Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism.

Guengerich, F. Peter; Martin, Martha V.; Beaune, P; Kremers, Pierre; Wolff, Thomas; Waxman, David J.

doi:10.1016/s0021-9258(19)89213-x

Cited by 657 publications

(128 citation statements)

References 41 publications

Supporting

Mentioning

128

Contrasting

Order By: Relevance

“…[1,2] It was found that 1,4-dihydropyridines are analogues of nicotinamide adenosine dinucleotide hydride (NADH) coenzyme that undergo oxidative aromatization to the corresponding pyridine due to the catalysis of cytochrome P-450 in biological systems. [3] Recently, the synthesis of pyridines has attracted considerable attention due to their use as natural products, pharmaceuticals, building blocks, dyes, reagents, and ligands in organic chemistry. [4] Oxidation of 1,4 dihydropyridines is one of the main methods for the preparation of 4-substuted pyridine derivatives which are hard to access via the friedel crafts alkylation.…”

Section: Introductionmentioning

confidence: 99%

Superparamagnetic core‐shell metal–organic framework Fe₃O₄@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Janani

Abdoli‐Senejani

Isfahani

2021

Applied Organom Chemis

View full text Add to dashboard Cite

A facile and efficient method was described for oxidation of some 3,5-diacyl or 3,5-diester 1,4-dihydropyridines using H 2 O 2 in the presence of superparamagnetic core-shell metal-organic framework Fe 3 O 4 @Ni-MOF. The Fe 3 O 4 @Ni-MOF has been obtained byStep-by-Step method in which magnetic Fe 3 O 4 magnetic nanoparticles were coated with Ni-MOF using a mercaptoacetic acid linker. The synthesized catalyst was characterized using thermogravimetric analysis, FT-IR spectroscopy, powder X-ray diffraction, field emission scanning electron microscopy and energy-dispersive X-ray analysis. The novel superparamagnetic core-shell metal-organic framework Fe 3 O 4 @Ni-MOF revealed high efficiency for oxidation of various 1,4-dihydropyridines using hydrogen peroxide. The Box-Behnken design matrix and the response surface method were applied to investigate the optimization of the reaction conditions. The conditions for optimal reaction yield and time were: amount of catalyst ≈17 mmol, temperature ≈78 C and amount of hydrogen peroxide ≈ 1 ml. A variety of 3,5-diacyl or 3,5-diester 1,4-dihydropyridines with different substituted functional groups have been converted to corresponding pyridines with good to excellent isolated yields using H 2 O 2 and Fe 3 O 4 @Ni-MOF. The catalyst was reused up to five times for the oxidation of 1,4-dihydropyridines without a significant loss in catalytic activity. The short reaction times, simplicity of method, good to excellent yields and reusability of catalyst were some advantages of the proposed procedure.

show abstract

Section: Introductionmentioning

confidence: 99%

Superparamagnetic core‐shell metal–organic framework Fe₃O₄@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Janani

Abdoli‐Senejani

Isfahani

2021

Applied Organom Chemis

View full text Add to dashboard Cite

show abstract

“…In the rat, therefore, there is some direct evidence for the involvement of different isoenzymes in oestradiol 2-hydroxylation. In man, Guengerich et al [10] described the immunoinhibition of oestradiol 2-hydroxylase by an antibody to P-450NF (P450111A1) in human liver microsomes. Similarly Guengerich [11] has also recently described the inhibition of 17aethinyloestradiol 2-hydroxylation by this antibody, although purified P-450NF had only relatively low catalytic 17a-ethinyloestradiol 2-hydroxylase activity.…”

Section: Introductionmentioning

confidence: 99%

Differences in the cytochrome P-450 isoenzymes involved in the 2-hydroxylation of oestradiol and 17 α-ethinyloestradiol. Relative activities of rat and human liver enzymes

