RELATION BETWEEN IN VITRO ALTERATION BY ALLYL COMPOUNDS AND FORMS OF CYTOCHROME P-450

1980 ◽  
pp. 1001-1004
Author(s):  
V. Luu-The ◽  
J. Cumps ◽  
P. Dumont
Keyword(s):  
Cytochrome P 450 ◽  
Allyl Compounds

Oxygenation of 18-hydroxycorticosterone as the final reaction for aldosterone biosynthesis

1984 ◽  
Vol 107 (3) ◽  
pp. 395-400 ◽  
Author(s):  
Itaru Kojima ◽  
Etsuro Ogata ◽  
Hiroshi Inano ◽  
Bun-ichi Tamaoki
Keyword(s):  
Carbon Monoxide ◽  
Hydroxysteroid Dehydrogenase ◽  
Dependent Manner ◽  
In Vitro Production ◽  
Mitochondrial Preparation ◽  
Final Reaction ◽  
Vitro Production ◽  
Dose Dependent ◽  
Cytochrome P 450

Abstract. Incubation of 18-hydroxycorticosterone with the sonicated mitochondrial preparation of bovine adrenal glomerulosa tissue leads to the production of aldosterone, as measured by radioimmunoassay. The in vitro production of aldosterone from 18-hydroxycorticosterone requires both molecular oxygen and NADPH, and is inhibited by carbon monoxide. Cytochrome P-450 inhibitors such as metyrapone, SU 8000. SU 10603, SKF 525A, amphenone B and spironolactone decrease the biosynthesis of aldosterone from 18-hydroxycorticosterone. These results support the conclusion that the final reaction in aldosterone synthesis from 18-hydroxycorticosterone is catalyzed by an oxygenase, but not by 18-hydroxysteroid dehydrogenase. By the same preparation, the production of [3H]aldosterone but not [3H]18-hydroxycorticosterone from [1,2-3H ]corticosterone is decreased in a dose-dependent manner by addition of non-radioactive 18-hydroxycorticosterone.

Antimutagenic Activity of Lutein –An Oxycarotenoid Present in the Macula and its Inhibition of Cytochrome P 450 Enzymes in vitro

2013 ◽  
Vol 6 (3) ◽  
pp. 213-220 ◽  
Author(s):  
Edakkadath Sindhu ◽  
Alikkunjhi Firdous ◽  
Ramnath Viswanathan ◽  
Ramadasan Kuttan
Keyword(s):  
Antimutagenic Activity ◽  
Cytochrome P 450

Alteration in the expression of genes for cholesterol side-chain cleavage enzyme and 21-hydroxylase by hypophysectomy and ACTH administration in the rat adrenal

1990 ◽  
Vol 4 (3) ◽  
pp. 239-245 ◽  
Author(s):  
T. Imai ◽  
H. Seo ◽  
Y. Murata ◽  
M. Ohno ◽  
Y. Satoh ◽  
...  
Keyword(s):  
Steady State ◽  
Adrenal Weight ◽  
Side Chain ◽  
Total Rna ◽  
Side Chain Cleavage ◽  
Chain Cleavage ◽  
Acth Treatment ◽  
Steady State Levels ◽  
Cytochrome P 450

ABSTRACT The changes in steady-state levels of mRNA for cholesterol side-chain cleavage cytochrome P-450 (P-450scc) and steroid 21-hydroxylase cytochrome P-450 (P-450c21) caused by hypophysectomy and ACTH treatment were determined in rat adrenals. Hypophysectomy caused marked decreases in adrenal weight and total RNA per gland. Administration of ACTH resulted in increases in adrenal weight and total RNA. A significant correlation between the amount of RNA and adrenal weight was observed. Both P-450scc and P-450c21 mRNAs were decreased by hypophysectomy and increased by ACTH treatment. P-450scc mRNA decreased to 20% and P-450c21 mRNA to 76% of control values 1 day after hypophysectomy. ACTH caused a significant increase in P-450scc mRNA after 3 h. However, a significant increase in P-450c21 mRNA was observed 12 h after administration of ACTH. These results are concordant with previous studies in vitro utilizing cultured adrenocortical cells. Moreover, the induction of steady-state levels of P-450scc mRNA was faster than that observed by other investigators in studies in vitro. These results may indicate that integrity of the adrenal gland in vivo is important for the action of ACTH.

