Observations on the role of the reticuloendothelial system in the metabolism of adrenocortical steroids

Sawyer, Nevin; Oliver, Jack W.; Troop, Robert C.

doi:10.1016/s0039-128x(63)80026-4

Cited by 10 publications

(9 citation statements)

References 7 publications

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“…It is known that macromolecules of short single-chain oligonucleotides Table III. in a solution can have a common shape of the particles like the ellipsoid of a revolution or cylinder [22]. Thus, the values of radius of gyration (R g ϭ 1.2 Ϯ 0.06 nm) and volume (V ϭ 6.308 nm 3 ) we obtained for oligonucleotide 1 correspond to the structure of a cylinder of 0.727-nm radius and 3.8-nm height.…”

Section: Analysis Of Interaction Between Synthetic Oligonucleotides Amentioning

confidence: 82%

“…This group is formed at the reduction of the ⌬ 4 -3-ketogroup in Kupffer cells, exhibiting the 5␣-and 5␤-reductase activity [3]. It can be seen in Figure 3 that a perceptible DNA interaction with apoA-I occurs only in the presence of THC.…”

Section: Discussionmentioning

confidence: 95%

“…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%

“…They exhibit the 5␣-and 5␤-reductase activity. The ⌬ 4 -3-ketogroup of the hormone A ring is reduced [3]. Tetrahydroderivatives of steroid hormones were previously considered the biologically inactive forms [4].…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Analysis Of Interaction Between Synthetic Oligonucleotides Amentioning

confidence: 82%

Section: Discussionmentioning

confidence: 95%

Section: Synthesis Of Oligonucleotidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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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“…This process depends on the presence of 5or-and 5 [~-reductases restoring double bonds between positions 3 and 4 in ring A of the hormone with the formation of tetrahydrocompounds [12]. Af- ter stimulation with LPS, macrophages, but not endotheliocytes, internalize HDL 3 [2], whose protein components consist mainly of apoA-I [9].…”

Section: Resultsmentioning

confidence: 99%

Effect of tetrahydrocortisol on protein biosynthesis in hepatocytes

2000

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Cooperative effect of high-density lipoproteins and glucocorticoids on protein biosynthesis in hepatocytes was associated with the formation of biologically active hormone in Kupffer cells. Apolipoprotein A-I, a constituent of high-density lipoproteins, transported the active hormone from liver macrophages to hepatocytes. Apolipoprotein A-I-induced stimulation of protein biosynthesis was observed only in Kupffer cells. Apolipoprotein A-I alone or in combination with hormones did not change the rate of protein biosynthesis in liver endotheliocytes.

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Elevated rates and altered characteristics of the clearance of carbon from the blood of rabbits with variations in environmental conditions

Donald

1972

The Journal of Pathology

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Observations on the role of the reticuloendothelial system in the metabolism of adrenocortical steroids

Cited by 10 publications

References 7 publications

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

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

Effect of tetrahydrocortisol on protein biosynthesis in hepatocytes

Elevated rates and altered characteristics of the clearance of carbon from the blood of rabbits with variations in environmental conditions

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