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{{Infobox_gene}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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| update_citations = yes
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{{GNF_Protein_box
| image = PBB_Protein_CYP1A2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2hi4.
| Name = Cytochrome P450, family 1, subfamily A, polypeptide 2
| HGNCid = 2596
| Symbol = CYP1A2
| AltSymbols =; CP12; P3-450; P450(PA)
| OMIM = 124060
| ECnumber = 
| Homologene = 68082
| MGIid = 88589
| GeneAtlas_image1 = PBB_GE_CYP1A2_207609_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYP1A2_207608_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1544
    | Hs_Ensembl = ENSG00000140505
    | Hs_RefseqProtein = NP_000752
    | Hs_RefseqmRNA = NM_000761
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 72828237
    | Hs_GenLoc_end = 72835994
    | Hs_Uniprot = P05177
    | Mm_EntrezGene = 13077
    | Mm_Ensembl = ENSMUSG00000032310
    | Mm_RefseqmRNA = NM_009993
    | Mm_RefseqProtein = NP_034123
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 57475074
    | Mm_GenLoc_end = 57481792
    | Mm_Uniprot = P00186
  }}
}}
{{SI}}


'''Cytochrome P450 1A2''' (abbreviated '''CYP1A2'''), a member of the [[cytochrome P450]] mixed-function oxidase system, is involved in the metabolism of [[xenobiotic]]s in the body.<ref name="pmid15128046">{{cite journal | vauthors = Nelson DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, Nebert DW | title = Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants | journal = Pharmacogenetics | volume = 14 | issue = 1 | pages = 1–18 | date = Jan 2004 | pmid = 15128046 | doi = 10.1097/00008571-200401000-00001 }}</ref> In humans, the CYP1A2 enzyme is encoded by the ''CYP1A2'' [[gene]].<ref name="pmid3681487">{{cite journal | vauthors = Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ | title = Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15 | journal = Journal of Experimental Pathology | volume = 3 | issue = 1 | pages = 1–17 | year = 1987 | pmid = 3681487 | doi =  }}</ref>


'''Cytochrome P450 1A2''' (abbreviated '''CYP1A2'''), a member of the [[cytochrome P450]] mixed-function oxidase system, is involved in the metabolism of [[xenobiotic]]s in the body.
== Function ==


Expression of CYP1A2 appears to be induced by various dietary constituents.<ref>{{cite journal |author=Fontana R, Lown K, Paine M, Fortlage L, Santella R, Felton J, Knize M, Greenberg A, Watkins P |title=Effects of a chargrilled meat diet on expression of CYP3A, CYP1A, and P-glycoprotein levels in healthy volunteers |journal=Gastroenterology |volume=117 |issue=1 |pages=89-98 |year=1999 |pmid=10381914}}</ref>
CYP1A2 is a member of the [[cytochrome P450]] superfamily of enzymes. The cytochrome P450 proteins are [[monooxygenase]]s which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP1A2 localizes to the [[endoplasmic reticulum]] and its expression is induced by some [[polycyclic aromatic hydrocarbon]]s (PAHs), some of which are found in cigarette smoke. The enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include [[caffeine]], aflatoxin B1, and [[paracetamol]] (acetaminophen). The transcript from this gene contains four Alu sequences flanked by direct repeats in the 3' untranslated region.<ref name="entrez">{{cite web | title = Entrez Gene: cytochrome P450| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1544| accessdate = }}</ref>


<br clear=all>
CYP1A2 also metabolizes [[polyunsaturated fatty acid]]s into signaling molecules that have physiological as well as pathological activities.  It has monoxygenase activity for certain of these fatty acids in that it metabolizes [[arachidonic acid]] to 19-hydroxyeicosatetraenoic acid (19-HETE) (see [[20-Hydroxyeicosatetraenoic acid]]) but also has [[epoxygenase]] activity in that it metabolizes [[docosahexaenoic acid]] to [[epoxide]]s, primarily 19''R'',20''S''-epoxyeicosapentaenoic acid and 19''S'',20''R''-epoxyeicosapentaenoic acid isomers (termed 19,20-EDP) and similarly metabolizes [[eicosapentaenoic acid]] to epoxides, primarily 17''R'',18''S''-eicosatetraenic acid and 17''S'',18''R''-eicosatetraenic acid isomers (termed 17,18-EEQ).<ref>{{cite journal | vauthors = Westphal C, Konkel A, Schunck WH | title = CYP-eicosanoids--a new link between omega-3 fatty acids and cardiac disease? | journal = Prostaglandins & Other Lipid Mediators | volume = 96 | issue = 1–4 | pages = 99–108 | date = Nov 2011 | pmid = 21945326 | doi = 10.1016/j.prostaglandins.2011.09.001 }}</ref>


==CYP1A2 Ligands==
19-HETE is an inhibitor of 20-HETE, a broadly active signaling molecule, e.g. it constricts [[arteriole]]s, elevates blood pressure, promotes [[inflammation]] responses, and stimulates the growth of various types of tumor cells; however the in vivo ability and significance of 19-HETE in inhibiting 20-HETE has not been demonstrated (see [[20-Hydroxyeicosatetraenoic acid]]). The EDP (see [[Epoxydocosapentaenoic acid]]) and EEQ (see [[epoxyeicosatetraenoic acid]]) metabolites have a broad range of activities. In various animal models and in vitro studies on animal and human tissues, they decrease hypertension and pain perception; suppress inflammation; inhibit [[angiogenesis]], endothelial cell migration and endothelial cell proliferation; and inhibit the growth and metastasis of human breast and prostate cancer cell lines.<ref name="ReferenceA">{{cite journal | vauthors = Fleming I | title = The pharmacology of the cytochrome P450 epoxygenase/soluble epoxide hydrolase axis in the vasculature and cardiovascular disease | journal = Pharmacological Reviews | volume = 66 | issue = 4 | pages = 1106–40 | date = Oct 2014 | pmid = 25244930 | doi = 10.1124/pr.113.007781 }}</ref><ref>{{cite journal | vauthors = Zhang G, Kodani S, Hammock BD | title = Stabilized epoxygenated fatty acids regulate inflammation, pain, angiogenesis and cancer | journal = Progress in Lipid Research | volume = 53 | pages = 108–23 | date = Jan 2014 | pmid = 24345640 | doi = 10.1016/j.plipres.2013.11.003 | pmc=3914417}}</ref><ref>{{cite journal | vauthors = He J, Wang C, Zhu Y, Ai D | title = Soluble epoxide hydrolase: A potential target for metabolic diseases | journal = Journal of Diabetes | date = Dec 2015 | pmid = 26621325 | doi = 10.1111/1753-0407.12358 | volume=8 | issue = 3 | pages=305–13}}</ref><ref name="Wagner K 2014">{{cite journal | vauthors = Wagner K, Vito S, Inceoglu B, Hammock BD | title = The role of long chain fatty acids and their epoxide metabolites in nociceptive signaling | journal = Prostaglandins & Other Lipid Mediators | volume = 113-115 | pages = 2–12 | date = Oct 2014 | pmid = 25240260 | doi = 10.1016/j.prostaglandins.2014.09.001 | pmc=4254344}}</ref> It is suggested that the EDP and EEQ metabolites function in humans as they do in animal models and that, as products of the [[omega-3 fatty acid]]s, docosahexaenoic acid and eicosapentaenoic acid, the EDP and EEQ metabolites contribute to many of the beneficial effects attributed to dietary omega-3 fatty acids.<ref name="ReferenceA" /><ref name="Wagner K 2014" /><ref>{{cite journal | vauthors = Fischer R, Konkel A, Mehling H, Blossey K, Gapelyuk A, Wessel N, von Schacky C, Dechend R, Muller DN, Rothe M, Luft FC, Weylandt K, Schunck WH | title = Dietary omega-3 fatty acids modulate the eicosanoid profile in man primarily via the CYP-epoxygenase pathway | journal = Journal of Lipid Research | volume = 55 | issue = 6 | pages = 1150–1164 | date = Mar 2014 | pmid = 24634501 | doi = 10.1194/jlr.M047357 | pmc=4031946}}</ref>  EDP and EEQ metabolites are short-lived, being inactivated within seconds or minutes of formation by [[epoxide hydrolase]]s, particularly [[soluble epoxide hydrolase]], and therefore act locally.
Table of selected [[enzyme substrate|substrates]], [[enzyme induction and inhibition|inducers]] and [[enzyme induction and inhibition|inhibitors]] of CYP1A2<sup>1</sup>
 
