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{{Infobox_gene}}
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'''Solute carrier family 22 member 3''' (SLC22A3) also known as the '''organic cation transporter 3''' (OCT3) or '''extraneuronal monoamine transporter''' (EMT) is a [[protein]] that in humans is encoded by the ''SLC22A3'' [[gene]].<ref name="pmid9632645">{{cite journal | vauthors = Kekuda R, Prasad PD, Wu X, Wang H, Fei YJ, Leibach FH, Ganapathy V | title = Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta | journal = J Biol Chem | volume = 273 | issue = 26 | pages = 15971–9 |date=Aug 1998 | pmid = 9632645 | pmc =  | doi =10.1074/jbc.273.26.15971  }}</ref><ref name="pmid9933568">{{cite journal | vauthors = Verhaagh S, Schweifer N, Barlow DP, Zwart R | title = Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27 | journal = Genomics | volume = 55 | issue = 2 | pages = 209–18 |date=Sep 1999 | pmid = 9933568 | pmc =  | doi = 10.1006/geno.1998.5639 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SLC22A3 solute carrier family 22 (extraneuronal monoamine transporter), member 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6581| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Solute carrier family 22 (extraneuronal monoamine transporter), member 3
| HGNCid = 10967
| Symbol = SLC22A3
| AltSymbols =; EMT; OCT3; EMTH
| OMIM = 604842
| ECnumber = 
| Homologene = 22630
| MGIid = 1333817
| GeneAtlas_image1 = PBB_GE_SLC22A3_205421_at_tn.png
| Function = {{GNF_GO|id=GO:0015075 |text = ion transmembrane transporter activity}} {{GNF_GO|id=GO:0015101 |text = organic cation transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
  | Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0015695 |text = organic cation transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6581
    | Hs_Ensembl = ENSG00000146477
    | Hs_RefseqProtein = NP_068812
    | Hs_RefseqmRNA = NM_021977
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 160689415
    | Hs_GenLoc_end = 160796004
    | Hs_Uniprot = O75751
    | Mm_EntrezGene = 20519
    | Mm_Ensembl = ENSMUSG00000023828
    | Mm_RefseqmRNA = XM_977528
    | Mm_RefseqProtein = XP_982622
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 12263330
    | Mm_GenLoc_end = 12351062
    | Mm_Uniprot = Q547K2
  }}
}}
'''Solute carrier family 22 (extraneuronal monoamine transporter), member 3''', also known as '''SLC22A3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC22A3 solute carrier family 22 (extraneuronal monoamine transporter), member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6581| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. This gene is one of three similar cation transporter genes located in a cluster on chromosome 6. The encoded protein contains twelve putative transmembrane domains and is a plasma integral membrane protein.<ref name="entrez">{{cite web | title = Entrez Gene: SLC22A3 solute carrier family 22 (extraneuronal monoamine transporter), member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6581| accessdate = }}</ref>
| summary_text = Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. This gene is one of three similar cation transporter genes located in a cluster on chromosome 6. The encoded protein contains twelve putative transmembrane domains and is a plasma integral membrane protein.<ref name="entrez"/>
}}
}}
==Distribution==
OCT3 is widely distributed in brain tissue. It is not yet completely clear whether its location is primarily neuronal or glial. Areas of the brain in which it has been reported include: hippocampus, retrosplenial cortex, visual cortex, hypothalamus, amygdala, nucleus accumbens, thalamus, raphe nucleus, subiculum, superior and inferior colliculi, and islands of Calleja.<ref name="pmid19025979">{{cite journal | vauthors = Gasser PJ, Orchinik M, Raju I, Lowry CA | title = Distribution of organic cation transporter 3, a corticosterone-sensitive monoamine transporter, in the rat brain. | journal = J Comp Neurol| volume = 512 | issue = 4 | pages = 529–555 |date=Feb 2009| pmid = 19025979 | pmc =  | doi =10.1002/cne.21921  }}</ref><ref name="pmid16581093">{{cite journal | vauthors = Amphoux A, Vialou V, Drescher E, Brüss M, Mannoury La Cour C, Rochat C, Millan MJ, Giros B, Bönisch H, Gautron S | title = Differential pharmacological in vitro properties of organic cation transporters and regional distribution in rat brain. | journal = Neuropharmacology| volume = 50 | issue = 8 | pages = 941–952 |date=Jun 2006| pmid = 16581093| pmc =  | doi =10.1016/j.neuropharm.2006.01.005  }}</ref>
==Pharmacology==
Organic cation transporter 3 is a polyspecific transporter whose transport is independent of sodium. Known substrates for transport include: [[histamine]], [[serotonin]], [[norepinephrine]], [[dopamine]] and [[MPP+]]. Capacity for transport and affinity for these substrates may vary between rat and human isoforms however.<ref name="pmid16581093"/>
Transport activity of OCT3 is inhibited by recreational and pharmaceutical drugs, including [[MDMA]], [[phencyclidine]] (PCP), [[MK-801]], [[amphetamine]], [[methamphetamine]] and [[cocaine]].<ref name="pmid16581093"/> Transport is also inhibited by the chemical [[decynium-22]] and physiological concentrations of [[corticosterone]] and [[cortisol]]. K<sub>i</sub> values for decynium-22 and corticosterone inhibition of OCT3 transport are respectively 10 and 100&nbsp;times lower than K<sub>i</sub> values of OCT1 and OCT2.<ref name="pmid12110607">{{cite journal | vauthors = Hayer-Zillgen M, Brüss M, Bönisch H | title = Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3 | journal = Br J Pharmacol| volume = 136| issue = 6| pages = 829–836 |date=Jul 2002| pmid = 12110607 | pmc =  1573414| doi =10.1038/sj.bjp.0704785  }}</ref>


