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R Mathisen

Publications and source records attributed to R Mathisen.

9 recordsLinked to original sources

Estrogen mimics bind with similar affinity and specificity to the hepatic estrogen receptor in Atlantic salmon (Salmo salar) and rainbow trout (Oncorhynchus mykiss).

A variety of organic chemicals have been documented to bind to and activate the estrogen receptor (ER) and consequently induce estrogenic effects in different animals. Although the function of the ER seems phylogenetically conserved in vertebrates, a considerable interspecies variation in the structure of the ER has been demonstrated. In this study, the hepatic ER from Atlantic salmon (Salmo salar) and rainbow trout (Oncorhunchus mykiss) were partly characterized, and the ligand-binding preference for a range of endogenous steroids and environmental estrogens (estrogen mimics) was determined by receptor-radio ligand studies. The results show that both Atlantic salmon and rainbow trout livers contain ERs that bind 1,2,4,6,7-[(3)H]estradiol ([(3)H]-E2) with high affinity and low capacity (K(d) = 2.5-4.4 nM and B(max) = 27-97 fmol/mg protein). The Atlantic salmon ER (asER) and rainbow trout ER (rtER) exhibit similar [(3)H]-E2 binding characteristics, although livers from female fish contained a two to three times higher amounts of ER than the males in the two species. In competition studies with [(3)H]-E2, the asER and rtER were found to bind both native steroids (E2 > estrone > 17 beta-estradiol 17-glucuronide >> testosterone and 11-ketotestosterone) and putative estrogen mimics (diethylstilbestrol, 4-hydroxytamoxifen, ethynylestradiol > genistein, zearalenone > 4-t-octylphenol, 4-n-nonylphenol, and o,p'-DDT). The pesticides toxaphen and dieldrin, which are proposed to bind to and activate the human ER, did not display significant binding affinity for the fish ER, however. In general, the asER and rtER were found to bind both native steroids and estrogen mimics with similar affinity and specificity. The present results suggest that closely related species such as Atlantic salmon and rainbow trout display similar ER ligand-binding requirements, although interspecies differences in ER affinity and specificity between divergent species such as fish and humans may exist.

Animals↗

Induction of vitellogenin synthesis in an Atlantic salmon (Salmo salar) hepatocyte culture: a sensitive in vitro bioassay for the oestrogenic and anti-oestrogenic activity of chemicals.

A variety of organic compounds have been documented to bind to the oestrogen receptor and induce oestrogenic effects in different vertebrates. The presence of these environmental oestrogens or oestrogen mimics in the aquatic environment has been suspected of disrupting the normal endocrinology of wild populations of fish. In this study, induction of vitellogenin synthesis in primary hepatocytes from Atlantic salmon (Salmo salar) was optimized and validated as an oestrogenic in vitro bioassay using a sensitive capture vitellogenin enzyme-linked immunosorbent assay. After proper optimization (cell media supplements, cell density, temperature and exposure time), this assay gave a sensitive and reproducible response to both endogenous steroids (relative potency: 17beta-oestradiol>>oestriol>oestrone>17alpha-oestradiol) and a range of common oestrogen mimics (relative potency: ethynyloestradiol and diethylstilboestrol>>genistein and zearalenone>>bisphenol A and 4-t-octylphenol>4-n-nonylphenol and 2'-chloro,4-chloro-diphenyltrichloroethane (o,p'-DDT). However, the androgen testosterone and the putative oestrogen mimics dieldrin and toxaphene were not shown to be oestrogenic using this hepatocyte bioassay. Oestrogen-induced vitellogenin synthesis was efficiently inhibited by the anti-oestrogen ZM 189.154, suggesting that this bioassay may be used for testing both the oestrogenic and the anti-oestrogenic properties of chemicals.

Animals↗