{| class="wikitable" width=100%
CYP1A2 is not regarded as being a major contributor to forming the cited epoxides<ref name="Wagner K 2014" /> but could act locally in certain tissues to do so.
! Substrates !! Inhibitors !! Inducers
 
|-  
== Effect of diet ==
| '''Often mentioned''' <ref name=importance> Mentioned both in the reference named FASS and were previously mentioned in Wikipedia. Further contributions may follow other systems</ref>:
 
*some [[Antidepressant]]s
Expression of CYP1A2 appears to be induced by various dietary constituents.<ref>{{cite journal | vauthors = Fontana RJ, Lown KS, Paine MF, Fortlage L, Santella RM, Felton JS, Knize MG, Greenberg A, Watkins PB | title = Effects of a chargrilled meat diet on expression of CYP3A, CYP1A, and P-glycoprotein levels in healthy volunteers | journal = Gastroenterology | volume = 117 | issue = 1 | pages = 89–98 | date = Jul 1999 | pmid = 10381914 | doi = 10.1016/S0016-5085(99)70554-8 }}</ref> Vegetables such as cabbages, cauliflower and broccoli are known to increase levels of CYP1A2. Lower activity of CYP1A2 in South Asians appears to be due to cooking these vegetables in curries using ingredients such as [[cumin]] and [[turmeric]], ingredients known to inhibit the enzyme.<ref name="sydnews">{{citation|url=http://sydney.edu.au/news/pharm/1311.html?newsstoryid=7969|work= University of Sydney Faculty of Pharmacy News |title=South Asians and Europeans react differently to common drugs|date= 17 October 2011|author=Sanday, Kate }}</ref>
**[[Amitriptyline]] ([[tricyclic antidepressant]])
 
**[[Imipramine]] (antidepressant)
== Ligands ==
**[[Clomipramine]] (tricyclic antidepressant)  
 
*[[Clozapine]] ([[atypical antipsychotic]])
Following is a table of selected [[enzyme substrate|substrates]], [[enzyme induction and inhibition|inducers]] and [[enzyme induction and inhibition|inhibitors]] of CYP1A2.
*[[Caffeine]] ([[stimulant]])
*[[Olanzapine]] (atypical antipsychotic)
*[[Ropivacaine]] ([[local anaesthetic]])
*[[Theophylline]] (Xanthine)
*[[Zolmitriptan]] ([[Serotonin receptor agonist]])


'''Other''':
Inhibitors of CYP1A2 can be classified by their [[potency (pharmacology)|potency]], such as:
*[[cyclobenzaprine]] ([[muscle relaxant]], [[depressant]])
*'''Strong inhibitor''' being one that causes at least a 5-fold increase in the plasma [[area under the curve (pharmacokinetics)|AUC values]], or more than 80% decrease in [[clearance (medicine)|clearance]] of substrates.<ref name=":0">{{Cite web|url=http://www.fda.gov/Drugs/DevelopmentApprovalProcess/DevelopmentResources/DrugInteractionsLabeling/ucm093664.htm#classInhibit|title=Drug Interactions & Labeling - Drug Development and Drug Interactions: Table of Substrates, Inhibitors and Inducers|last=Center for Drug Evaluation and Research|website=www.fda.gov|language=en|access-date=2016-06-01}}</ref>
*[[estradiol]] (in [[hypoestrogenism]])
*'''Moderate inhibitor''' being one that causes at least a 2-fold increase in the plasma AUC values, or 50-80% decrease in clearance of substrates.<ref name=":0" />
*[[fluvoxamine]] ([[SSRI]] antidepressant)
*'''Weak inhibitor''' being one that causes at least a 1.25-fold but less than 2-fold increase in the plasma AUC values, or 20-50% decrease in clearance of substrates.<ref name=":0" />
*[[haloperidol]] ([[Typical antipsychotic]])
*[[ondansetron]] ([[5-HT3 antagonist]])
*[[mexiletine]] ([[Antiarrhythmic agent]])  
*[[Melatonin]] (antioxidant, sleep-inducer)
*[[Tamoxifen]] ([[selective estrogen receptor modulator|SERM]])  
*[[naproxen]] ([[NSAID]])
*[[paracetamol]] ([[analgesic]], [[antipyretic]])
*[[phenacetin]] ([[analgesic]])
*[[propranolol]] ([[beta blocker]])
*[[riluzole]] (in [[amyotrophic lateral sclerosis]])
*[[tacrine]] ([[parasympathomimetic]])
*[[tizanidine]] (α-2 [[adrenergic agonist]])
*[[Verapamil]] ([[calcium channel blocker]])
*[[warfarin]] ([[anticoagulant]])
*[[zileuton]] (in [[asthma]])
*[[lidocaine]] ([[local anesthetic]], [[antiarrhythmic]])


