CYP1A1: Difference between revisions
Jump to navigation
Jump to search
←Redirected page to Cytochrome P450, family 1, member A1 |
No edit summary |
||
| Line 1: | Line 1: | ||
# | {{PBB|geneid=1543}} | ||
{{SI}} | |||
{{EH}} | |||
'''Cytochrome P450, family 1, subfamily A, polypeptide 1''' is a [[protein]]<ref name="pmid10493257">{{cite journal | author = Kawajiri K | title = CYP1A1 | journal = IARC scientific publications | volume = | issue = 148 | pages = 159–72 | year = 1999 | pmid = 10493257 | doi = | url = | issn = }}</ref> which in humans in encoded by the '''''CYP1A1''''' [[gene]].<ref name="pmid15128046">{{cite journal | author = 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 | year = 2004 | month = January | pmid = 15128046 | doi = | url = http://meta.wkhealth.com/pt/pt-core/template-journal/lwwgateway/media/landingpage.htm?issn=0960-314X&volume=14&issue=1&spage=1 | issn = }}</ref> The protein a member of the [[cytochrome P450]] superfamily of enzymes.<ref name="pmid9890157">{{cite journal | author = Smith G, Stubbins MJ, Harries LW, Wolf CR | title = Molecular genetics of the human cytochrome P450 monooxygenase superfamily | journal = Xenobiotica; the fate of foreign compounds in biological systems | volume = 28 | issue = 12 | pages = 1129–65 | year = 1998 | month = December | pmid = 9890157 | doi = | url = | issn = }}</ref> | |||
==Function== | |||
CYP1A1 is involved in phase I [[xenobiotic]] and [[drug metabolism]] (one substrate of it is [[theophylline]]). It is inhibited by [[fluoroquinolone]]s and [[macrolide]]s and induced by [[aromatic hydrocarbons]].<ref name="pmid8313840">{{cite journal | author = Beresford AP | title = CYP1A1: friend or foe? | journal = Drug metabolism reviews | volume = 25 | issue = 4 | pages = 503–17 | year = 1993 | pmid = 8313840 | doi = | url = | issn = }}</ref> | |||
CYP1A1 is also known as AHH (aryl hydrocarbon hydroxylase). It is involved in the metabolic activation of aromatic hydrocarbons ([[polycyclic aromatic hydrocarbons]], PAH), for example, [[benzopyrene|benzopyrene]] (BP), by transforming it to an [[epoxide]]. In this reaction, the oxidation of benzo[a]pyrene is catalysed by CYP1A1 to form BP-7,8-epoxide, which can be further oxidized by [[epoxide hydrolase]] (EH) to form BP-7,8-dihydrodiol. Finally CYP1A1 catalyses this intermediate to form BP-7,8-dihydrodiol-9,10-epoxide, which is the ultimate [[carcinogen]].<ref name="pmid8313840"/> | |||
==Regulation== | |||
The expression of the CYP1A1 and CYP1B1 genes are regulated by the [[aryl hydrocarbon receptor]], a ligand activated [[transcription factor]].<ref name="pmid17431034">{{cite journal | author = Ma Q, Lu AY | title = CYP1A induction and human risk assessment: an evolving tale of in vitro and in vivo studies | journal = Drug metabolism and disposition: the biological fate of chemicals | volume = 35 | issue = 7 | pages = 1009–16 | year = 2007 | month = July | pmid = 17431034 | doi = 10.1124/dmd.107.015826 | url = | issn = }}</ref> | |||
==Polymorphisms== | |||
Several [[polymorphism (biology)|polymorphism]]s have been identified in CYP1A1, some of which lead to more highly inducible AHH activity. CYP1A1 [[polymorphism]]s include:<ref name="pmid1707592">{{cite journal | author = Petersen DD, McKinney CE, Ikeya K, Smith HH, Bale AE, McBride OW, Nebert DW | title = Human CYP1A1 gene: cosegregation of the enzyme inducibility phenotype and an RFLP | journal = American journal of human genetics | volume = 48 | issue = 4 | pages = 720–5 | year = 1991 | month = April | pmid = 1707592 | pmc = 1682951 | doi = | url = | issn = }}</ref><ref name="pmid7901425">{{cite journal | author = Cosma G, Crofts F, Taioli E, Toniolo P, Garte S | title = Relationship between genotype and function