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  • Söderqvist, Gunnar, et al. (författare)
  • Metabolism of estrone sulfate by normal breast tissue : Influence of menopausal status and oral contraceptives
  • 1994
  • Ingår i: Journal of Steroid Biochemistry and Molecular Biology. - : Elsevier BV. - 0960-0760. ; 48:2-3, s. 221-224
  • Tidskriftsartikel (refereegranskat)abstract
    • The metabolism of [ 3 H]estrone sulfate ([ 3 H]E 1 S) was studied in normal breast tissue from 10 premenopausal women without oral contraceptives (OC), in 12 OC users and in 9 untreated postmenopausal women. [ 3 H]E 1 S was converted into estrone ([ 3 H]E 1 ) and estradiol-17β ([ 3 H]E 2 ) by tissue samples from all three groups of women, with only minor formation of other unconjugated compounds. The rate of [ 3 H]E 2 formation was significantly higher in premenopausal women without OC than in postmenopausal women. Among premenopausal women, OC users had a significantly lower rate of total hydrolysis and of [ 3 H]E 1 formation than non-users. The rate of total hydrolysis of [ 3 H]E 1 S in normal breast tissue from all three groups of women was similar to that in muscle, but the rate of [ 3 H]E 2 formation was ten times higher. Both total hydrolysis rate and rate of [ 3 H]E 2 formation were significantly lower in normal breast tissue than in breast carcinoma and in normal and neoplastic endometrium. The specific ability of normal breast tissue to convert E 1 S into the terminal biologically active estrogen E 2 may be important for estrogenic stimulation of the breast in subjects with low circulating E 2 levels. The lower rate of E 1 formation in OC users may reflect an inhibitory effect of the progestagen compound in such preparations.
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  • Akner, Gunnar, 1953-, et al. (författare)
  • Subcellular distribution of the glucocorticoid receptor and evidence for its association with microtubules
  • 1995
  • Ingår i: Journal of Steroid Biochemistry and Molecular Biology. - : Elsevier BV. - 0960-0760 .- 1879-1220. ; 52:1, s. 1-16
  • Forskningsöversikt (refereegranskat)abstract
    • The cellular distribution of the glucocorticoid receptor (GR) has not yet been firmly established. The extensive literature indicates that GR is present both in the cytoplasm and the cell nucleus, however, some studies have failed to detect cytoplasmic GR. It is still controversial as to whether GR is randomly diffusing in the cytoplasm and nucleus, or if the GR-distribution is organized or controlled in some way, which may be of importance for the transduction of glucocorticoid effects to cells. There is evidence that both non-activated and activated GR is associated with the plasma membrane, a number of cytoplasmic organelles and the nucleus. Both morphological and biochemical evidence show that GR is associated with microtubules during different stages of the cell cycle, i.e. GR co-localizes, co-purifies and co-polymerizes with tubulin. This indicates that GR is structurally linked to the intracellular MT-network which may be of importance in the mechanism of action of glucocorticoid hormones. The literature in this field is reviewed including the reported data on subcellular GR-localization.
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  • DONOVAN, M, et al. (författare)
  • The cellular retinoic acid binding proteins
  • 1995
  • Ingår i: The Journal of steroid biochemistry and molecular biology. - 0960-0760. ; 53, s. 459-
  • Tidskriftsartikel (refereegranskat)
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