Ball¹,

Forrester

Wolf

et al. 1990

Biochemical Journal

View full text Add to dashboard Cite

The metabolism of oestradiol and 17 alpha-ethinyloestradiol to their 2-hydroxy derivatives is an important determinant in their biological effects. In this work, we have investigated which rat or human cytochrome P-450 isoenzymes are involved in catalysing these reactions. Oestradiol 2-hydroxylation was catalysed by a wide variety of rat cytochrome P-450s from gene families P450IA, P450IIB, P450IIC and P450IIIA. Interestingly, 17 alpha-ethinyloestradiol, which only differs structurally from oestradiol at a position distant from the site of oxidation, was metabolized predominantly by members of the P450IIC gene subfamily. In order to establish which enzymes are responsible for the oxidation of these substrates in man, antibodies to rat liver cytochrome P-450 isoenzymes were used to inhibit these reactions in a panel of human liver microsomal fractions. Also, possible correlations between the proteins recognized by the antibodies and the 2-hydroxylation rate were determined. These experiments provide evidence that 2-hydroxylation of 17 alpha-ethinyloestradiol in man is catalysed by cytochromes from the P450IIC, P450IIE and P450IIIA gene families. In contrast, the major proteins involved in oestradiol metabolism are from the P450IA gene family, although members of the P450IIC and P450IIE gene families may also play a role. These data demonstrate that the differences in the capacity of rat P-450s to metabolize these substrates are also present in the comparable enzymes involved in man, and that a variety of factors will determine the rate of disposition of these compounds in man.

show abstract

“…95 As our own work on P450 3A4 developed, I realized that there was considerable overlap between the substrate repertoires of the newly discovered P450 3A4 and what was then called MDR-1. 96,97 The MDR-1 protein turned out not to be only associated with tumors but was also a normal plasma membrane constituent in the liver, intestine, and brain. 98,99 Since then, a number of other efflux Figure 6.…”

Section: Discussionmentioning

confidence: 99%

Intersection of the Roles of Cytochrome P450 Enzymes with Xenobiotic and Endogenous Substrates: Relevance to Toxicity and Drug Interactions

Guengerich

2016

Chem. Res. Toxicol.

114

View full text Add to dashboard Cite

Today much is known about cytochrome P450 (P450) enzymes and their catalytic specificity, but the range of reactions catalyzed by each still continues to surprise. Historically P450s had been considered to be involved in either the metabolism of xenobiotics or endogenous chemicals, in the former case playing a generally protective role and in the latter case a defined physiological role. However, the line of demarcation is sometimes blurred. It is difficult to be completely specific in drug design, and some P450s involved in the metabolism of steroids and vitamins can be off-targets. In a number of cases, drugs have been developed that act on some of those P450s as primary targets, e.g., steroid aromatase inhibitors. Several of the P450s involved in the metabolism of endogenous substrates are less specific than once thought and oxidize several related structures. Some of the P450s that primarily oxidize endogenous chemicals have been shown to oxidize xenobiotic chemicals, even in a bioactivation mode.

show abstract

Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism.

Cited by 657 publications

References 41 publications

Superparamagnetic core‐shell metal–organic framework Fe₃O₄@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Superparamagnetic core‐shell metal–organic framework Fe₃O₄@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Differences in the cytochrome P-450 isoenzymes involved in the 2-hydroxylation of oestradiol and 17 α-ethinyloestradiol. Relative activities of rat and human liver enzymes

Intersection of the Roles of Cytochrome P450 Enzymes with Xenobiotic and Endogenous Substrates: Relevance to Toxicity and Drug Interactions

Contact Info

Product

Resources

About

Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism.

Cited by 657 publications

References 41 publications

Superparamagnetic core‐shell metal–organic framework Fe3O4@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Superparamagnetic core‐shell metal–organic framework Fe3O4@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Differences in the cytochrome P-450 isoenzymes involved in the 2-hydroxylation of oestradiol and 17 α-ethinyloestradiol. Relative activities of rat and human liver enzymes

Intersection of the Roles of Cytochrome P450 Enzymes with Xenobiotic and Endogenous Substrates: Relevance to Toxicity and Drug Interactions

Contact Info

Product

Resources

About

Superparamagnetic core‐shell metal–organic framework Fe₃O₄@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide

Superparamagnetic core‐shell metal–organic framework Fe₃O₄@Ni‐MOF as efficient catalyst for oxidation of 1,4‐dihydropyridines using hydrogen peroxide