Cargando…

The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo

Cytochrome (CYP) 450 isoenzymes are the basic enzymes involved in Phase I biotransformation. The most important role in biotransformation belongs to CYP3A4, CYP2D6, CYP2C9, CYP2C19 and CYP1A2. Inhibition and induction of CYP isoenzymes caused by drugs are important and clinically relevant pharmacoki...

Descripción completa

Detalles Bibliográficos
Autores principales: Sychev, Dmitrij A, Ashraf, Ghulam Md, Svistunov, Andrey A, Maksimov, Maksim L, Tarasov, Vadim V, Chubarev, Vladimir N, Otdelenov, Vitalij A, Denisenko, Natal’ja P, Barreto, George E, Aliev, Gjumrakch
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5951216/
https://www.ncbi.nlm.nih.gov/pubmed/29780235
http://dx.doi.org/10.2147/DDDT.S149069
_version_ 1783322992540909568
author Sychev, Dmitrij A
Ashraf, Ghulam Md
Svistunov, Andrey A
Maksimov, Maksim L
Tarasov, Vadim V
Chubarev, Vladimir N
Otdelenov, Vitalij A
Denisenko, Natal’ja P
Barreto, George E
Aliev, Gjumrakch
author_facet Sychev, Dmitrij A
Ashraf, Ghulam Md
Svistunov, Andrey A
Maksimov, Maksim L
Tarasov, Vadim V
Chubarev, Vladimir N
Otdelenov, Vitalij A
Denisenko, Natal’ja P
Barreto, George E
Aliev, Gjumrakch
author_sort Sychev, Dmitrij A
collection PubMed
description Cytochrome (CYP) 450 isoenzymes are the basic enzymes involved in Phase I biotransformation. The most important role in biotransformation belongs to CYP3A4, CYP2D6, CYP2C9, CYP2C19 and CYP1A2. Inhibition and induction of CYP isoenzymes caused by drugs are important and clinically relevant pharmacokinetic mechanisms of drug interaction. Investigation of the activity of CYP isoenzymes by using phenotyping methods (such as the determination of the concentration of specific substrates and metabolites in biological fluids) during drug administration provides the prediction of negative side effects caused by drug interaction. In clinical practice, the process of phenotyping of CYP isoenzymes and some endogenous substrates in the ratio of cortisol to 6β-hydroxycortisol in urine for the evaluation of CYP3A4 activity has been deemed to be a quite promising, safe and minimally invasive method for patients nowadays.
format Online
Article
Text
id pubmed-5951216
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Dove Medical Press
record_format MEDLINE/PubMed
spelling pubmed-59512162018-05-18 The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo Sychev, Dmitrij A Ashraf, Ghulam Md Svistunov, Andrey A Maksimov, Maksim L Tarasov, Vadim V Chubarev, Vladimir N Otdelenov, Vitalij A Denisenko, Natal’ja P Barreto, George E Aliev, Gjumrakch Drug Des Devel Ther Review Cytochrome (CYP) 450 isoenzymes are the basic enzymes involved in Phase I biotransformation. The most important role in biotransformation belongs to CYP3A4, CYP2D6, CYP2C9, CYP2C19 and CYP1A2. Inhibition and induction of CYP isoenzymes caused by drugs are important and clinically relevant pharmacokinetic mechanisms of drug interaction. Investigation of the activity of CYP isoenzymes by using phenotyping methods (such as the determination of the concentration of specific substrates and metabolites in biological fluids) during drug administration provides the prediction of negative side effects caused by drug interaction. In clinical practice, the process of phenotyping of CYP isoenzymes and some endogenous substrates in the ratio of cortisol to 6β-hydroxycortisol in urine for the evaluation of CYP3A4 activity has been deemed to be a quite promising, safe and minimally invasive method for patients nowadays. Dove Medical Press 2018-05-08 /pmc/articles/PMC5951216/ /pubmed/29780235 http://dx.doi.org/10.2147/DDDT.S149069 Text en © 2018 2018 Sychev et al. This work is published and licensed by Dove Medical Press Limited The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed.
spellingShingle Review
Sychev, Dmitrij A
Ashraf, Ghulam Md
Svistunov, Andrey A
Maksimov, Maksim L
Tarasov, Vadim V
Chubarev, Vladimir N
Otdelenov, Vitalij A
Denisenko, Natal’ja P
Barreto, George E
Aliev, Gjumrakch
The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
title The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
title_full The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
title_fullStr The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
title_full_unstemmed The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
title_short The cytochrome P450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
title_sort cytochrome p450 isoenzyme and some new opportunities for the prediction of negative drug interaction in vivo
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5951216/
https://www.ncbi.nlm.nih.gov/pubmed/29780235
http://dx.doi.org/10.2147/DDDT.S149069
work_keys_str_mv AT sychevdmitrija thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT ashrafghulammd thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT svistunovandreya thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT maksimovmaksiml thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT tarasovvadimv thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT chubarevvladimirn thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT otdelenovvitalija thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT denisenkonataljap thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT barretogeorgee thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT alievgjumrakch thecytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT sychevdmitrija cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT ashrafghulammd cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT svistunovandreya cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT maksimovmaksiml cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT tarasovvadimv cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT chubarevvladimirn cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT otdelenovvitalija cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT denisenkonataljap cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT barretogeorgee cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo
AT alievgjumrakch cytochromep450isoenzymeandsomenewopportunitiesforthepredictionofnegativedruginteractioninvivo