Pathways of corticosteroid formation in guinea-pig adrenals

Yudaev, N. A.; Afinogenova, S A

doi:10.1016/0022-4731(78)90103-6

Cited by 10 publications

(4 citation statements)

References 14 publications

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“…Previously it was believed that reduced forms of steroid hormones (tetrahydrocompounds) are biologically inactive . We were the first to demonstrate that this is not true. , Such hormones as tetrahydrocortisol, androsterone, dehydroepiandrosterone, and others in complex with apolipoprotein A I (protein carrier) significantly activate gene expression and increase the rate of protein biosyntehsis in the liver.…”

Section: Introductionmentioning

confidence: 94%

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)_n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

2006

J. Phys. Chem. B

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A small-angle X-ray scattering study showed that the action of tetrahydrocortisol (THC) in complex with apolipoprotein A I (ApoA-I) on DNA leads to local melting of DNA. The most probable site of interaction between this complex and DNA is the (GCC)n-type sequence. Oligonucleotides (duplexes) of this type have been synthesized. It was demonstrated that the interaction of this oligonucleotide with the THC-ApoA-I complex leads to dissociation into complementary oligonucleotides. The latter ones also interact with the THC-ApoA-I complex. The kinetics of this multistep process is presented. The mechanism of interaction between hormones or their ApoA-I complexes and duplex CC(GCC)5.GG(CGG)5Li2 was studied using IR spectroscopy. It was shown that the interaction with THC or the THC-ApoA-I complex leads to the formation of hydrogen bonds between the OH group of the hormone A-ring and the C=O group of cytosine or guanine. Interaction with cortisol or the cortisol-ApoA-I complex leads to the formation of a hydrogen bond with the NH group of cytosine; in addition, THC and cortisol form hydrogen bonds with the PO2 group of the duplex and with the OH group of the monosaccharide. The interaction of ApoA-I with the duplex is accompanied by the formation of hydrogen bonds between the protein NH2 group and the C=O group of cytosine and the P=O group. The order-to-order structural transition takes place in the duplex under the action of THC or cortisol, with THC causing a higher ordering as compared to cortisol. The order-to-disorder structural transition occurs in the duplex under the action of the THC-ApoA-I, cortisol-ApoA-I, or ApoA-I complexes. Shifting the pH of the medium from 7.2 to 6.0 also leads to an order-to-disorder-type structural transition.

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Section: Introductionmentioning

confidence: 94%

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)_n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

2006

J. Phys. Chem. B

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“…The changes revealed in the adrenal cortex after repeated hypoxia are primarily associated with the development of general adaptation syndrome which is characterized by enhanced corticosteroid production, ACC hyperplasia, and pronounced hyperemia of the adrenal gland [2][3][4]9,14].…”

Section: -mentioning

confidence: 99%

Tissue reorganization of rat adrenal cortex induced by hypoxia and its correction with nandrolone

et al. 1999

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Acute hypoxia has a pronounced catabolic effect, whereas repeated hypoxic episodes promote hypertrophy of the adrenal cortex. Steroid hyperproduction caused by stress reaction after single hypoxic episode persists after repeated hypoxic episodes. The relations between vessels and parenchyma play the key role in spatial reorganization of the adrenal cortex. Increased volume and surface-volume ratios between sinusoids and adrenocorticocytes point to the enhancement of transcapillary exchange and can be regarded as an adaptive compensatory reaction on the tissue level. Nandrolone decreases antianabolic and stress effects of hypoxia, thus potentiating compensatory adaptive reactions both after single and repeated hypoxic episodes.Key Words: adrenal cortex; hypoxia; nandrolone; morphology; stereology There are ample data concerning hypoxia and changes in tissues and organs caused by inadequate oxygen supply [1,5,7]. From biological point of view, hypoxia can be regarded as a stress factor, therefore oxygen deficiency induces unspecific stress reaction in the organism [8,10]. An important component of this reaction is activation of the adrenals and enhanced hormone synthesis and secretion. This strain combined with negative effect of oxygen deficiency on energy supply of biosynthetic processes in adrenocorticocytes (ACC) results in significant structural and functional changes in this organ and secretory insufficiency.Recently, the possibitity of correcting hypoxic states with antihypoxants of different origin attracted attention of many authors [6,7,11 ]. However, hypoxiainduced morphological changes in the adrenal glands, particularly, spatial reorganization of the main tissue components, and the possibility of correcting these changes are not completely elucidated.