The protective properties of synthetic porphyrin tin complexes in toxic hyperbilirubinemia

2000 ◽  
Vol 04 (03) ◽  
pp. 243-247 ◽  
Author(s):  
T. O. PHILIPPOVA ◽  
B. N. GALKIN ◽  
N. YA. GOLOVENKO ◽  
Z. I. ZHILINA ◽  
S. V. VODZINSKII
Keyword(s):  
Heme Oxygenase ◽  
Serum Bilirubin ◽  
Protoporphyrin Ix ◽  
Serum Bilirubin Level ◽  
Oxygenase Activity ◽  
Tetraphenyl Porphyrin ◽  
Tin Complexes ◽  
Cytochrome P 450

Tin complexes of meso-substituted synthetic porphyrins, namely Sn 4+-meso-tetraphenyl- porphyrin ( Sn - TPP ) and Sn 4+-meso-tetrakis(N-methyl-3-pyridyl)porphyrin tetratosylate ( Sn - TMe -3- PyP ), efficiently decrease the serum bilirubin level when injected subcutaneously at a dose of 100 μM kg−1 body weight into mice. These compounds are active during hyperbilirubinemia, induced by phenylhydrazine, hemin and tetrachloromethane, and also during autoimmune hemolytic anemia. In the latter case a decrease in serum bilirubin content was observed, as well as a decrease in the amount of blood reticulocytes which reflects a milder course of the disease. The Sn complexes under study induce, in vivo, cytochrome P-450, inhibit microsomal heme oxygenase and decrease the intensity of lipid peroxidation. At the same time, in vitro the hepatic and splenic heme oxygenase activity is blocked only when a 0.1 μM concentration of Sn - TMe -3- PyP or Sn -protoporphyrin IX is added to the incubation mixture. Sn - TPP does not affect the activity of this enzyme in vitro.

Influence of Safeners on the in vivo and in vitro Metabolism of Bentazon and Metolachlor by Grain Sorghum Shoots: a Preliminary Report

1991 ◽  
Vol 46 (9-10) ◽  
pp. 906-914 ◽  
Author(s):  
Donald E. Moreland ◽  
Frederick T. Corbin
Keyword(s):  
Grain Sorghum ◽  
In Vitro Studies ◽  
Naphthalic Anhydride ◽  
Surface Sterilization ◽  
Polar Components ◽  
In Vitro Shoots ◽  
Treated Seed ◽  
Cytochrome P 450

Abstract Metabolism of bentazon and metolachlor by excised shoots and a microsomal fraction iso­lated from the shoots, of 3-day-old, dark-grown, grain sorghum (Sorghum bicolor cv. Funk G 522 DR) seedlings was studied. The effects of seed treatments, on the subsequent metabo­lism of the herbicides, with the safeners naphthalic anhydride, oxabetrinil, and CGA 133205 were compared against surface-sterilization and Captan-treatments. Bentazon was aryl hydroxylated in both in vivo and in vitro studies with the hydroxylated derivative undergoing glycosylation only under in vivo conditions. Both shoots and microsomes isolated from shoots of safener-treated seed showed enhanced metabolism of bentazon relative to the controls. In­ hibition by tetcyclacis, a potent inhibitor of plant cytochrome P-450 monooxygenases, in both the in vivo and in vitro studies, and a requirement for NADPH in the in vitro studies suggested that the formation of hydroxybentazon was mediated by a cytochrome P-450 monooxygenase. Metolachlor was metabolized to polar material and O-desmethylmetolachlor under in vivo conditions. Only the demethylated product was formed in vitro. Shoots isolated from safener-treated seed showed enhanced formation of polar com pounds which were assumed to have arisen from conjugation with glutathione. Tetcyclacis did not affect the formation of the polar components. However, the formation of O-desmethylmetolachlor was depressed in the shoots excised from safener-treated seed under both in vivo and in vitro conditions. Tetcyclacis completely prevented formation of the demethylated metabolite. Hence, formation of this meta­bolite is considered to be P-450 mediated. The differential response obtained with the safeners, i.e., stimulation of aryl hydroxylation of bentazon and depression of metolachlor demethylation, suggests that the reactions are probably catalyzed by different cytochrome P-450 mono­oxygenases.

scholarly journals In vitro interaction of potential antiviral TMPRSS2 inhibitors with human serum albumin and cytochrome P 450 isoenzymes

2022 ◽  
Vol 146 ◽  
pp. 112513
Author(s):  
Erzsébet Pászti-Gere ◽  
Anna Szentkirályi ◽  
Zsófia Fedor ◽  
Gábor Nagy ◽  
Zoltán Szimrók ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Vitro Interaction ◽  
Cytochrome P 450
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