BCRP

関

ATP-binding cassette transport- ers, ABCG2

同

breast cancer-resistant protein

WordNet

1. before the Christian era; used following dates before the supposed year Christ was born; "in 200 BC" (同)B.C., before Christ

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/08/05 20:52:59」(JST)

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ABCG2
Identifiers
Aliases	ABCG2, ATP-binding cassette, sub-family G (WHITE), member 2 (Junior blood group), ABC15, ABCP, BCRP, BCRP1, BMDP, CD338, CDw338, EST157481, GOUT1, MRX, MXR, MXR1, UAQTL1, MXR-1, ATP binding cassette subfamily G member 2 (Junior blood group)
External IDs	MGI: 1347061 HomoloGene: 55852 GeneCards: ABCG2
Gene ontology Molecular function • nucleotide binding • xenobiotic-transporting ATPase activity • heme transporter activity • protein homodimerization activity • transporter activity • ATPase activity • protein binding • ATP binding • ATPase activity, coupled to transmembrane movement of substances • cholesterol transporter activity Cellular component • mitochondrial membrane • membrane • mitochondrion • nucleus • plasma membrane • integral component of membrane • apical plasma membrane • receptor complex Biological process • urate metabolic process • response to drug • cellular iron ion homeostasis • heme transport • drug transmembrane transport • xenobiotic transport • transmembrane transport • cholesterol efflux • transport Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9429	26357
Ensembl	ENSG00000118777	ENSMUSG00000029802
UniProt	Q9UNQ0	Q7TMS5
RefSeq (mRNA)	NM_001257386 NM_004827 NM_001348985 NM_001348986 NM_001348987 NM_001348988 NM_001348989	NM_011920
RefSeq (protein)	NP_001244315 NP_004818 NP_001335914 NP_001335915 NP_001335916 NP_001335917 NP_001335918	NP_036050
Location (UCSC)	Chr 4: 88.09 – 88.23 Mb	Chr 6: 58.58 – 58.7 Mb
PubMed search
Wikidata
View/Edit Human View/Edit Mouse

ATP-binding cassette sub-family G member 2 is a protein that in humans is encoded by the ABCG2 gene. ABCG2 has also been designated as CDw338 (cluster of differentiation w338).

Function

The membrane-associated protein encoded by this gene is included in the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. Alternatively referred to as the Breast Cancer Resistance Protein, this protein functions as a xenobiotic transporter which may play a role in multi-drug resistance to chemotherapeutic agents including mitoxantrone and camptothecin analogues. Early observations of significant ABCG2-mediated resistance to anthracyclines were subsequently attributed mutations encountered in vitro but not in nature or the clinic. Significant expression of this protein has been observed in the placenta, and it has been shown to have a role in protecting the fetus from xenobiotics in the maternal circulation.

The transporter has also been shown to play protective roles in blocking absorption at the apical membrane of the intestine, and at the blood-testis barrier, the blood–brain barrier, and the membranes of hematopoietic progenitor and other stem cells. At the apical membranes of the liver and kidney, it enhances excretion of xenobiotics. In the lactating mammary gland, it has a role on excreting vitamins such as riboflavin and biotin into milk.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [[File: [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] |{{{bSize}}}px|alt=Fluorouracil (5-FU) Activity edit]] File:FluoropyrimidineActivity_WP1601.png Fluorouracil (5-FU) Activity edit

Click on genes, proteins and metabolites below to link to respective articles. [[File: [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] [[ ]] |{{{bSize}}}px|alt=Irinotecan Pathway edit]] File:IrinotecanPathway_WP229.png Irinotecan Pathway edit

See also

• ATP-binding cassette transporter

Further reading

• Hazai E, Bikadi Z (2008). "Homology modeling of breast cancer resistance protein (ABCG2).". J Struct Biol. 162 (1): 63–74. PMID 18249138. doi:10.1016/j.jsb.2007.12.001. 
• Abbott BL (2006). "ABCG2 (BCRP): a cytoprotectant in normal and malignant stem cells". Clin Adv Hematol Oncol. 4 (1): 63–72. PMID 16562373. 
• Schmitz G, Langmann T, Heimerl S (2002). "Role of ABCG1 and other ABCG family members in lipid metabolism.". J. Lipid Res. 42 (10): 1513–20. PMID 11590207. 
• Ejendal KF, Hrycyna CA (2003). "Multidrug resistance and cancer: the role of the human ABC transporter ABCG2.". Curr. Protein Pept. Sci. 3 (5): 503–11. PMID 12369998. doi:10.2174/1389203023380521. 
• Doyle LA, Ross DD (2003). "Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2).". Oncogene. 22 (47): 7340–58. PMID 14576842. doi:10.1038/sj.onc.1206938. 
• Sugimoto Y, Tsukahara S, Ishikawa E, Mitsuhashi J (2005). "Breast cancer resistance protein: molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics.". Cancer Sci. 96 (8): 457–65. PMID 16108826. doi:10.1111/j.1349-7006.2005.00081.x. 
• Ishikawa T, Tamura A, Saito H, et al. (2006). "Pharmacogenomics of the human ABC transporter ABCG2: from functional evaluation to drug molecular design.". Naturwissenschaften. 92 (10): 451–63. PMID 16160819. doi:10.1007/s00114-005-0019-4. 
• Krishnamurthy P, Schuetz JD (2006). "Role of ABCG2/BCRP in biology and medicine.". Annu. Rev. Pharmacol. Toxicol. 46: 381–410. PMID 16402910. doi:10.1146/annurev.pharmtox.46.120604.141238. 
• Robey RW, Polgar O, Deeken J, et al. (2007). "ABCG2: determining its relevance in clinical drug resistance.". Cancer Metastasis Rev. 26 (1): 39–57. PMID 17323127. doi:10.1007/s10555-007-9042-6. 

