Abstract
Epidermis is one of the well-known estrogen target tissues. Information regarding estrogen metabolism in epidermis is still very limited compared to that of estrogen action. In the breast cancer tissue, 17β-estradiol (E 2) is inactivated by sulfation and the expression level of estrogen sulfotransferase (SULT1E1) is inversely correlated with its malignancy. However, there is little datum about inactivation of estradiol in skin. In order to detect and measure E 2 and its metabolites simultaneously, we established an assay method with radio HPLC. A majority of [ 3H] labeled E 2 was converted to E 2 sulfate in normal human epidermal keratinocyte (NHEK) cells. The estimated activity of sulfotransferase toward E 2 at 20 nM was 0.11±0.01 (pmol/min/mg protein). Significant induction of estrogen sulfotransferase activity was observed in calcium-differentiated NHEK cells (0.58±0.07 (pmol/min/mg protein)). The gene expression of SULT1E1 was fifteen-fold higher in differentiated keratinocyte than in proliferating keratinocyte, whereas that of steroid sulfatase was reduced. These results suggest that E 2 inactivation is primarily mediated by SULT1E1 in keratinocyte and E 2 action is likely suppressed in epidermal differentiation.
| Original language | English |
|---|---|
| Pages (from-to) | 1147-1151 |
| Number of pages | 5 |
| Journal | Biological and Pharmaceutical Bulletin |
| Volume | 34 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2011 Jul |
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Keywords
- Estrogen
- Keratinocyte
- Sulfotransferase
ASJC Scopus subject areas
- Pharmaceutical Science
- Pharmacology
Cite this
Sulfation of estradiol in human epidermal keratinocyte. / Kushida, Akira; Hattori, Kenji; Yamaguchi, Nozomi; Kobayashi, Tetsuyuki; Date, Akira; Tamura, Hiroomi.
In: Biological and Pharmaceutical Bulletin, Vol. 34, No. 7, 07.2011, p. 1147-1151.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Sulfation of estradiol in human epidermal keratinocyte
AU - Kushida, Akira
AU - Hattori, Kenji
AU - Yamaguchi, Nozomi
AU - Kobayashi, Tetsuyuki
AU - Date, Akira
AU - Tamura, Hiroomi
PY - 2011/7
Y1 - 2011/7
N2 - Epidermis is one of the well-known estrogen target tissues. Information regarding estrogen metabolism in epidermis is still very limited compared to that of estrogen action. In the breast cancer tissue, 17β-estradiol (E 2) is inactivated by sulfation and the expression level of estrogen sulfotransferase (SULT1E1) is inversely correlated with its malignancy. However, there is little datum about inactivation of estradiol in skin. In order to detect and measure E 2 and its metabolites simultaneously, we established an assay method with radio HPLC. A majority of [ 3H] labeled E 2 was converted to E 2 sulfate in normal human epidermal keratinocyte (NHEK) cells. The estimated activity of sulfotransferase toward E 2 at 20 nM was 0.11±0.01 (pmol/min/mg protein). Significant induction of estrogen sulfotransferase activity was observed in calcium-differentiated NHEK cells (0.58±0.07 (pmol/min/mg protein)). The gene expression of SULT1E1 was fifteen-fold higher in differentiated keratinocyte than in proliferating keratinocyte, whereas that of steroid sulfatase was reduced. These results suggest that E 2 inactivation is primarily mediated by SULT1E1 in keratinocyte and E 2 action is likely suppressed in epidermal differentiation.
AB - Epidermis is one of the well-known estrogen target tissues. Information regarding estrogen metabolism in epidermis is still very limited compared to that of estrogen action. In the breast cancer tissue, 17β-estradiol (E 2) is inactivated by sulfation and the expression level of estrogen sulfotransferase (SULT1E1) is inversely correlated with its malignancy. However, there is little datum about inactivation of estradiol in skin. In order to detect and measure E 2 and its metabolites simultaneously, we established an assay method with radio HPLC. A majority of [ 3H] labeled E 2 was converted to E 2 sulfate in normal human epidermal keratinocyte (NHEK) cells. The estimated activity of sulfotransferase toward E 2 at 20 nM was 0.11±0.01 (pmol/min/mg protein). Significant induction of estrogen sulfotransferase activity was observed in calcium-differentiated NHEK cells (0.58±0.07 (pmol/min/mg protein)). The gene expression of SULT1E1 was fifteen-fold higher in differentiated keratinocyte than in proliferating keratinocyte, whereas that of steroid sulfatase was reduced. These results suggest that E 2 inactivation is primarily mediated by SULT1E1 in keratinocyte and E 2 action is likely suppressed in epidermal differentiation.
KW - Estrogen
KW - Keratinocyte
KW - Sulfotransferase
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UR - http://www.scopus.com/inward/citedby.url?scp=79960301236&partnerID=8YFLogxK
U2 - 10.1248/bpb.34.1147
DO - 10.1248/bpb.34.1147
M3 - Article
C2 - 21720030
AN - SCOPUS:79960301236
VL - 34
SP - 1147
EP - 1151
JO - Biological and Pharmaceutical Bulletin
JF - Biological and Pharmaceutical Bulletin
SN - 0918-6158
IS - 7
ER -