inhibition of 17beta-hydroxysteroid dehydrogenases 1 is proposed to be a prime candidate for inhibition in patients who develop aromatase inhibitor resistance or in combination with aromatase inhibitors as a first line treatment
inhibition of 17beta-hydroxysteroid dehydrogenases 1 may be a prime candidate for inhibition in patients with breast cancer who develop aromatase inhibitor resistance or in combination with aromatase inhibitors as a first line treatment
the ratio of HSD17B1 to HSD17B2 is a good indicator of tamoxifen treatment benefit, as post-menopausal patients with tumors expressing a high HSD17B1/HSD17B2 protein ratio have less benefit from tamoxifen treatment
17beta-HSD1 belongs to the short-chain dehydrogenase/reductase (SDR) family and contains the conserved Rossmann-fold for nucleotide binding, the catalytic triad with residues Ser142, Tyr155, and Lys159 and a dimerization region. Residue Cys10 is highly conserved among species, including rodents and zebrafish, suggesting a role for this residue in the stability and/or function of the protein. The cysteine residue at this position is conserved in all members of the SDR9C family, except for 17beta-HSD2, which has a cysteine residue downstream by two positions
HSD17B12 is a member of the hydroxysteroid dehydrogenase superfamily, a multifunctional group of enzymes involved in the metabolism of steroids, retinoids, bile and fatty acids
enzyme inhibition can lead to desired increase of estradiol and testosterone levels in the bone tissue and may be used for the treatment of osteoporosis
enzyme inhibition can lead to desired increase of estradiol and testosterone levels in the bone tissue and may be used for the treatment of osteoporosis
estrone treatment in 17betaHSD1 positive NSCLC cells, A-549 and LK-87, results in estradiol production and enhances cell proliferation, which is abrogated effectively by 17betaHSD1 siRNA knockdown
knockdown of 17beta-HSD1 gene, HSD17B1, modulates the transcript profile of the hormone-dependent breast cancer cell line T47D, T47D, with 105 genes regulated 1.5 fold or higher in estradiol-independent manner
knockdown of 17beta-HSD1 gene, HSD17B1, modulates the transcript profile of the hormone-dependent breast cancer cell line T47D, with 105 genes regulated 1.5fold or higher in estradiol-independent manner. Genes that are primarily involved in the cell cycle progression, such as the cyclin A2 gene, CCNA2, are generally down-regulated whereas genes involved in apoptosis and cell death, including the pro-apoptotic gene XAF1, IFIH1 and FGF12, are upregulated by 17beta-HSD1 knockdown
AKR1B15.1 is a mitochondrial carbonyl reductase. Two alternatively spliced protein isoforms encoded by the human AKRgene AKR1B15 exist, the AKR1B15.1 isoform catalyzes reduction of steroids and 3-keto-acyl-CoA conjugates
besides as a biomarker in cancer, AKR1C3 is important in the reduction of steroids and prostaglandins, and function as part of a chemical barrier to defend the body from intrusion of toxic chemicals
by acting as a 17-ketosteroid reductase, AKR1C3 produces potent androgens in peripheral tissues which activate the androgen receptor or act as substrates for aromatase. AKR1C3 is implicated in the production of androgens in castration-resistant prostate cancer and polycystic ovarian syndrome and is implicated in the production of aromatase substrates in breast cancer
enzyme involved in maintaining high estradiol levels in breast tumors of postmenopausal women. In certain breast cancer patients, intratumoral estradiol is produced by the 17beta-HSD1-mediated reduction of estrone produced by aromatase. A high level of 17-beta-HSD1 correlates with an increased risk of developing a late relapse of breast cancer in ER-positive breast cancer patients
17beta-hydroxysteroid dehydrogenase type 6 converts the androgen 5alpha-dihydrotestosterone to the estrogen 5alpha-androstane-3beta,17beta-diol, and this leads to activation of the estrogen receptor beta reporter. This conversion of dihydrotestosterone occurs at concentrations that are in the physiological range of this hormone in the prostate
17beta-hydroxysteroiddehydrogenasetype IV (HSD17B4),coding for a steroidogenic enzyme that converts estradiol (E2) into an inactive metabolite. HSD17B4 mRNA is expressed more in the song regions of males compared to females throughout development, suggesting that regulation of E2 is important for male-typical song development. 17beta-Estradiol treatments increase HSD17B4 mRNA in the auditory region of males, which is contraryto findings in the song system. Different behaviors may be guided by the same genes and hormones, but the exact nature of the gene-hormone relationships may differ according to brain region and behavior
endogenous production of 17beta-estradiol in hematological malignant cells might also contribute to immunohormonal imbalance in patients with these disorders. Human T and B lymphocytes are positive for ERa, ERb and GPR30 receptors. Using putative membrane receptors, estrogens are able to modulate cytokine profiles in T cells and the control of B-cell maturation and selection. In particular, estrogens are able to inhibit T cell proliferation, interleukin-2 (IL-2) biosynthesis, and increase B-cell proliferation and antibody production. 17beta-Estradiol is able to upregulate cyclic AMP response element modulator alpha leading to reduced IL-2 gene expression in human T lymphocytes. HSD17B1 may play a crucial role in the development of estrogen-dependent diseases
estrone treatment in 17betaHSD1 positive NSCLC cells, A-549 and LK-87, results in estradiol production and enhances cell proliferation, which is abrogated effectively by 17betaHSD1 siRNA knockdown
by its oxidative activity, the enzyme can decrease the concentration of two important neurosteroids, allopregnanolone (ALLOP) and 17beta-estradiol, respectively preventing their neurogenesis and neuroprotective effects
the enzyme 17beta-HSD1 may be involved in oncogenesis by favoring antiapoptosis pathway in breast cancer cells and correborates with its previously shown role in increasing breast cancer cell proliferation. The gene regulation occurring in steroid-deprived conditions shows that 17beta-HSD1 can modulate endogenous gene expression in steroid-independent manners
the enzyme increases breast cancer cell proliferation via a dual effect on 17-beta-estradiol and 5alpha-dihydrotestosterone levels and impacts gene expression and protein profile of breast cancer cells cultured in 17-beta-estradiol-contained medium
Lys149 is a critical residue for the discrimination between C-18 and C-19 steroid substrate. Analysis of the role of Cys10 for 17beta-HSD1 function, overview
role of a cysteine residue, Cys10 in the Rossmann-fold NADPH binding region, for 17beta-HSD1 function, important interactions of Cys10 with residues involved in the stabilization of amino acids of the NADPH binding pocket, three-dimensional enzyme structure modeling, overview
1.1.1.62 17beta-estradiol 17-dehydrogenase
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