(A)
MMP-
(B)
100
OJ 8)
0:::
·vi
BJ
.40
0:::
JJ
ANTI-AGING COMPOUNDS FROM JEJU ISLAND
NcmSNP SNP TO PHA PHY FG CA NT CJ EGCG
31
Figure 4. The expression of MMP-1 in human fibroblasts (ATCC, CRL-207 6). All plant extracts were used
at 100 µg/ml, except EGCG (25 µM). Non-SNP: in the absence of sodium nitroprusside. SNP: in the
presence of sodium nitroprusside. TO: Typha orientalis (seed). PHA: Pyrrosia hastata (root). PHY: Persicaria
hydropiper (whole plant). FG: Filipendula glaberrima (root). CA: Capsicum annum (whole plant). NT: Nymphaea
tetragona (rhizome). CJ: Camellia japonica (leaf). EGCG: (-)epigallocatechin-3-gallate.
of its small area. We searched for plants with effective anti-aging compounds for the skin
among the natural plants of Jeju Island.
Sixty plants from Jeju Island were extracted, and their activities were investigated for
free radical scavenging activity, elastase inhibition activity, and reduction of the expres-
sion of MMP-1 mRNA related to collagenase, which is known to degrade collagenase
and induce wrinkling of the skin. As a result, we found twelve plants with highly effective
DPPH radical scavenging activity and seven plants with good anti-elastase activity. Five
of the seven species with superior effects on elastase activity inhibition also had high
DPPH radical scavenging activity, which suggests that there is a certain correlation
between the causes of the two activities. When comparing the inhibition activities of the
seven extracts on MMP-1 expression in human fibroblasts with EGCG as a positive
control, four extracts, Persicaria hydropiper (whole plant), Filipendula glaberrima (root),
32 JOURNAL OF COSMETIC SCIENCE
Nymphaea tetragona (rhizome), and Camellia japonica (leaf) completely inhibited MMP-1
expression in human fibroblasts and could be developed as active ingredients for anti-
aging cosmetics. These results encourage us to find the active compounds of those
extracts. Further study regarding the active compounds is necessary, and we hope to
report the results of these investigations in the near future.
ACKNOWLEDGMENT
This work was supported by a grant from the Ministry of Commerce, Industry, and
Energy, "The Development of an Active Ingredient for Skin Physiology and Its Appli-
cation in Cosmetics" (subject number 2004-10014847), as part of a regional special-
ization technique development project within a regional industry promotional project of
the Ministry of Commerce, Industry, and Energy.
REFERENCES
(1) A. Perrin, E. Bauza, C. Dal Farra, and N. Domloge, Stimulating effect of collagen-like peptide on the
extracellular matrix of human skin: Histological studies, Int. j. Tissue React., 26, 97-104 (2004).
(2) G. J. Fisher, The pathophysiology of photoaging of the skin, Cutis, 75, 5-8 (2005).
(3) J. H. Chung, S. H. Youn, 0. S. Kwon, H. C. Eun, K. H. Kim, K. C. Park, K. H. Cho, and]. I. Youn,
Enhanced proliferation and collagen synthesis of human dermal fibroblasts in chronically photodam-
aged skin, Photodermatol. Photoimmunol. Photomed., 12, 84-89 (1996).
(4) L. L. Johnson, R. Dyer, and D. J. Hupe, Matrix metalloproteinases, Curr. Opin. Chem. Biol., 2, 466-471
(1998).
(5) S. 0. Yoon, S. J. Park, C. H. Yun, and A. S. Chung, Roles of matrix metalloproteinases in tumor
metastasis and angiogenesis,j. Biochem. Mo!. Biol., 36, 128-137 (2003).
(6) J. Westermark and V. M. Kahari, Regulation of matrix metalloproteinase expression in tumor invasion,
FASEB ].,13, 781-792 (1999).
(7) L. L. Johnson, R. Dyer, and D. J. Hupe, Matrix metalloproteinases, Curr. Opin. Chem. Biol., 2, 466-471
(1998).
(8) H. Birkedal-Hansen, W. G. Moore, M. K. Bodden, L. J. Windsor, B. Birkedal-Hansen, A. DeCarlo,
and J. A. Engler, Matrix metalloproteinases: A review, Crit. Rev. Oral. Biol. Med., 4, 197-250 (1993).
(9) J. Gross and C. M. Lapiere, Collagenolytic activity in amphibian tissues: A tissue culture assay, PNAS,
USA, 48, 1014-1022 (1962).
(10) P. Brenneisen, J. Oh, M. Wlaschek, J. Wenk, K. Briviba, C. Hommel, G. Herrmann, H. Sies, and K.
Scharffetter-Kochanek, Ultraviolet B wavelength dependence for the regulation of two major matrix-
metalloproteinases and their inhibitor TIMP-1 in human dermal fibroblasts, Photochem. Photobiol., 64,
877-885 (1996).
(11) Y. Kawaguchi, H. Tanaka, and T. Okada, The effects of ultraviolet A and reactive oxygen species on
the mRNA expression of 72-kDa type IV collagenase and its tissue inhibitor in cultured human dermal
fibroblasts, Arch. Dermatol. Res., 288, 39-44 (1995).
(12) H. Watanabe, T. Shimizu, J. Nishihira, R. Abe, T. Nakayama, M. Taniguchi, H. Sabe, T. Ishibashi,
and H. Shimizu, Ultraviolet A-induced production of matrix metalloproteinase-1 is mediated by
macrophage migration inhibitory factor (MIF) in human dermal fibroblasts, j. Biol. Chem., 279,
1676-1683 (2004).
(13) W. Meyer, K. Neurand, and B. Radke, Elastic fibre arrangement in the skin of the pig, Arch. Dermatol.
Res., 270, 391-401 (1981).
(14) 0. Wiedow,J. M. Schroder, H. Gregory,]. A. Young, and E. Christophers, Elafin: An elastase-specific
inhibitor of human skin-Purification, characterization, and complete amino acid sequence, J. Biol.
Chem., 265, 14791-14795 (1990).
(15) Y. Tomita and M. Seiji, Inactivation mechanism of tyrosinase in mouse melanoma, J. Dermatol., 4,
245-249 (1977).
Previous Page Next Page