|| '''Strong''' <ref name=FASS>[http://www.fass.se/LIF/produktfakta/fakta_lakare_artikel.jsp?articleID=18352 Swedish environmental classification of pharmaceuticals] Facts for prescribers (Fakta för förskrivare)</ref>:  
{| class="wikitable"
*[[Ciprofloxacin]] ([[fluoroquinolone]] [[bactericidal]])  
! Substrates !! Inhibitors !! Inducers
|- valign="top"
|
*many [[antidepressant]]s
**[[amitriptyline]]<ref name=Flockhart/><ref name=FASS>[http://www.fass.se/LIF/produktfakta/fakta_lakare_artikel.jsp?articleID=18352 Swedish environmental classification of pharmaceuticals] - [[FASS (drug catalog)]] - Facts for prescribers (Fakta för förskrivare). Retrieved July 2011</ref> ([[tricyclic antidepressant]])
**[[clomipramine]]<ref name=Flockhart/><ref name=FASS/> (tricyclic antidepressant)
**[[imipramine]]<ref name=Flockhart/><ref name=FASS/> (tricyclic antidepressant)
**[[agomelatine]]
**[[duloxetine]]
*some [[atypical antipsychotic]]s
**[[clozapine]]<ref name=Flockhart/><ref name=FASS/>
**[[olanzapine]]<ref name=Flockhart/><ref name=FASS/>
*[[haloperidol]]<ref name=Flockhart/><ref name=FASS/> ([[typical antipsychotic]])
*[[caffeine]]<ref name=Flockhart/><ref name=FASS/> ([[xanthine]], [[stimulant]])
*[[ropivacaine]]<ref name=Flockhart/><ref name=FASS/> ([[local anaesthetic]])
*[[theophylline]]<ref name=Flockhart/><ref name=FASS/> ([[xanthine]], in [[respiratory disease]]s)
*[[zolmitriptan]]<ref name=Flockhart/><ref name=FASS/> ([[serotonin receptor agonist]])
*[[melatonin]]<ref name=FASS/> (antioxidant, sleep-inducer)
*[[tamoxifen]]<ref name=FASS/> ([[selective estrogen receptor modulator|SERM]]) 
*[[erlotinib]]<ref>{{cite web |title=Erlotinib |url = https://www.drugs.com/ppa/erlotinib.html | quote = Metabolized primarily by CYP3A4 and, to a lesser degree, by CYP1A2 and the extrahepatic isoform CYP1A1}}</ref> (Tarceva, a [[tyrosine kinase inhibitor]])
*[[cyclobenzaprine]]<ref name=Flockhart/> ([[muscle relaxant]], [[depressant]])
*[[estradiol]]<ref name=Flockhart/> (in [[hypoestrogenism]])
*[[fluvoxamine]]<ref name=Flockhart/> ([[SSRI]] antidepressant)
*[[mexiletine]]<ref name=Flockhart/> ([[antiarrhythmic agent]])
*[[naproxen]]<ref name=Flockhart/> ([[NSAID]])
*[[ondansetron]]<ref name=Flockhart/> ([[5-HT3 antagonist]])
*[[phenacetin]]<ref name=Flockhart/> ([[analgesic]])
*[[paracetamol]]<ref name=Flockhart/> ([[analgesic]], [[antipyretic]])
*[[propranolol]]<ref name=Flockhart/>  ([[beta blocker]])
*[[riluzole]]<ref name=Flockhart/> (in [[amyotrophic lateral sclerosis]])
*[[tacrine]]<ref name=Flockhart/> ([[parasympathomimetic]])
*[[tizanidine]]<ref name=Flockhart/> (α-2 [[adrenergic agonist]])
*[[verapamil]]<ref name=Flockhart/> ([[calcium channel blocker]])
*[[warfarin]]<ref name=Flockhart/> ([[anticoagulant]])
*[[zileuton]]<ref name=Flockhart/> (in [[asthma]])
|| '''Strong'''<!--inhibitors-->:
*[[ciprofloxacin]]<ref name=Flockhart/><ref name=FASS /> ([[fluoroquinolone]] [[bactericidal]])  
*Many other [[fluoroquinolone]]s ([[broad-spectrum antibiotics]])  
*Many other [[fluoroquinolone]]s ([[broad-spectrum antibiotics]])  
*[[Fluvoxamine]] ([[SSRI]] antidepressant)  
*[[fluvoxamine]]<ref name=Flockhart/><ref name=FASS/> ([[SSRI]] antidepressant)  
*[[Verapamil]] ([[calcium channel blocker]])
*[[verapamil]] (a non-[[dihydropyridine]] [[calcium channel blocker]]) according to [[FASS (drug formulary)|FASS]], a Swedish national authority.<ref name=FASS/> However, [[UpToDate]] attributes verapamil to ''weak'' CYP1A2 inhibitor<ref name="UpToDate">{{cite web | title=Verapamil: Drug information. Lexicomp| website=UpToDate | url=https://www.uptodate.com/contents/verapamil-drug-information | access-date=2019-01-13 | quote=Metabolism/Transport Effects: Substrate of CYP1A2 (minor), CYP2B6 (minor), CYP2C9 (minor), CYP2E1 (minor), CYP3A4 (major), P-glycoprotein/ABCB1; Note: Assignment of Major/Minor substrate status based on clinically relevant drug interaction potential; Inhibits CYP1A2 (weak), CYP3A4 (moderate), P-glycoprotein/ABCB1}}</ref>


'''unspecified''':
'''Moderate'''<!--inhibitors-->
*[[amiodarone]] ([[antiarrhythmic agent]])
*[[St. John's wort]]<ref name=Dostalek>{{cite journal | vauthors = Dostalek M, Pistovcakova J, Jurica J, Sulcová A, Tomandl J | title = The effect of St John's wort (hypericum perforatum) on cytochrome p450 1a2 activity in perfused rat liver | journal = Biomedical Papers of the Medical Faculty of the University Palacký, Olomouc, Czechoslovakia | volume = 155 | issue = 3 | pages = 253–7 | date = Sep 2011 | pmid = 22286810 | doi = 10.5507/bp.2011.047 }}</ref>
*[[cimetidine]] ([[H2-receptor antagonist]])
*'''Herbs and herbal Teas'''
*furafylline
**Peppermint, German Chamomile(Chamazulene), and Dandelion Teas<ref>{{cite journal|last=Maliakal|first=Pius|title=Effect of herbal teas on hepatic drug metabolizing enzymes in rats|journal=Journal of Pharmacy and Pharmacology|volume=53|issue=10|pages=1323–1329|doi=10.1211/0022357011777819|year=2001}}</ref>
*[[interferon]] ([[antiviral]], [[antiseptic]], [[antioncogenic]])  
*[[methoxsalen]] (in [[psoriasis]])
*[[caffeine]] ([[stimulant]])
*[[echinacea]] ([[Immunostimulator]])
*[[enoxacin]] ([[antibacterial ]])
*[[mexiletine]] ([[Antiarrhythmic agent]])  
*[[hormonal contraception]]
*[[zileuton]] (in [[asthma]]) 


