5 Miesel R, Zuber M, Hartung R, Hass R, Kröger H. Total radical-trapping antioxidative capacity of plasma and whole blood chemiluminescence in patients with inflammatory and autoimmune rheumatic diseases.  Redox Report. 1995;  1 323-30
    PubMedSearch in Google Scholar
  • 6 Harborne J B. Dictionary of Natural Products. Vol. 10 1994 New York; Chapman & Hall 5716
    Search in Google Scholar
  • 7 Harborne J B. Dictionary of Natural Products. Vol. 9 1994 New York; Chapman & Hall 5468
    Search in Google Scholar
  • 8 Lowry O H, Rosebrough N J, Farr A L, Rendall R J. Protein measurement with folin phenol reagent.  Journal of Biological Chemistry. 1951;  193 265-71
    PubMedSearch in Google Scholar
  • 9 Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissue by thiobarbituric acid reaction.  Analytical Biochemistry. 1979;  95 351-8
    CrossrefPubMedSearch in Google Scholar
  • 10 Marklund S, Marklund G. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase.  European Journal of Biochemistry. 1974;  47 469-74
    CrossrefPubMedSearch in Google Scholar
  • 11 Aebi H. Catalase. In: Methods of Enzymatic Analysis. (Vergmeyer HU, ed.) Academic Press New York; 1974: p. 673
    Search in Google Scholar
  • 12 Paglia E D, Valentine W N. Studies on the quantitative and qualitative characterization of erythrocytes glutathione peroxidase.  Journal of Laboratory Clinical Medicine. 1967;  70 158-69
    PubMedSearch in Google Scholar
  • 13 Omura T, Sato R. The carbon monoxide binding pigments of liver microsomes: Evidence for its hemoprotein nature.  Journal of Biological Chemistry. 1964;  239 2370-85
    PubMedSearch in Google Scholar
  • 14 Stripe F, Della C E. The regulation of rat liver xanthine oxidase: Conversion in vitro of the enzyme activity from dehydrogenase (Type D) to oxidase (Type O).  Journal of Biological Chemistry. 1969;  244 3855-63
    PubMedSearch in Google Scholar
  • 15 Rajagopalan K V, Fridovich I, Handler P, Palmer G, Beinert H. Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy.  Journal of Biological Chemistry. 1968;  243 3783-96
    PubMedSearch in Google Scholar

Prof. Associate Hee-Juhn Park

Division of Applied Plant Sciences

Sangji University

Woosan-dong

Wonju 220-702

Korea

Phone: +82-+33-730-0564

Fax: +82-+33-730-0564

Email: hjpark@mail.sangji.ac.kr