==See also==
==See also==
Line 58: Line 22:


==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
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{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Kekuda R, Prasad PD, Wu X, ''et al.'' |title=Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta. |journal=J. Biol. Chem. |volume=273 |issue= 26 |pages= 15971-9 |year= 1998 |pmid= 9632645 |doi=  }}
*{{cite journal   |vauthors=Wu X, Kekuda R, Huang W, etal |title=Identity of the organic cation transporter OCT3 as the extraneuronal monoamine transporter (uptake2) and evidence for the expression of the transporter in the brain. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32776–86 |year= 1999 |pmid= 9830022 |doi=10.1074/jbc.273.49.32776 }}
*{{cite journal  | author=Wu X, Kekuda R, Huang W, ''et al.'' |title=Identity of the organic cation transporter OCT3 as the extraneuronal monoamine transporter (uptake2) and evidence for the expression of the transporter in the brain. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32776-86 |year= 1999 |pmid= 9830022 |doi= }}
*{{cite journal  | vauthors=Gründemann D, Schechinger B, Rappold GA, Schömig E |title=Molecular identification of the corticosterone-sensitive extraneuronal catecholamine transporter. |journal=Nat. Neurosci. |volume=1 |issue= 5 |pages= 349–51 |year= 1999 |pmid= 10196521 |doi= 10.1038/1557 }}
*{{cite journal  | author=Verhaagh S, Schweifer N, Barlow DP, Zwart R |title=Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27. |journal=Genomics |volume=55 |issue= 2 |pages= 209-18 |year= 1999 |pmid= 9933568 |doi= 10.1006/geno.1998.5639 }}
*{{cite journal  | vauthors=Gründemann D, Schömig E |title=Gene structures of the human non-neuronal monoamine transporters EMT and OCT2. |journal=Hum. Genet. |volume=106 |issue= 6 |pages= 627–35 |year= 2000 |pmid= 10942111 |doi=10.1007/s004390050035  }}
*{{cite journal | author=Gründemann D, Schechinger B, Rappold GA, Schömig E |title=Molecular identification of the corticosterone-sensitive extraneuronal catecholamine transporter. |journal=Nat. Neurosci. |volume=1 |issue= 5 |pages= 349-51 |year= 1999 |pmid= 10196521 |doi= 10.1038/1557 }}
*{{cite journal   |vauthors=Wu X, Huang W, Ganapathy ME, etal |title=Structure, function, and regional distribution of the organic cation transporter OCT3 in the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=279 |issue= 3 |pages= F449–58 |year= 2000 |pmid= 10966924 |doi= }}
*{{cite journal  | author=Gründemann D, Schömig E |title=Gene structures of the human non-neuronal monoamine transporters EMT and OCT2. |journal=Hum. Genet. |volume=106 |issue= 6 |pages= 627-35 |year= 2000 |pmid= 10942111 |doi=  }}
*{{cite journal  | vauthors=Wieland A, Hayer-Zillgen M, Bönisch H, Brüss M |title=Analysis of the gene structure of the human (SLC22A3) and murine (Slc22a3) extraneuronal monoamine transporter. |journal=Journal of Neural Transmission |volume=107 |issue= 10 |pages= 1149–57 |year= 2001 |pmid= 11129104 |doi=10.1007/s007020070028 }}
*{{cite journal | author=Wu X, Huang W, Ganapathy ME, ''et al.'' |title=Structure, function, and regional distribution of the organic cation transporter OCT3 in the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=279 |issue= 3 |pages= F449-58 |year= 2000 |pmid= 10966924 |doi=  }}
*{{cite journal   |vauthors=Wessler I, Roth E, Deutsch C, etal |title=Release of non-neuronal acetylcholine from the isolated human placenta is mediated by organic cation transporters. |journal=Br. J. Pharmacol. |volume=134 |issue= 5 |pages= 951–6 |year= 2001 |pmid= 11682442 |doi= 10.1038/sj.bjp.0704335 | pmc=1573028 }}