|| '''Often mentioned'''<ref name=importance/>:  
'''Weak'''<!--inhibitors-->
*[[tobacco]]
*[[cimetidine]]<ref name=Flockhart>{{cite web |author=Flockhart DA |title=Drug Interactions: Cytochrome P<sub>450</sub> Drug Interaction Table |publisher=[[Indiana University School of Medicine]] |year=2007 |url=http://medicine.iupui.edu/flockhart/table.htm}} Retrieved on July 2011</ref> ([[H2-receptor antagonist]])
*[[caffeine]]<ref name="url_FDA">{{cite web | url = http://www.fda.gov/drugs/developmentapprovalprocess/developmentresources/druginteractionslabeling/ucm093664.htm | title = Drug Development and Drug Interactions: Table of Substrates, Inhibitors and Inducers | publisher = U.S. Food and Drug Administration }}</ref>
*echinacea<ref name="pmid14749695">{{cite journal|date=Jan 2004|title=The effect of echinacea (Echinacea purpurea root) on cytochrome P450 activity in vivo|journal=Clinical Pharmacology and Therapeutics|volume=75|issue=1|pages=89–100|doi=10.1016/j.clpt.2003.09.013|pmid=14749695|vauthors=Gorski JC, Huang SM, Pinto A, Hamman MA, Hilligoss JK, Zaheer NA, Desai M, Miller M, Hall SD}}</ref>


'''Other''':  
'''<!--inhibitors of-->Unspecified potency''':
*Some foods
*[[amiodarone]]<ref name=Flockhart/> ([[antiarrhythmic agent]])
**[[grapefruit juice]] (its bitter flavanone [[naringenin]])<ref>{{cite journal |author=Edwards DJ, Bernier SM |title=Inhibitory effect of grapefruit juice and its bitter principal, naringenin, on CYP1A2 dependent metabolism of caffeine in man |journal=Life Sciences |volume=59 |issue=13 |pages=1025-1030 |year=1996 |pmid=8485024}}</ref>
*[[interferon]]<ref name=Flockhart/> ([[Antiviral drug|antiviral]], [[antiseptic]], [[antioncogenic]])
**[[broccoli]]  
*[[methoxsalen]]<ref name=Flockhart/> (in [[psoriasis]])
**brussel sprouts
*[[Mibefradil]]<ref name=Flockhart/> ([[calcium channel blocker]])
**chargrilled [[meat]]  
*'''Some foods'''
*[[insulin]] (in [[diabetes]])
**[[grapefruit juice]] (its bitter [[flavanone]] [[naringenin]])<ref>{{cite journal | vauthors = Fuhr U, Klittich K, Staib AH | title = Inhibitory effect of grapefruit juice and its bitter principal, naringenin, on CYP1A2 dependent metabolism of caffeine in man | journal = British Journal of Clinical Pharmacology | volume = 35 | issue = 4 | pages = 431–6 | date = Apr 1993 | pmid = 8485024 | pmc = 1381556 | doi = 10.1111/j.1365-2125.1993.tb04162.x }}</ref>
*[[modafinil]] ([[eugeroic]])
**[[cumin]]<ref name="sydnews"/>
*[[nafcillin]] ([[beta-lactam antibiotic]])
**[[turmeric]]<ref name="sydnews"/>
*[[omeprazole]] ([[proton pump inhibitor]])  
*[[isoniazid]]<ref>{{cite journal|title=Isoniazid is a mechanism-based inhibitor of cytochrome P450 1A2, 2A6, 2C19 and 3A4 isoforms in human liver microsomes.|vauthors=Wen X, Wang JS, Neuvonen PJ, Backman JT |pmid=11868802|volume=57|issue=11 |date=Jan 2002|journal=Eur J Clin Pharmacol|pages=799–804|doi=10.1007/s00228-001-0396-3}}</ref>
*[[hyperforin]] (constituent of [[St Johns Wort]]) ([[antidepressant]])  
|| <!--inducers-->
*[[carbamazepine]] ([[anticonvulsant]])
*[[tobacco]]<ref name=Flockhart/><ref name=FASS/>
*[[phenobarbital]] ([[anticonvulsant]])  
*'''Some foods/herbs'''
*[[rifampicin]] ([[bactericidal]])  
**[[broccoli]]<ref name="sydnews"/><ref name=Flockhart/>
**[[brussels sprout]]s<ref name=Flockhart/>
**[[grilling|chargrill]]ed [[meat]]<ref name=Flockhart/>
**[[cauliflower]]<ref name="sydnews"/>
*[[insulin]]<ref name=Flockhart/> (in [[diabetes]])  
*[[methylcholanthrene]]<ref name=Flockhart/> ([[carcinogen]])
*[[modafinil]]<ref name=Flockhart/> ([[eugeroic]])  
*[[nafcillin]]<ref name=Flockhart/> ([[beta-lactam antibiotic]])  
*[[beta-Naphthoflavone]]<ref name=Flockhart/> ([[chemopreventive]])
*[[omeprazole]]<ref name=Flockhart/> ([[proton pump inhibitor]])  
|-
|-
|}
|}
== See also ==
*[[Cytochrome P450 oxidase]]


== References ==
== References ==
{{reflist|2}}
{{reflist|35em}}
* {{cite journal |author=Meijerman I, Beijnen J, Schellens J |title=Herb-drug interactions in oncology: focus on mechanisms of induction |journal=Oncologist |volume=11 |issue=7 |pages=742-52 |year= |pmid=16880233}}