External links

• ABCG2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
• Human ABCG2 genome location and ABCG2 gene details page in the UCSC Genome Browser.

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

UpToDate Contents

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English Journal

• Expression of breast cancer resistance protein in peripheral T cell subsets from HIV‑1‑infected patients with antiretroviral therapy.

• Zhang JC1, Deng ZY2, Wang Y1, Xie F3, Sun L4, Zhang FX1.
• Molecular medicine reports.Mol Med Rep.2014 Aug;10(2):939-46. doi: 10.3892/mmr.2014.2282. Epub 2014 May 29.
• The aim of the present study was to investigate the expression of breast cancer resistance protein (BCRP) in peripheral T cell subsets of human immunodeficiency virus 1 (HIV‑1)‑infected patients, and to analyze the association between the levels of BCRP expression and disease progression in HIV
• PMID 24890893

• Hepatocellular Exposure of Troglitazone Metabolites in Rat Sandwich-Cultured Hepatocytes Lacking Bcrp and Mrp2: Interplay between Formation and Excretion.

• Yang K1, Brouwer KL2.
• Drug metabolism and disposition: the biological fate of chemicals.Drug Metab Dispos.2014 Jul;42(7):1219-26. doi: 10.1124/dmd.114.057190. Epub 2014 May 5.
• Inhibition of bile acid transport by troglitazone (TGZ) and its major metabolite, TGZ sulfate (TS), may lead to hepatocellular accumulation of toxic bile acids; TS accumulation and hepatotoxicity may be associated with impaired TS biliary excretion. This study evaluated the impact of impaired transp
• PMID 24799397

• Expression of the ABC transport proteins MDR1 (ABCB1) and BCRP (ABCG2) in bovine rumen.

• Haslam IS1, Simmons NL.
• Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology.J Comp Physiol B.2014 Jul;184(5):673-81. doi: 10.1007/s00360-014-0804-5. Epub 2014 Apr 20.
• Rumen fermentation of plant-based forage in bovines is the major site for generation and absorption of short-chain fatty acids. Consequentially, the rumen is also the site for initial exposure to toxins released from diet. Accordingly, we have investigated the expression of bovine ABC transporters i
• PMID 24747985

Japanese Journal

• Impact of P-glycoprotein and breast cancer resistance protein on the brain distribution of antiepileptic drugs in knockout mouse models.

• Nakanishi Haruka,Yonezawa Atsushi,Matsubara Kazuo,Yano Ikuko
• European journal of pharmacology 710(1-3), 20-28, 2013-06-15
• … Refractory epilepsy is reportedly associated with an overexpression of ATP-binding cassette transporters such as P-glycoprotein (Pgp) and breast cancer resistance protein (Bcrp). … In this study, we examined the contribution of Pgp and Bcrp to the brain distribution of 12 antiepileptic drugs (AEDs) in Mdr1a/1b(-/-) and Mdr1a/1b(-/-)/Bcrp(-/-) mice within a therapeutic concentration range. …
• NAID 120005289852

• 急性白血病の薬剤耐性とABCトランスポーター

• 泉二 登志子,王 艶華,MOTOJI Toshiko,WANG Yan-Hua
• 東京女子医科大学雑誌 83(E2), E451-E457, 2013-03-31
• … その代表的な機序であるABCトランスポーターは、multidrug resistance 1(MDR1)と産物であるP-glycprotein(P-gp)、ABCG2遺伝子とその産物であるbreast cancer related protein(BCRP)、ABCC1遺伝子の産物であるmultidrug resistance-related protein(MRP1)などがある。 …
• NAID 110009575051

• Active intestinal absorption of fluoroquinolone antibacterial agent ciprofloxacin by organic anion transporting polypeptide, Oatp1a5

• Arakawa Hiroshi,Shirasaka Yoshiyuki,Haga Makoto,Nakanishi Takeo,Tamai Ikumi
• Biopharmaceutics and Drug Disposition 33(6), 332-341, 2012-09
• … In conclusion, the intestinal absorption of ciprofloxacin could be affected by influx transporters such as Oatp1a5 as well as the efflux transporters such as P-gp and Bcrp. …
• NAID 120004997009

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