*{{cite journal | author=Wieland A, Hayer-Zillgen M, Bönisch H, Brüss M |title=Analysis of the gene structure of the human (SLC22A3) and murine (Slc22a3) extraneuronal monoamine transporter. |journal=Journal of neural transmission (Vienna, Austria : 1996) |volume=107 |issue= 10 |pages= 1149-57 |year= 2001 |pmid= 11129104 |doi=  }}
*{{cite journal   |vauthors=Martel F, Keating E, Calhau C, etal |title=Regulation of human extraneuronal monoamine transporter (hEMT) expressed in HEK293 cells by intracellular second messenger systems. |journal=Naunyn Schmiedebergs Arch. Pharmacol. |volume=364 |issue= 6 |pages= 487–95 |year= 2002 |pmid= 11770002 |doi=10.1007/s002100100476 }}
*{{cite journal  | author=Wessler I, Roth E, Deutsch C, ''et al.'' |title=Release of non-neuronal acetylcholine from the isolated human placenta is mediated by organic cation transporters. |journal=Br. J. Pharmacol. |volume=134 |issue= 5 |pages= 951-6 |year= 2001 |pmid= 11682442 |doi= 10.1038/sj.bjp.0704335 }}
*{{cite journal  | vauthors=Hayer-Zillgen M, Brüss M, Bönisch H |title=Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3. |journal=Br. J. Pharmacol. |volume=136 |issue= 6 |pages= 829–36 |year= 2003 |pmid= 12110607 |doi= 10.1038/sj.bjp.0704785  | pmc=1573414 }}
*{{cite journal  | author=Martel F, Keating E, Calhau C, ''et al.'' |title=Regulation of human extraneuronal monoamine transporter (hEMT) expressed in HEK293 cells by intracellular second messenger systems. |journal=Naunyn Schmiedebergs Arch. Pharmacol. |volume=364 |issue= 6 |pages= 487-95 |year= 2002 |pmid= 11770002 |doi= }}
*{{cite journal  | vauthors=Gründemann D, Hahne C, Berkels R, Schömig E |title=Agmatine is efficiently transported by non-neuronal monoamine transporters extraneuronal monoamine transporter (EMT) and organic cation transporter 2 (OCT2). |journal=J. Pharmacol. Exp. Ther. |volume=304 |issue= 2 |pages= 810–7 |year= 2003 |pmid= 12538837 |doi= 10.1124/jpet.102.044404 }}
*{{cite journal | author=Hayer-Zillgen M, Brüss M, Bönisch H |title=Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3. |journal=Br. J. Pharmacol. |volume=136 |issue= 6 |pages= 829-36 |year= 2003 |pmid= 12110607 |doi= 10.1038/sj.bjp.0704785 }}
*{{cite journal   |vauthors=Lazar A, Gründemann D, Berkels R, etal |title=Genetic variability of the extraneuronal monoamine transporter EMT (SLC22A3). |journal=J. Hum. Genet. |volume=48 |issue= 5 |pages= 226–30 |year= 2003 |pmid= 12768439 |doi= 10.1007/s10038-003-0015-5 }}
*{{cite journal | author=Gründemann D, Hahne C, Berkels R, Schömig E |title=Agmatine is efficiently transported by non-neuronal monoamine transporters extraneuronal monoamine transporter (EMT) and organic cation transporter 2 (OCT2). |journal=J. Pharmacol. Exp. Ther. |volume=304 |issue= 2 |pages= 810-7 |year= 2003 |pmid= 12538837 |doi= 10.1124/jpet.102.044404 }}
*{{cite journal   |vauthors=Haag C, Berkels R, Gründemann D, etal |title=The localisation of the extraneuronal monoamine transporter (EMT) in rat brain. |journal=J. Neurochem. |volume=88 |issue= 2 |pages= 291–7 |year= 2004 |pmid= 14690517 |doi=10.1111/j.1471-4159.2004.02180.x  }}
*{{cite journal | author=Lazar A, Gründemann D, Berkels R, ''et al.'' |title=Genetic variability of the extraneuronal monoamine transporter EMT (SLC22A3). |journal=J. Hum. Genet. |volume=48 |issue= 5 |pages= 226-30 |year= 2003 |pmid= 12768439 |doi= 10.1007/s10038-003-0015-5 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Haag C, Berkels R, Gründemann D, ''et al.'' |title=The localisation of the extraneuronal monoamine transporter (EMT) in rat brain. |journal=J. Neurochem. |volume=88 |issue= 2 |pages= 291-7 |year= 2004 |pmid= 14690517 |doi= }}