of the human CYP1A1 gene | journal = Journal of toxicology and environmental health | volume = 40 | issue = 2-3 | pages = 309–16 | year = 1993 | pmid = 7901425 | doi = | url = | issn = }}</ref><ref name="pmid8001264">{{cite journal | author = Crofts F, Taioli E, Trachman J, Cosma GN, Currie D, Toniolo P, Garte SJ | title = Functional significance of different human CYP1A1 genotypes | journal = Carcinogenesis | volume = 15 | issue = 12 | pages = 2961–3 | year = 1994 | month = December | pmid = 8001264 | doi = | url = http://carcin.oxfordjournals.org/cgi/content/abstract/15/12/2961 | issn = }}</ref><ref name="pmid8609043">{{cite journal | author = Kiyohara C, Hirohata T, Inutsuka S | title = The relationship between aryl hydrocarbon hydroxylase and polymorphisms of the CYP1A1 gene | journal = Japanese journal of cancer research : Gann | volume = 87 | issue = 1 | pages = 18–24 | year = 1996 | month = January | pmid = 8609043 | doi = | url = | issn = }}</ref> | |||
* M1, [[thymine|T]]→[[cytosine|C]] substitution at [[nucleotide]] 3801 in the 3'-[[non-coding RNA|non-coding]] region | |||
* M2, [[adenine|A]]→[[guanine|G]] substitution at nucleotide 2455 leading to an amino acid change of [[isoleucine]] to [[valine]] at [[Codon#RNA_codon_table|codon]] 462 | |||
* M3, [[thymine|T]]→[[cytosine|C]] substitution at nucleotide 3205 in the 3'-non-coding region | |||
* M4, [[cytosine|C]]→[[adenine|A]] substitution at nucleotide 2453 leading to an amino acid change of [[threonine]] to [[asparagine]] at codon 461 | |||
{{-}} | |||
==References== | |||
{{Reflist|2}} | |||
==Further reading== | |||
{{refbegin | 2}} | |||
{{PBB_Further_reading | |||
| citations = | |||
*{{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 | author=Masson LF, Sharp L, Cotton SC, Little J |title=Cytochrome P-450 1A1 gene polymorphisms and risk of breast cancer: a HuGE review. |journal=Am. J. Epidemiol. |volume=161 |issue= 10 |pages= 901–15 |year= 2005 |pmid= 15870154 |doi= 10.1093/aje/kwi121 }} | |||
*{{cite journal | author=Hildebrandt AG, Schwarz D, Krusekopf S, ''et al.'' |title=Recalling P446. P4501A1 (CYP1A1) opting for clinical application. |journal=Drug Metab. Rev. |volume=39 |issue= 2-3 |pages= 323–41 |year= 2007 |pmid= 17786624 |doi= 10.1080/03602530701498026 }} | |||
}} | |||
{{refend}} | |||
{{SIB}} | |||
{{Cytochrome P450}} | |||
[[Category:Cytochrome P450]] | |||
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> | |||
{{PBB_Controls | |||
| update_page = yes | |||
| require_manual_inspection = no | |||
| update_protein_box = yes | |||
| update_summary = no | |||
| update_citations = no | |||
}} | |||
[[es:CYP1A1]] | |||
[[it:CYP1A1]] | |||
{{WH}} | |||
{{WS}} | |||
Revision as of 21:26, 7 January 2009
|
WikiDoc Resources for CYP1A1 |
|
Articles |
|---|
|
Media |
|
Evidence Based Medicine |
|
Clinical Trials |
|
Ongoing Trials on CYP1A1 at Clinical Trials.gov Clinical Trials on CYP1A1 at Google
|
|
Guidelines / Policies / Govt |
|
US National Guidelines Clearinghouse on CYP1A1
|
|
Books |
|
News |
|
Commentary |
|
Definitions |
|
Patient Resources / Community |
|
Directions to Hospitals Treating CYP1A1 Risk calculators and risk factors for CYP1A1
|
|
Healthcare Provider Resources |
|
Continuing Medical Education (CME) |
|
International |
|
|
|
Business |
|
Experimental / Informatics |
Please Take Over This Page and Apply to be Editor-In-Chief for this topic: There can be one or more than one Editor-In-Chief. You may also apply to be an Associate Editor-In-Chief of one of the subtopics below. Please mail us [1] to indicate your interest in serving either as an Editor-In-Chief of the entire topic or as an Associate Editor-In-Chief for a subtopic. Please be sure to attach your CV and or biographical sketch.