==Further reading==
==External links==
{{refbegin | 2}}
* {{UCSC gene info|CYP1A2}}
{{PBB_Further_reading
 
| citations =  
== Further reading ==
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
{{refbegin|35em}}
*{{cite journal | author=Landi MT, Sinha R, Lang NP, Kadlubar FF |title=Human cytochrome P4501A2. |journal=IARC Sci. Publ. |volume= |issue= 148 |pages= 173-95 |year= 1999 |pmid= 10493258 |doi=  }}
* {{cite journal | vauthors = Meijerman I, Beijnen JH, Schellens JH | title = Herb-drug interactions in oncology: focus on mechanisms of induction | journal = The Oncologist | volume = 11 | issue = 7 | pages = 742–52 | year = 2006 | pmid = 16880233 | doi = 10.1634/theoncologist.11-7-742 }}
*{{cite journal | author=Nelson DR, Zeldin DC, Hoffman SM, ''et al.'' |title=Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. |journal=Pharmacogenetics |volume=14 |issue= 1 |pages= 1-18 |year= 2004 |pmid= 15128046 |doi=  }}
* {{cite journal | vauthors = Smith G, Stubbins MJ, Harries LW, Wolf CR | title = Molecular genetics of the human cytochrome P450 monooxygenase superfamily | journal = Xenobiotica | volume = 28 | issue = 12 | pages = 1129–65 | date = Dec 1998 | pmid = 9890157 | doi = 10.1080/004982598238868 }}
*{{cite journal  | author=Ikeya K, Jaiswal AK, Owens RA, ''et al.'' |title=Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1399-408 |year= 1990 |pmid= 2575218 |doi= }}
* {{cite journal | vauthors = Landi MT, Sinha R, Lang NP, Kadlubar FF | title = Human cytochrome P4501A2 | journal = IARC Scientific Publications | volume = | issue = 148 | pages = 173–95 | year = 1999 | pmid = 10493258 | doi =  }}
*{{cite journal | author=Butler MA, Iwasaki M, Guengerich FP, Kadlubar FF |title=Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 20 |pages= 7696-700 |year= 1989 |pmid= 2813353 |doi= }}
* {{cite journal | vauthors = Ikeya K, Jaiswal AK, Owens RA, Jones JE, Nebert DW, Kimura S | title = Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression | journal = Molecular Endocrinology | volume = 3 | issue = 9 | pages = 1399–408 | date = Sep 1989 | pmid = 2575218 | doi = 10.1210/mend-3-9-1399 }}
*{{cite journal | author=Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH |title=Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. |journal=DNA |volume=4 |issue= 5 |pages= 395-400 |year= 1986 |pmid= 3000715 |doi= }}
* {{cite journal | vauthors = Butler MA, Iwasaki M, Guengerich FP, Kadlubar FF | title = Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 20 | pages = 7696–700 | date = Oct 1989 | pmid = 2813353 | pmc = 298137 | doi = 10.1073/pnas.86.20.7696 }}
*{{cite journal | author=Quattrochi LC, Pendurthi UR, Okino ST, ''et al.'' |title=Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 18 |pages= 6731-5 |year= 1986 |pmid= 3462722 |doi= }}
* {{cite journal | vauthors = Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH | title = Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6 | journal = DNA | volume = 4 | issue = 5 | pages = 395–400 | date = Oct 1985 | pmid = 3000715 | doi = 10.1089/dna.1985.4.395 }}
*{{cite journal | author=Wrighton SA, Campanile C, Thomas PE, ''et al.'' |title=Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat. |journal=Mol. Pharmacol. |volume=29 |issue= 4 |pages= 405-10 |year= 1986 |pmid= 3517618 |doi=  }}
* {{cite journal | vauthors = Quattrochi LC, Pendurthi UR, Okino ST, Potenza C, Tukey RH | title = Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 83 | issue = 18 | pages = 6731–5 | date = Sep 1986 | pmid = 3462722 | pmc = 386583 | doi = 10.1073/pnas.83.18.6731 }}
*{{cite journal | author=Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ |title=Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15. |journal=J. Exp. Pathol. |volume=3 |issue= 1 |pages= 1-17 |year= 1988 |pmid= 3681487 |doi=  }}
* {{cite journal | vauthors = Wrighton SA, Campanile C, Thomas PE, Maines SL, Watkins PB, Parker G, Mendez-Picon G, Haniu M, Shively JE, Levin W | title = Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat | journal = Molecular Pharmacology | volume = 29 | issue = 4 | pages = 405–10 | date = Apr 1986 | pmid = 3517618 | doi =  }}
*{{cite journal  | author=Jaiswal AK, Nebert DW, Gonzalez FJ |title=Human P3(450): cDNA and complete amino acid sequence. |journal=Nucleic Acids Res. |volume=14 |issue= 16 |pages= 6773-4 |year= 1986 |pmid= 3755823 |doi= }}
* {{cite journal | vauthors = Jaiswal AK, Nebert DW, Gonzalez FJ | title = Human P3(450): cDNA and complete amino acid sequence | journal = Nucleic Acids Research | volume = 14 | issue = 16 | pages = 6773–4 | date = Aug 1986 | pmid = 3755823 | pmc = 311685 | doi = 10.1093/nar/14.16.6773 }}
*{{cite journal | author=Eugster HP, Probst M, Würgler FE, Sengstag C |title=Caffeine, estradiol, and progesterone interact with human CYP1A1 and CYP1A2. Evidence from cDNA-directed expression in Saccharomyces cerevisiae. |journal=Drug Metab. Dispos. |volume=21 |issue= 1 |pages= 43-9 |year= 1993 |pmid= 8095225 |doi=  }}
* {{cite journal | vauthors = Eugster HP, Probst M, Würgler FE, Sengstag C | title = Caffeine, estradiol, and progesterone interact with human CYP1A1 and CYP1A2. Evidence from cDNA-directed expression in Saccharomyces cerevisiae | journal = Drug Metabolism and Disposition | volume = 21 | issue = 1 | pages = 43–9 | year = 1993 | pmid = 8095225 | doi =  }}
*{{cite journal | author=Schweikl H, Taylor JA, Kitareewan S, ''et al.'' |title=Expression of CYP1A1 and CYP1A2 genes in human liver. |journal=Pharmacogenetics |volume=3 |issue= 5 |pages= 239-49 |year= 1994 |pmid= 8287062 |doi= }}
* {{cite journal | vauthors = Schweikl H, Taylor JA, Kitareewan S, Linko P, Nagorney D, Goldstein JA | title = Expression of CYP1A1 and CYP1A2 genes in human liver | journal = Pharmacogenetics | volume = 3 | issue = 5 | pages = 239–49 | date = Oct 1993 | pmid = 8287062 | doi = 10.1097/00008571-199310000-00003 }}
*{{cite journal | author=Yamazaki H, Inoue K, Mimura M, ''et al.'' |title=7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes. |journal=Biochem. Pharmacol. |volume=51 |issue= 3 |pages= 313-9 |year= 1996 |pmid= 8573198 |doi= }}
* {{cite journal | vauthors = Yamazaki H, Inoue K, Mimura M, Oda Y, Guengerich FP, Shimada T | title = 7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes | journal = Biochemical Pharmacology | volume = 51 | issue = 3 | pages = 313–9 | date = Feb 1996 | pmid = 8573198 | doi = 10.1016/0006-2952(95)02178-7 }}
*{{cite journal | author=Hakkola J, Raunio H, Purkunen R, ''et al.'' |title=Detection of cytochrome P450 gene expression in human placenta in first trimester of pregnancy. |journal=Biochem. Pharmacol. |volume=52 |issue= 2 |pages= 379-83 |year= 1996 |pmid= 8694864 |doi= }}
* {{cite journal | vauthors = Hakkola J, Raunio H, Purkunen R, Pelkonen O, Saarikoski S, Cresteil T, Pasanen M | title = Detection of cytochrome P450 gene expression in human placenta in first trimester of pregnancy | journal = Biochemical Pharmacology | volume = 52 | issue = 2 | pages = 379–83 | date = Jul 1996 | pmid = 8694864 | doi = 10.1016/0006-2952(96)00216-X }}
*{{cite journal | author=Guengerich FP, Johnson WW |title=Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14741-50 |year= 1998 |pmid= 9398194 |doi= 10.1021/bi9719399 }}
* {{cite journal | vauthors = Guengerich FP, Johnson WW | title = Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems | journal = Biochemistry | volume = 36 | issue = 48 | pages = 14741–50 | date = Dec 1997 | pmid = 9398194 | doi = 10.1021/bi9719399 }}
*{{cite journal | author=Wacke R, Kirchner A, Prall F, ''et al.'' |title=Up-regulation of cytochrome P450 1A2, 2C9, and 2E1 in chronic pancreatitis. |journal=Pancreas |volume=16 |issue= 4 |pages= 521-8 |year= 1998 |pmid= 9598815 |doi= }}
* {{cite journal | vauthors = Wacke R, Kirchner A, Prall F, Nizze H, Schmidt W, Fischer U, Nitschke FP, Adam U, Fritz P, Belloc C, Drewelow B | title = Up-regulation of cytochrome P450 1A2, 2C9, and 2E1 in chronic pancreatitis | journal = Pancreas | volume = 16 | issue = 4 | pages = 521–8 | date = May 1998 | pmid = 9598815 | doi = 10.1097/00006676-199805000-00011 }}
*{{cite journal | author=Macé K, Bowman ED, Vautravers P, ''et al.'' |title=Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues. |journal=Eur. J. Cancer |volume=34 |issue= 6 |pages= 914-20 |year= 1998 |pmid= 9797707 |doi= }}
* {{cite journal | vauthors = Macé K, Bowman ED, Vautravers P, Shields PG, Harris CC, Pfeifer AM | title = Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues | journal = European Journal of Cancer | volume = 34 | issue = 6 | pages = 914–20 | date = May 1998 | pmid = 9797707 | doi = 10.1016/S0959-8049(98)00034-3 }}
*{{cite journal | author=Huang JD, Guo WC, Lai MD, ''et al.'' |title=Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese. |journal=Drug Metab. Dispos. |volume=27 |issue= 1 |pages= 98-101 |year= 1999 |pmid= 9884316 |doi=  }}
* {{cite journal | vauthors = Huang JD, Guo WC, Lai MD, Guo YL, Lambert GH | title = Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese | journal = Drug Metabolism and Disposition | volume = 27 | issue = 1 | pages = 98–101 | date = Jan 1999 | pmid = 9884316 | doi =  }}
*{{cite journal | author=Tatemichi M, Nomura S, Ogura T, ''et al.'' |title=Mutagenic activation of environmental carcinogens by microsomes of gastric mucosa with intestinal metaplasia. |journal=Cancer Res. |volume=59 |issue= 16 |pages= 3893-8 |year= 1999 |pmid= 10463577 |doi=  }}
* {{cite journal | vauthors = Tatemichi M, Nomura S, Ogura T, Sone H, Nagata H, Esumi H | title = Mutagenic activation of environmental carcinogens by microsomes of gastric mucosa with intestinal metaplasia | journal = Cancer Research | volume = 59 | issue = 16 | pages = 3893–8 | date = Aug 1999 | pmid = 10463577 | doi =  }}
}}
{{refend}}
{{refend}}