*{{cite journal   |vauthors=Bottalico B, Larsson I, Brodszki J, etal |title=Norepinephrine transporter (NET), serotonin transporter (SERT), vesicular monoamine transporter (VMAT2) and organic cation transporters (OCT1, 2 and EMT) in human placenta from pre-eclamptic and normotensive pregnancies. |journal=Placenta |volume=25 |issue= 6 |pages= 518–29 |year= 2004 |pmid= 15135235 |doi= 10.1016/j.placenta.2003.10.017 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Jiang W, Prokopenko O, Wong L, etal |title=IRIP, a new ischemia/reperfusion-inducible protein that participates in the regulation of transporter activity. |journal=Mol. Cell. Biol. |volume=25 |issue= 15 |pages= 6496–508 |year= 2005 |pmid= 16024787 |doi= 10.1128/MCB.25.15.6496-6508.2005 | pmc=1190334 }}
*{{cite journal  | author=Bottalico B, Larsson I, Brodszki J, ''et al.'' |title=Norepinephrine transporter (NET), serotonin transporter (SERT), vesicular monoamine transporter (VMAT2) and organic cation transporters (OCT1, 2 and EMT) in human placenta from pre-eclamptic and normotensive pregnancies. |journal=Placenta |volume=25 |issue= 6 |pages= 518-29 |year= 2004 |pmid= 15135235 |doi= 10.1016/j.placenta.2003.10.017 }}
*{{cite journal  | vauthors=Bourdet DL, Pritchard JB, Thakker DR |title=Differential substrate and inhibitory activities of ranitidine and famotidine toward human organic cation transporter 1 (hOCT1; SLC22A1), hOCT2 (SLC22A2), and hOCT3 (SLC22A3). |journal=J. Pharmacol. Exp. Ther. |volume=315 |issue= 3 |pages= 1288–97 |year= 2006 |pmid= 16141367 |doi= 10.1124/jpet.105.091223 }}
*{{cite journal  | author=Jiang W, Prokopenko O, Wong L, ''et al.'' |title=IRIP, a new ischemia/reperfusion-inducible protein that participates in the regulation of transporter activity. |journal=Mol. Cell. Biol. |volume=25 |issue= 15 |pages= 6496-508 |year= 2005 |pmid= 16024787 |doi= 10.1128/MCB.25.15.6496-6508.2005 }}
*{{cite journal   |vauthors=Aoyama N, Takahashi N, Kitaichi K, etal |title=Association between gene polymorphisms of SLC22A3 and methamphetamine use disorder. |journal=Alcohol. Clin. Exp. Res. |volume=30 |issue= 10 |pages= 1644–9 |year= 2006 |pmid= 17010131 |doi= 10.1111/j.1530-0277.2006.00215.x }}
*{{cite journal  | author=Bourdet DL, Pritchard JB, Thakker DR |title=Differential substrate and inhibitory activities of ranitidine and famotidine toward human organic cation transporter 1 (hOCT1; SLC22A1), hOCT2 (SLC22A2), and hOCT3 (SLC22A3). |journal=J. Pharmacol. Exp. Ther. |volume=315 |issue= 3 |pages= 1288-97 |year= 2006 |pmid= 16141367 |doi= 10.1124/jpet.105.091223 }}
*{{cite journal   |vauthors=Bottalico B, Noskova V, Pilka R, etal |title=The organic cation transporters (OCT1, OCT2, EMT) and the plasma membrane monoamine transporter (PMAT) show differential distribution and cyclic expression pattern in human endometrium and early pregnancy decidua. |journal=Mol. Reprod. Dev. |volume=74 |issue= 10 |pages= 1303–11 |year= 2007 |pmid= 17393420 |doi= 10.1002/mrd.20697 }}
*{{cite journal | author=Aoyama N, Takahashi N, Kitaichi K, ''et al.'' |title=Association between gene polymorphisms of SLC22A3 and methamphetamine use disorder. |journal=Alcohol. Clin. Exp. Res. |volume=30 |issue= 10 |pages= 1644-9 |year= 2006 |pmid= 17010131 |doi= 10.1111/j.1530-0277.2006.00215.x }}
*{{cite journal | author=Bottalico B, Noskova V, Pilka R, ''et al.'' |title=The organic cation transporters (OCT1, OCT2, EMT) and the plasma membrane monoamine transporter (PMAT) show differential distribution and cyclic expression pattern in human endometrium and early pregnancy decidua. |journal=Mol. Reprod. Dev. |volume=74 |issue= 10 |pages= 1303-11 |year= 2007 |pmid= 17393420 |doi= 10.1002/mrd.20697 }}
}}
}}
{{refend}}
{{refend}}


