Genetic polymorphism of cytochrome P450 1A1 in a northern Italian population: high frequency of the CYP1A1*2C allele

2011 ◽  
Vol 49 (6) ◽  
Author(s):  
Alfredo Santovito ◽  
Piero Cervella ◽  
Massimiliano Delpero
Keyword(s):  
Cytochrome P450 ◽  
Genetic Polymorphism ◽  
High Frequency ◽  
Italian Population ◽  
Cytochrome P450 1A1

Genetic Polymorphism of Cytochrome P450 1A1 (CYP1A1) and Glutathione Transferases (M1, T1 and P1) among Africans

2002 ◽  
Vol 40 (9) ◽  
Author(s):  
Collet Dandara ◽  
Jane Sayi ◽  
Collen M. Masimirembwa ◽  
Ayoub Magimba ◽  
Sylvia Kaaya ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Genetic Polymorphism ◽  
Glutathione Transferases ◽  
Cytochrome P450 1A1

Molecular Regulation of Cytochrome P450 1A1 Induction By Hyperoxia in Human Pulmonary Cells

PEDIATRICS ◽  
2016 ◽  
Vol 137 (Supplement 3) ◽  
pp. 507A-507A
Author(s):  
Sudeepta K Basu ◽  
Renjithkumar Kalikkot Thekkeveedu ◽  
Chun Chu ◽  
Paramhamsa Maturu ◽  
Weiwu Jiang ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Molecular Regulation ◽  
Cytochrome P450 1A1 ◽  
Pulmonary Cells

Associations of CYP2A6 Gene Polymorphism with Smoking Status Among Jordanians: Gender-Related Differences

2019 ◽  
Vol 20 (9) ◽  
pp. 765-770 ◽  
Author(s):  
Hana M. Hammad ◽  
Amer Imraish ◽  
Belal Azab ◽  
Al M. Best ◽  
Yousef S. Khader ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Genetic Polymorphism ◽  
Smoking Status ◽  
Hepatic Enzyme ◽  
Nicotine Metabolism ◽  
Significant Frequency ◽  
Cytochrome P450 2A6 ◽  
Study Population ◽  
Major Metabolic Pathway ◽  
Cyp2a6 Gene

Background: Cytochrome P450 2A6 enzyme (CYP2A6), an essential hepatic enzyme involved in the metabolism of drugs, is responsible for a major metabolic pathway of nicotine. Variation in the activity of polymorphic CYP2A6 alleles has been implicated in inter-individual differences in nicotine metabolism. Aims: The objective of the current study was to assess the association between the smoking status and the cytochrome P450 2A6 enzyme (CYP2A6) genotype in Jordanians. Methods: In the current study, 218 (117 Male and 101 female) healthy unrelated Jordanian volunteers were recruited. CYP2A6*1B, CYP2A6*4 and CYP2A6*9 were determined and correlated with subject smoking status. Results: *1A/*1A was the most common genetic polymorphism in the overall study population, with no significant frequency differences between smokers and non-smokers. When the population was divided according to gender, only male smokers showed a significant correlation between genotype and smoking status. Considering the CYP2A6*9 genotype, the results showed differences in distribution between smokers and non-smokers, but only women showed a significant association between CYP2A6*9 allele genotype and smoking status. Conclusion: The results of this study show that there is a significant association between CYP2A6*9 genotype and smoking status. They also show that CYP2A6 genotype is significantly influenced by gender.

Chicken Egg Yolk as an Excellent Source of Highly Specific Antibodies Against Cytochromes P450

2004 ◽  
Vol 69 (3) ◽  
pp. 659-673 ◽  
Author(s):  
Petr Hodek ◽  
Tomáš Koblas ◽  
Helena Rýdlová ◽  
Božena Kubíčková ◽  
Miroslav Šulc ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochromes P450 ◽  
Egg Yolk ◽  
Good Alternative ◽  
Invasive Technique ◽  
Cytochrome P450 1A1 ◽  
Orconectes Limosus ◽  
Chicken Egg ◽  
Cytochrome P450 2B4 ◽  
Human Livers

Using chicken antibodies IgY (purified from egg yolks) against mammalian cytochromes P450 and by means of cytochrome P450 marker substrates, we found for the first time the presence of hepatopancreatic cytochrome P450 in crayfishOrconectes limosus(an inducible cytochrome P450 2B-like enzyme) and we were able to detect and quantify cytochrome P450 1A1 in microsomes of human livers. Expression levels of cytochrome P450 1A1 in human livers constituted less than 0.6% of the total hepatic cytochrome P450 complement. The results obtained in our study are clear examples that chicken IgY are suitable for cytochrome P450 detection and quantification. Due to the evolutionary distance, chicken IgY reacts with more epitopes on a mammalian antigen, which gives an amplification of the signal. Moreover, this approach offers many advantages over common mammalian antibody production since chicken egg is an abundant source of antibodies (about 100 mg IgY/yolk) and the egg collection is a non-invasive technique. In the case of antibodies against cytochrome P450 2B4, we documented fast and steady production of highly specific immunoglobulins. Thus, chicken antibodies should be considered as a good alternative to and/or superior substitute for conventional polyclonal antibody produced in mammals.

scholarly journals An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Goutam Mukherjee ◽  
Prajwal P. Nandekar ◽  
Rebecca C. Wade
Keyword(s):  
Electron Transfer ◽  
Cytochrome P450 ◽  
Drug Targets ◽  
Catalytic Domain ◽  
Cytochrome P450 1A1 ◽  
P450 Oxidoreductase ◽  
Distal Side ◽  
Cytochrome P450 Oxidoreductase ◽  
Membrane Bound ◽  
Transient Interactions

AbstractCytochrome P450 (CYP) heme monooxygenases require two electrons for their catalytic cycle. For mammalian microsomal CYPs, key enzymes for xenobiotic metabolism and steroidogenesis and important drug targets and biocatalysts, the electrons are transferred by NADPH-cytochrome P450 oxidoreductase (CPR). No structure of a mammalian CYP–CPR complex has been solved experimentally, hindering understanding of the determinants of electron transfer (ET), which is often rate-limiting for CYP reactions. Here, we investigated the interactions between membrane-bound CYP 1A1, an antitumor drug target, and CPR by a multiresolution computational approach. We find that upon binding to CPR, the CYP 1A1 catalytic domain becomes less embedded in the membrane and reorients, indicating that CPR may affect ligand passage to the CYP active site. Despite the constraints imposed by membrane binding, we identify several arrangements of CPR around CYP 1A1 that are compatible with ET. In the complexes, the interactions of the CPR FMN domain with the proximal side of CYP 1A1 are supplemented by more transient interactions of the CPR NADP domain with the distal side of CYP 1A1. Computed ET rates and pathways agree well with available experimental data and suggest why the CYP–CPR ET rates are low compared to those of soluble bacterial CYPs.

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