[[Category:Cytochrome P450]]
{{NLM content}}
 
== See also ==
*[[Cytochrome P450 oxidase]]
 


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Latest revision as of 05:09, 13 January 2019

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Orthologs
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Cytochrome P450 1A2 (abbreviated CYP1A2), a member of the cytochrome P450 mixed-function oxidase system, is involved in the metabolism of xenobiotics in the body.[1] In humans, the CYP1A2 enzyme is encoded by the CYP1A2 gene.[2]

Function

CYP1A2 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP1A2 localizes to the endoplasmic reticulum and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include caffeine, aflatoxin B1, and paracetamol (acetaminophen). The transcript from this gene contains four Alu sequences flanked by direct repeats in the 3' untranslated region.[3]

CYP1A2 also metabolizes polyunsaturated fatty acids into signaling molecules that have physiological as well as pathological activities. It has monoxygenase activity for certain of these fatty acids in that it metabolizes arachidonic acid to 19-hydroxyeicosatetraenoic acid (19-HETE) (see 20-Hydroxyeicosatetraenoic acid) but also has epoxygenase activity in that it metabolizes docosahexaenoic acid to epoxides, primarily 19R,20S-epoxyeicosapentaenoic acid and 19S,20R-epoxyeicosapentaenoic acid isomers (termed 19,20-EDP) and similarly metabolizes eicosapentaenoic acid to epoxides, primarily 17R,18S-eicosatetraenic acid and 17S,18R-eicosatetraenic acid isomers (termed 17,18-EEQ).[4]

19-HETE is an inhibitor of 20-HETE, a broadly active signaling molecule, e.g. it constricts arterioles, elevates blood pressure, promotes inflammation responses, and stimulates the growth of various types of tumor cells; however the in vivo ability and significance of 19-HETE in inhibiting 20-HETE has not been demonstrated (see 20-Hydroxyeicosatetraenoic acid). The EDP (see Epoxydocosapentaenoic acid) and EEQ (see epoxyeicosatetraenoic acid) metabolites have a broad range of activities. In various animal models and in vitro studies on animal and human tissues, they decrease hypertension and pain perception; suppress inflammation; inhibit angiogenesis, endothelial cell migration and endothelial cell proliferation; and inhibit the growth and metastasis of human breast and prostate cancer cell lines.[5][6][7][8] It is suggested that the EDP and EEQ metabolites function in humans as they do in animal models and that, as products of the omega-3 fatty acids, docosahexaenoic acid and eicosapentaenoic acid, the EDP and EEQ metabolites contribute to many of the beneficial effects attributed to dietary omega-3 fatty acids.[5][8][9] EDP and EEQ metabolites are short-lived, being inactivated within seconds or minutes of formation by epoxide hydrolases, particularly soluble epoxide hydrolase, and therefore act locally.

