Profiling transcript levels for steroidogenic enzymes in fetal tissues

Pezzi, Vincenzo; Mathis, J. Michael; Rainey, William E.; Carr, Bruce R.

doi:10.1016/j.jsbmb.2003.07.006

Cited by 142 publications

(85 citation statements)

References 39 publications

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“…In the presence of 5α-androstanedione, a keto-steroid and prototypical substrate for 3α-HSD, the α-ZOL production was significantly inhibited. Also in the presence of pregnenolone, the apparent formation of α-ZOL was inhibited, corresponding to the finding that pregnenolone can be a substrate for human Type 3 3α-HSD [32], Hence, it can be concluded that in the pig liver the reduction of ZEA towards α-ZOL is catalysed predominantly by microsomal 3α-reductases. In contrast to the α-ZOL production, the formation of β-ZOL by pig liver microsomes was only inhibited in the presence of pregnolonone, a typical endogenous substrate for 3β-HSD.…”

Section: Discussionmentioning

confidence: 56%

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Bioactivation of zearalenone by porcine hepatic biotransformation

2005

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-Zearalenone (ZEA) is a resorcylic acid lactone derivative produced by various Fusarium species that are widely found in food and feeds. The structure of zearalenone is flexible enough to allow a conformation able to bind to mammalian oestrogen receptors, where it acts as an agonist. Using oestrogen-dependent Human Breast Cancer (MCF-7) cells, the oestrogenic activity of zearalenone and its derivatives were compared using 17 β-oestradiol as a positive control. The results obtained demonstrate that the oestrogenic potency of ZEA derivatives could be ranked in the following order: α-zearalenol > α-zearalanol > zearalenone > β-zearalenol. Since pigs have been reported to be among the most sensitive animal species, biotransformation studies with pig liver subcellular fractions were conducted. These studies indicated that α-zearalenol is the main hepatic metabolite of zearalenone in pigs, and it is assumed that 3α-and 3β-hydroxysteroid dehydrogeneases are involved in the hepatic biotransformation, since the formation of α-zearalenol and β-zearalenol could be inhibited by prototypic substrates for either enzyme. The bioactivation of ZEA into the more active α-zearalenol seems to provide a possible explanation for the observed high sensitivity of pigs towards feedingstuffs contaminated with the mycotoxin. zearalenone / MCF-7 cells / oestrogenic effects / biotransformation / pigs

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Section: Discussionmentioning

confidence: 56%

“…Human 3β-HSD-isomerases belong to the SDR (short-chain dehydrogenase/reductase) family, catalysing a dehydrogenase activity involving NADH as the co-factor [38]. PCR analysis demonstrated a moderate amount of 3β-HSD-1 RNA in human foetal liver [32], but reports on these enzymes in pig tissues are lacking.…”

Section: Discussionmentioning

confidence: 99%

Bioactivation of zearalenone by porcine hepatic biotransformation

2005

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“…CYP11A, cholesterol side-chain cleavage enzyme; CYP17, 17α-hydroxylase and 17,20-lyase; CYP21, 21-hydroxylase; CYP11B1, 11β-hydroxylase; CYP11B2, aldosterone synthase; CYP19, aromatase; StAR, steroidogenic acute regulatory protein; SULT2A1, dehydroepiandrosterone-sulfotransferase; 17-OHPreg, 17α-hydroxypregnenolone; 17-OHProg, 17α-hydroxyprogesterone; 17βHSD3, 17β-hydroxysteroid dehydrogenase type 3; 3βHSD2, 3β-hydroxysteroid dehydrogenase type 2. Cartoon was modified from Pezzi, et al (35). …”

Section: Function Of Runx2 and Estrogen In Bone Tissuesmentioning

confidence: 99%

“…The human aromatase gene is comprised of a 30-kb coding region containing nine exons and a 93-kb regulatory region containing 10 untranslated exons I and is located in the chromosome 15q21.2 region (28)(29)(30). Aromatase is expressed in many tissues including the ovaries (31), muscle, skin, adipose tissue (32-34), placenta (35), and bone (36)(37)(38)(39)(40). The unusually large regulatory region contains 10 tissue-specific promoters that are alternatively used in various cell types (28,29).…”

Section: Alternative Usage Of Multiple Aromatase Promoters In Variousmentioning

confidence: 99%

Interrelationship of Runx2 and estrogen pathway in skeletal tissues

Jeong¹,

Choi²

2011

BMB Reports

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Two key molecules in skeletal tissues are bone formation master transcription factor Runx2 and the steroid hormone estrogen. It is well known that these two molecules play pivotal roles in bone homeostasis; however, the functional interaction between Runx2 and estrogen synthesis in skeletal tissues is largely unknown. Recent studies have indicated that there is a positive relationship between Runx2 and the estrogen biosynthesis pathway. In this review, a possible functional link between Runx2 and estrogen synthesis pathway in skeletal tissues will be discusses as well as the biological significance of this interaction.[BMB reports 2011; 44(10): 613-618]

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“…Synthesis of steroids in the CNS and PNS is known to begin early during development and remain into adulthood (Compagnone et al 1995, Pezzi et al 2003, King et al 2004. In these tissues, steroidogenesis does not occur in dedicated cells, but has been reported to be associated with several of the excitable and supporting cell types including neurons (different types), astrocytes, oligodendrocytes, Schwann cells and their progenitors (Le Goascogne et al 1987, Hu et al 1987b, Jung-Testas et al 1989, Koenig et al 1995, King et al 2002, Sierra et al 2003, Saalmann et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Current status and future perspectives: TSPO in steroid neuroendocrinology

Selvaraj

2016

Journal of Endocrinology

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The mitochondrial translocator protein (TSPO), previously known as the peripheral benzodiazepine receptor (PBR), has received significant attention both as a diagnostic biomarker and as a therapeutic target for different neuronal disease pathologies. Recently, its functional basis believed to be mediating mitochondrial cholesterol import for steroid hormone production has been refuted by studies examining both in vivo and in vitro genetic Tspo-deficient models. As a result, there now exists a fundamental gap in the understanding of TSPO function in the nervous system, and its putative pharmacology in neurosteroid production. In this review, we discuss several recent findings in steroidogenic cells that are in direct contradiction to previous studies, and necessitate a re-examination of the purported role for TSPO in de novo neurosteroid biosynthesis. We critically examine the pharmacological effects of different TSPObinding drugs with particular focus on studies that measure neurosteroid levels. We highlight the basis of key misconceptions regarding TSPO that continue to pervade the literature, and the need for interpretation with caution to avoid negative impacts. We also summarize the emerging perspectives that point to new directions that need to be investigated for understanding the molecular function of TSPO, only after which the true potential of this therapeutic target in medicine may be realized.

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Profiling transcript levels for steroidogenic enzymes in fetal tissues

Cited by 142 publications

References 39 publications

Bioactivation of zearalenone by porcine hepatic biotransformation

Bioactivation of zearalenone by porcine hepatic biotransformation

Interrelationship of Runx2 and estrogen pathway in skeletal tissues

Current status and future perspectives: TSPO in steroid neuroendocrinology

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