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“…Computer search of the database of mammalian nucleotide sequences (GenBank, EMBL DNA library) revealed the presence of a sequence of CC(GCC) [3][4][5] type at the 3Ј-end nontranslated section of the human apoA-I gene. The same sequence, but with a greater number of iterations, was found in the regulatory region of many mammalian and human genes.…”

Section: Synthesis Of Oligonucleotidesmentioning

confidence: 99%

“…The ⌬ 4 -3-ketogroup of the hormone A ring is reduced [3]. Tetrahydroderivatives of steroid hormones were previously considered the biologically inactive forms [4]. Then it was shown that in the complex with apolipoprotein A-I (apoA-I), they activate the protein biosynthesis in hepatocytes significantly [5].…”

Section: Introductionmentioning

confidence: 99%

Effect of glucocorticoids and their complexes with apolipoprotein A‐I on the secondary structure of eukaryotic DNA

Панин¹,

Kunitsyn²,

Tusikov³

2004

Int J of Quantum Chemistry

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ABSTRACT:The tetrahydrocortisol-apolipoprotein A-I complex specifically interacts with eukaryotic DNA isolated from rat liver. This interaction is highly cooperative and of a saturating nature. One DNA molecule binds about 54 molecules of the complex. Smallangle X-ray scattering has shown that hydrogen bonds between nitrous bases are destroyed and that single-stranded structures are formed at the interaction of the tetrahydrocortisolapolipoprotein A-I complex with eukaryotic DNA. The most probable site of binding the tetrahydrocortisol-apolipoprotein A-I complex with DNA is the sequence of the CC(GCC) n type entering the structure of many genes, among them the structure of the human apolipoprotein A-I gene. Oligonucleotide of this type has been synthesized. The association constant (K ass ) of its complexation was shown to be 1.66 ⅐ 10 6 M Ϫ1. Substitution of tetrahydrocortisol for cortisol in the complex results in a considerable decrease of K ass . IRspectroscopy study has shown that the interaction of tetrahydrocortisol with oligonucleotide CC(GCC) 3-5 is accompanied by the formation of hydrogen bonds via the CO-NH, PO 2 , and OH groups of desoxycytidinephosphate. The tetrahydrocortisol-apolipoprotein A-I complex alters the DNA secondary structure formed at the interaction with the hormone, causing the structural transition "order 3 tangle." It is assumed that in the GC-pairs of the given DNA sequence, tetrahydrocortisol initiates the rupture of hydrogen bonds, while the hydrophobic interactions between nitrous bases and apoA-I intensify this process.

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Pathways of corticosteroid formation in guinea-pig adrenals

Cited by 10 publications

References 14 publications

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)_n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)_n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

Tissue reorganization of rat adrenal cortex induced by hypoxia and its correction with nandrolone

Effect of glucocorticoids and their complexes with apolipoprotein A‐I on the secondary structure of eukaryotic DNA

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Pathways of corticosteroid formation in guinea-pig adrenals

Cited by 10 publications

References 14 publications

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

Tissue reorganization of rat adrenal cortex induced by hypoxia and its correction with nandrolone

Effect of glucocorticoids and their complexes with apolipoprotein A‐I on the secondary structure of eukaryotic DNA

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Product

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Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)_n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I

Changes in the Secondary Structure of Highly Polymeric DNA and CC(GCC)_n-Type Oligonucleotides under the Action of Steroid Hormones and Their Complexes with Apolipoprotein A I