{{membrane-protein-stub}}
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{{NLM content}}
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[[Category:Solute carrier family]]
[[Category:Solute carrier family]]
{{WikiDoc Sources}}
[[Category:Amphetamine]]

Latest revision as of 16:53, 6 December 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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Wikidata
View/Edit Human

Solute carrier family 22 member 3 (SLC22A3) also known as the organic cation transporter 3 (OCT3) or extraneuronal monoamine transporter (EMT) is a protein that in humans is encoded by the SLC22A3 gene.[1][2][3]

Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. This gene is one of three similar cation transporter genes located in a cluster on chromosome 6. The encoded protein contains twelve putative transmembrane domains and is a plasma integral membrane protein.[3]

Distribution

OCT3 is widely distributed in brain tissue. It is not yet completely clear whether its location is primarily neuronal or glial. Areas of the brain in which it has been reported include: hippocampus, retrosplenial cortex, visual cortex, hypothalamus, amygdala, nucleus accumbens, thalamus, raphe nucleus, subiculum, superior and inferior colliculi, and islands of Calleja.[4][5]

Pharmacology

Organic cation transporter 3 is a polyspecific transporter whose transport is independent of sodium. Known substrates for transport include: histamine, serotonin, norepinephrine, dopamine and MPP+. Capacity for transport and affinity for these substrates may vary between rat and human isoforms however.[5]

Transport activity of OCT3 is inhibited by recreational and pharmaceutical drugs, including MDMA, phencyclidine (PCP), MK-801, amphetamine, methamphetamine and cocaine.[5] Transport is also inhibited by the chemical decynium-22 and physiological concentrations of corticosterone and cortisol. Ki values for decynium-22 and corticosterone inhibition of OCT3 transport are respectively 10 and 100 times lower than Ki values of OCT1 and OCT2.[6]

See also

References

  1. ↑ Kekuda R, Prasad PD, Wu X, Wang H, Fei YJ, Leibach FH, Ganapathy V (Aug 1998). "Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta". J Biol Chem. 273 (26): 15971–9. doi:10.1074/jbc.273.26.15971. PMID 9632645.
  2. ↑ Verhaagh S, Schweifer N, Barlow DP, Zwart R (Sep 1999). "Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27". Genomics. 55 (2): 209–18. doi:10.1006/geno.1998.5639. PMID 9933568.
  3. ↑ 3.0 3.1 "Entrez Gene: SLC22A3 solute carrier family 22 (extraneuronal monoamine transporter), member 3".
  4. ↑ Gasser PJ, Orchinik M, Raju I, Lowry CA (Feb 2009). "Distribution of organic cation transporter 3, a corticosterone-sensitive monoamine transporter, in the rat brain". J Comp Neurol. 512 (4): 529–555. doi:10.1002/cne.21921. PMID 19025979.
  5. ↑ 5.0 5.1 5.2 Amphoux A, Vialou V, Drescher E, Brüss M, Mannoury La Cour C, Rochat C, Millan MJ, Giros B, Bönisch H, Gautron S (Jun 2006). "Differential pharmacological in vitro properties of organic cation transporters and regional distribution in rat brain". Neuropharmacology. 50 (8): 941–952. doi:10.1016/j.neuropharm.2006.01.005. PMID 16581093.
  6. ↑ Hayer-Zillgen M, Brüss M, Bönisch H (Jul 2002). "Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3". Br J Pharmacol. 136 (6): 829–836. doi:10.1038/sj.bjp.0704785. PMC 1573414. PMID 12110607.

Further reading


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

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