Cytochrome P450, family 1, subfamily A, polypeptide 1 is a protein[1] which in humans in encoded by the CYP1A1 gene.[2] The protein a member of the cytochrome P450 superfamily of enzymes.[3]
Function
CYP1A1 is involved in phase I xenobiotic and drug metabolism (one substrate of it is theophylline). It is inhibited by fluoroquinolones and macrolides and induced by aromatic hydrocarbons.[4]
CYP1A1 is also known as AHH (aryl hydrocarbon hydroxylase). It is involved in the metabolic activation of aromatic hydrocarbons (polycyclic aromatic hydrocarbons, PAH), for example, benzopyrene (BP), by transforming it to an epoxide. In this reaction, the oxidation of benzo[a]pyrene is catalysed by CYP1A1 to form BP-7,8-epoxide, which can be further oxidized by epoxide hydrolase (EH) to form BP-7,8-dihydrodiol. Finally CYP1A1 catalyses this intermediate to form BP-7,8-dihydrodiol-9,10-epoxide, which is the ultimate carcinogen.[4]
Regulation
The expression of the CYP1A1 and CYP1B1 genes are regulated by the aryl hydrocarbon receptor, a ligand activated transcription factor.[5]
Polymorphisms
Several polymorphisms have been identified in CYP1A1, some of which lead to more highly inducible AHH activity. CYP1A1 polymorphisms include:[6][7][8][9]
- M1, T→C substitution at nucleotide 3801 in the 3'-non-coding region
- M2, A→G substitution at nucleotide 2455 leading to an amino acid change of isoleucine to valine at codon 462
- M3, T→C substitution at nucleotide 3205 in the 3'-non-coding region
- M4, C→A substitution at nucleotide 2453 leading to an amino acid change of threonine to asparagine at codon 461
References
- ↑ Kawajiri K (1999). "CYP1A1". IARC scientific publications (148): 159–72. PMID 10493257.
- ↑ Nelson DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, Nebert DW (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. PMID 15128046. Unknown parameter
|month=ignored (help) - ↑ Smith G, Stubbins MJ, Harries LW, Wolf CR (1998). "Molecular genetics of the human cytochrome P450 monooxygenase superfamily". Xenobiotica; the fate of foreign compounds in biological systems. 28 (12): 1129–65. PMID 9890157. Unknown parameter
|month=ignored (help) - ↑ 4.0 4.1 Beresford AP (1993). "CYP1A1: friend or foe?". Drug metabolism reviews. 25 (4): 503–17. PMID 8313840.
- ↑ Ma Q, Lu AY (2007). "CYP1A induction and human risk assessment: an evolving tale of in vitro and in vivo studies". Drug metabolism and disposition: the biological fate of chemicals. 35 (7): 1009–16. doi:10.1124/dmd.107.015826. PMID 17431034. Unknown parameter
|month=ignored (help) - ↑ Petersen DD, McKinney CE, Ikeya K, Smith HH, Bale AE, McBride OW, Nebert DW (1991). "Human CYP1A1 gene: cosegregation of the enzyme inducibility phenotype and an RFLP". American journal of human genetics. 48 (4): 720–5. PMC 1682951. PMID 1707592. Unknown parameter
|month=ignored (help) - ↑ Cosma G, Crofts F, Taioli E, Toniolo P, Garte S (1993). "Relationship between genotype and function of the human CYP1A1 gene". Journal of toxicology and environmental health. 40 (2–3): 309–16. PMID 7901425.
- ↑ Crofts F, Taioli E, Trachman J, Cosma GN, Currie D, Toniolo P, Garte SJ (1994). "Functional significance of different human CYP1A1 genotypes". Carcinogenesis. 15 (12): 2961–3. PMID 8001264. Unknown parameter
|month=ignored (help) - ↑ Kiyohara C, Hirohata T, Inutsuka S (1996). "The relationship between aryl hydrocarbon hydroxylase and polymorphisms of the CYP1A1 gene". Japanese journal of cancer research : Gann. 87 (1): 18–24. PMID 8609043. Unknown parameter
|month=ignored (help)
Further reading
- Nelson DR, Zeldin DC, Hoffman SM; et al. (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. PMID 15128046.
- Masson LF, Sharp L, Cotton SC, Little J (2005). "Cytochrome P-450 1A1 gene polymorphisms and risk of breast cancer: a HuGE review". Am. J. Epidemiol. 161 (10): 901–15. doi:10.1093/aje/kwi121. PMID 15870154.
- Hildebrandt AG, Schwarz D, Krusekopf S; et al. (2007). "Recalling P446. P4501A1 (CYP1A1) opting for clinical application". Drug Metab. Rev. 39 (2–3): 323–41. doi:10.1080/03602530701498026. PMID 17786624.