CYP1A2 is not regarded as being a major contributor to forming the cited epoxides[8] but could act locally in certain tissues to do so.

Effect of diet

Expression of CYP1A2 appears to be induced by various dietary constituents.[10] Vegetables such as cabbages, cauliflower and broccoli are known to increase levels of CYP1A2. Lower activity of CYP1A2 in South Asians appears to be due to cooking these vegetables in curries using ingredients such as cumin and turmeric, ingredients known to inhibit the enzyme.[11]

Ligands

Following is a table of selected substrates, inducers and inhibitors of CYP1A2.

Inhibitors of CYP1A2 can be classified by their potency, such as:

  • Strong inhibitor being one that causes at least a 5-fold increase in the plasma AUC values, or more than 80% decrease in clearance of substrates.[12]
  • Moderate inhibitor being one that causes at least a 2-fold increase in the plasma AUC values, or 50-80% decrease in clearance of substrates.[12]
  • Weak inhibitor being one that causes at least a 1.25-fold but less than 2-fold increase in the plasma AUC values, or 20-50% decrease in clearance of substrates.[12]
Substrates Inhibitors Inducers
Strong:

Moderate

Weak

Unspecified potency:

See also

References

  1. ↑ Nelson DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, Nebert DW (Jan 2004). "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants". Pharmacogenetics. 14 (1): 1–18. doi:10.1097/00008571-200401000-00001. PMID 15128046.
  2. ↑ Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ (1987). "Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15". Journal of Experimental Pathology. 3 (1): 1–17. PMID 3681487.
  3. ↑ "Entrez Gene: cytochrome P450".
  4. ↑ Westphal C, Konkel A, Schunck WH (Nov 2011). "CYP-eicosanoids--a new link between omega-3 fatty acids and cardiac disease?". Prostaglandins & Other Lipid Mediators. 96 (1–4): 99–108. doi:10.1016/j.prostaglandins.2011.09.001. PMID 21945326.
  5. ↑ 5.0 5.1 Fleming I (Oct 2014). "The pharmacology of the cytochrome P450 epoxygenase/soluble epoxide hydrolase axis in the vasculature and cardiovascular disease". Pharmacological Reviews. 66 (4): 1106–40. doi:10.1124/pr.113.007781. PMID 25244930.
  6. ↑ Zhang G, Kodani S, Hammock BD (Jan 2014). "Stabilized epoxygenated fatty acids regulate inflammation, pain, angiogenesis and cancer". Progress in Lipid Research. 53: 108–23. doi:10.1016/j.plipres.2013.11.003. PMC 3914417. PMID 24345640.
  7. ↑ He J, Wang C, Zhu Y, Ai D (Dec 2015). "Soluble epoxide hydrolase: A potential target for metabolic diseases". Journal of Diabetes. 8 (3): 305–13. doi:10.1111/1753-0407.12358. PMID 26621325.
  8. ↑ 8.0 8.1 8.2 Wagner K, Vito S, Inceoglu B, Hammock BD (Oct 2014). "The role of long chain fatty acids and their epoxide metabolites in nociceptive signaling". Prostaglandins & Other Lipid Mediators. 113-115: 2–12. doi:10.1016/j.prostaglandins.2014.09.001. PMC 4254344. PMID 25240260.
  9. ↑ Fischer R, Konkel A, Mehling H, Blossey K, Gapelyuk A, Wessel N, von Schacky C, Dechend R, Muller DN, Rothe M, Luft FC, Weylandt K, Schunck WH (Mar 2014). "Dietary omega-3 fatty acids modulate the eicosanoid profile in man primarily via the CYP-epoxygenase pathway". Journal of Lipid Research. 55 (6): 1150–1164. doi:10.1194/jlr.M047357. PMC 4031946. PMID 24634501.
  10. ↑ Fontana RJ, Lown KS, Paine MF, Fortlage L, Santella RM, Felton JS, Knize MG, Greenberg A, Watkins PB (Jul 1999). "Effects of a chargrilled meat diet on expression of CYP3A, CYP1A, and P-glycoprotein levels in healthy volunteers". Gastroenterology. 117 (1): 89–98. doi:10.1016/S0016-5085(99)70554-8. PMID 10381914.
  11. ↑ 11.0 11.1 11.2 11.3 11.4 Sanday, Kate (17 October 2011), "South Asians and Europeans react differently to common drugs", University of Sydney Faculty of Pharmacy News
  12. ↑ 12.0 12.1 12.2 Center for Drug Evaluation and Research. "Drug Interactions & Labeling - Drug Development and Drug Interactions: Table of Substrates, Inhibitors and Inducers". www.fda.gov. Retrieved 2016-06-01.
  13. ↑ 13.00 13.01 13.02 13.03 13.04 13.05 13.06 13.07 13.08 13.09 13.10 13.11 13.12 13.13 13.14 13.15 13.16 13.17 13.18 13.19 13.20 13.21 13.22 13.23 13.24 13.25 13.26 13.27 13.28 13.29 13.30 13.31 13.32 13.33 13.34 13.35 13.36 13.37 13.38 13.39 13.40 13.41 Flockhart DA (2007). "Drug Interactions: Cytochrome P450 Drug Interaction Table". Indiana University School of Medicine. Retrieved on July 2011
  14. ↑ 14.00 14.01 14.02 14.03 14.04 14.05 14.06 14.07 14.08 14.09 14.10 14.11 14.12 14.13 14.14 14.15 Swedish environmental classification of pharmaceuticals - FASS (drug catalog) - Facts for prescribers (Fakta för förskrivare). Retrieved July 2011
  15. ↑ "Erlotinib". Metabolized primarily by CYP3A4 and, to a lesser degree, by CYP1A2 and the extrahepatic isoform CYP1A1
  16. ↑ "Verapamil: Drug information. Lexicomp". UpToDate. Retrieved 2019-01-13. Metabolism/Transport Effects: Substrate of CYP1A2 (minor), CYP2B6 (minor), CYP2C9 (minor), CYP2E1 (minor), CYP3A4 (major), P-glycoprotein/ABCB1; Note: Assignment of Major/Minor substrate status based on clinically relevant drug interaction potential; Inhibits CYP1A2 (weak), CYP3A4 (moderate), P-glycoprotein/ABCB1
  17. ↑ Dostalek M, Pistovcakova J, Jurica J, Sulcová A, Tomandl J (Sep 2011). "The effect of St John's wort (hypericum perforatum) on cytochrome p450 1a2 activity in perfused rat liver". Biomedical Papers of the Medical Faculty of the University Palacký, Olomouc, Czechoslovakia. 155 (3): 253–7. doi:10.5507/bp.2011.047. PMID 22286810.
  18. ↑ Maliakal, Pius (2001). "Effect of herbal teas on hepatic drug metabolizing enzymes in rats". Journal of Pharmacy and Pharmacology. 53 (10): 1323–1329. doi:10.1211/0022357011777819.
  19. ↑ "Drug Development and Drug Interactions: Table of Substrates, Inhibitors and Inducers". U.S. Food and Drug Administration.
  20. ↑ Gorski JC, Huang SM, Pinto A, Hamman MA, Hilligoss JK, Zaheer NA, Desai M, Miller M, Hall SD (Jan 2004). "The effect of echinacea (Echinacea purpurea root) on cytochrome P450 activity in vivo". Clinical Pharmacology and Therapeutics. 75 (1): 89–100. doi:10.1016/j.clpt.2003.09.013. PMID 14749695.
  21. ↑ Fuhr U, Klittich K, Staib AH (Apr 1993). "Inhibitory effect of grapefruit juice and its bitter principal, naringenin, on CYP1A2 dependent metabolism of caffeine in man". British Journal of Clinical Pharmacology. 35 (4): 431–6. doi:10.1111/j.1365-2125.1993.tb04162.x. PMC 1381556. PMID 8485024.
  22. ↑ Wen X, Wang JS, Neuvonen PJ, Backman JT (Jan 2002). "Isoniazid is a mechanism-based inhibitor of cytochrome P450 1A2, 2A6, 2C19 and 3A4 isoforms in human liver microsomes". Eur J Clin Pharmacol. 57 (11): 799–804. doi:10.1007/s00228-001-0396-3. PMID 11868802.

