Effects of 17β-estradiol on matrix metalloproteinase-1 synthesis by human dermal fibroblasts
Introduction
Human dermal skin tissue as well as others organ undergo degenerative processes during chronological aging, especially in postmenopausal women [1], [2], [3], [4], [5], [6], [7]. The normal female skin after menopause undergoes profound changes, including reduced skin thickness, wrinkling and enhanced dryness. In normal human dermis, both type I and III collagens are the predominant forms, comprising about 80% and 15%, respectively [8]. In postmenopausal women, the significant decrease of percentage of dermal type III as well as type I and the ratio of type III/type I were observed in comparison to premenopausal women [9].
Skin is a target organ of various hormones. For instance, human dermal fibroblasts have estrogen receptors, and estrogen plays many be involved in human skin aging [10], [11]. Recently, hormone replacement therapy (HRT) has been applied to restore or suppress not only skin aging but also aging of other organs. Some studies have shown that HRT increases the amount of dermal collagen, and skin thickness in postmenopausal women [2], [3], [11], [12], [13]. Sumino et al. had already shown the significant effects of HRT to improve cutaneous elasticity on postmenopausal women [14]. These clinical data suggest that estrogen may have a certain influence on dermal tissue remodeling.
Estrogens are C18 steroids derived from cholesterol, having three subtypes including estrone (E1), 17β-estradiol (E2) and estriol (E3). Among these, estradiol is a major estrogen produced in ovaries and has strong activity in the organ system [15]. The serum concentration of 17β-estradiol in normal premenopausal women ranges under 10−10 M [15]. In the present study, we asked whether or not 17β-estradiol could affect fibroblast activities with respect to type I collagen metabolism. In addition, we investigated whether or not TGF-β is involved in the process.
Section snippets
Reagents
Dulbecco's modified Eagle's medium (DMEM) and trypsin solution were obtained from Nihon Seiyaku, Tokyo, Japan, Bovine serum albumin (BSA) from Sigma, Steinheim, Germany, fetal bovine serum (FBS) from Cytosystems Castle Hill, Australia, 17β-estradiol from Biogenesis, Poole, UK, horseradish peroxidase-conjugated anti-goat IgG (mouse) antibody (sc-2354), rabbit anti-TGF-β type II receptor antibody (C-16/sc-220), goat anti-phosphorylate-TGF-β type II receptor antibody (Tyr 336/sc-17006) from Santa
Expressions of collagen α1(I), MMP-1 and TIMP-1 mRNA
Three cell lines from three healthy volunteers demonstrated similar expression patterns on collagen α1(I), MMP-1 and TIMP-1 analysis. There was no significant change in the level of mRNA expression of type I collagen, MMP-1 and TIMP-1 regardless of the presence or absence of 17β-estradiol at any concentrations (Fig. 1).
Concentrations of PIP, proMMP-1 and TIMP-1 in the supernatant
Results and detectable ranges of each kit are summarized in Table 1. Since the actual concentration was quite different among three cell lines, the results were expressed as
Discussion
In recent years, hormone research has brought about new aspects of estrogen in the postmenopausal female. The beneficial effects of estrogen on menopausal osteoporosis and cardioprotection have been reported [16], [17], [18], [19], [20]. Similarly, the preferable effects of HRT on age-related cutaneous changes are based on the estrogen's abilities to restore the cutaneous elasticity, the deficiency of collagen and skin thickness [2], [9], [13], [14], [21]. Profound alteration of connective
References (28)
- et al.
Treatment of skin ageing symptoms in perimenopausal females with estrogen compounds, a pilot study
Maturitas
(1994) - et al.
Skin collagen changes related to age and hormone replacement therapy
Maturitas
(1992) Hormone replacement therapy and the skin
Maturitas
(2000)- et al.
The influence of hormone replacement therapy on skin ageing, a pilot study
Maturitas
(2001) - et al.
Relationship between skin collagen and bone changes during aging
Maturitas
(1994) - et al.
Effects of postmenopausal hypoestrogenism on skin collagen
Maturitas
(1999) - et al.
A randomized, double-blind, placebo-controlled study on the effect of conjugated estrogens on skin thickness
Am J Obstet Gynecol
(1994) - et al.
Changes in bone collagen makers and in bone density in hormone treated and untreated postmenopausal women
Maturitas
(1997) - et al.
Regulation of matrix metalloproteinase expression by estrogen in fibroblasts that are derived from the pelvic floor
Am J Obstet Gynecol
(2002) - et al.
Differences in estrogen modulation of tissue inhibitor of matrix metalloproteinase-1 and matrix metalloproteinase-1 expression in cultured fibroblasts from continent and incontinent women
Am J Obstet Gynecol
(2003)
Molecular mechanisms of skin ageing
Mech Ageing Dev
Topical application of 17β-estradiol increases extracellular matrix protein synthesis by stimulating TGF-β signaling in aged human skin in vivo
J Invest Dermatol
Mediation of transforming of transforming growth factor-β1-stimulated matrix contraction by fibroblasts
Am J Pathol
Does estrogen prevent skin aging? Results from the first national health and nutricion examination survey (NHANESI)
Arch Dermatol
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