External links

Further reading

  • Meijerman I, Beijnen JH, Schellens JH (2006). "Herb-drug interactions in oncology: focus on mechanisms of induction". The Oncologist. 11 (7): 742–52. doi:10.1634/theoncologist.11-7-742. PMID 16880233.
  • Smith G, Stubbins MJ, Harries LW, Wolf CR (Dec 1998). "Molecular genetics of the human cytochrome P450 monooxygenase superfamily". Xenobiotica. 28 (12): 1129–65. doi:10.1080/004982598238868. PMID 9890157.
  • Landi MT, Sinha R, Lang NP, Kadlubar FF (1999). "Human cytochrome P4501A2". IARC Scientific Publications (148): 173–95. PMID 10493258.
  • Ikeya K, Jaiswal AK, Owens RA, Jones JE, Nebert DW, Kimura S (Sep 1989). "Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression". Molecular Endocrinology. 3 (9): 1399–408. doi:10.1210/mend-3-9-1399. PMID 2575218.
  • Butler MA, Iwasaki M, Guengerich FP, Kadlubar FF (Oct 1989). "Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines". Proceedings of the National Academy of Sciences of the United States of America. 86 (20): 7696–700. doi:10.1073/pnas.86.20.7696. PMC 298137. PMID 2813353.
  • Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH (Oct 1985). "Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6". DNA. 4 (5): 395–400. doi:10.1089/dna.1985.4.395. PMID 3000715.
  • Quattrochi LC, Pendurthi UR, Okino ST, Potenza C, Tukey RH (Sep 1986). "Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA". Proceedings of the National Academy of Sciences of the United States of America. 83 (18): 6731–5. doi:10.1073/pnas.83.18.6731. PMC 386583. PMID 3462722.
  • Wrighton SA, Campanile C, Thomas PE, Maines SL, Watkins PB, Parker G, Mendez-Picon G, Haniu M, Shively JE, Levin W (Apr 1986). "Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat". Molecular Pharmacology. 29 (4): 405–10. PMID 3517618.
  • Jaiswal AK, Nebert DW, Gonzalez FJ (Aug 1986). "Human P3(450): cDNA and complete amino acid sequence". Nucleic Acids Research. 14 (16): 6773–4. doi:10.1093/nar/14.16.6773. PMC 311685. PMID 3755823.
  • Eugster HP, Probst M, Würgler FE, Sengstag C (1993). "Caffeine, estradiol, and progesterone interact with human CYP1A1 and CYP1A2. Evidence from cDNA-directed expression in Saccharomyces cerevisiae". Drug Metabolism and Disposition. 21 (1): 43–9. PMID 8095225.
  • Schweikl H, Taylor JA, Kitareewan S, Linko P, Nagorney D, Goldstein JA (Oct 1993). "Expression of CYP1A1 and CYP1A2 genes in human liver". Pharmacogenetics. 3 (5): 239–49. doi:10.1097/00008571-199310000-00003. PMID 8287062.
  • Yamazaki H, Inoue K, Mimura M, Oda Y, Guengerich FP, Shimada T (Feb 1996). "7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes". Biochemical Pharmacology. 51 (3): 313–9. doi:10.1016/0006-2952(95)02178-7. PMID 8573198.
  • Hakkola J, Raunio H, Purkunen R, Pelkonen O, Saarikoski S, Cresteil T, Pasanen M (Jul 1996). "Detection of cytochrome P450 gene expression in human placenta in first trimester of pregnancy". Biochemical Pharmacology. 52 (2): 379–83. doi:10.1016/0006-2952(96)00216-X. PMID 8694864.
  • Guengerich FP, Johnson WW (Dec 1997). "Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems". Biochemistry. 36 (48): 14741–50. doi:10.1021/bi9719399. PMID 9398194.
  • Wacke R, Kirchner A, Prall F, Nizze H, Schmidt W, Fischer U, Nitschke FP, Adam U, Fritz P, Belloc C, Drewelow B (May 1998). "Up-regulation of cytochrome P450 1A2, 2C9, and 2E1 in chronic pancreatitis". Pancreas. 16 (4): 521–8. doi:10.1097/00006676-199805000-00011. PMID 9598815.
  • Macé K, Bowman ED, Vautravers P, Shields PG, Harris CC, Pfeifer AM (May 1998). "Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues". European Journal of Cancer. 34 (6): 914–20. doi:10.1016/S0959-8049(98)00034-3. PMID 9797707.
  • Huang JD, Guo WC, Lai MD, Guo YL, Lambert GH (Jan 1999). "Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese". Drug Metabolism and Disposition. 27 (1): 98–101. PMID 9884316.
  • Tatemichi M, Nomura S, Ogura T, Sone H, Nagata H, Esumi H (Aug 1999). "Mutagenic activation of environmental carcinogens by microsomes of gastric mucosa with intestinal metaplasia". Cancer Research. 59 (16): 3893–8. PMID 10463577.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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