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Article: Comparison between copper and cisplatin transport mediated by human copper transporter 1 (hCTR1)

TitleComparison between copper and cisplatin transport mediated by human copper transporter 1 (hCTR1)
Authors
Issue Date2012
PublisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/Publishing/Journals/MT/About.asp
Citation
Metallomics, 2012, v. 4 n. 7, p. 679-685 How to Cite?
AbstractCopper transporter 1 (CTR1) is a transmembrane protein that imports copper(i) into yeast and mammalian cells. Surprisingly, the protein also mediates the uptake of platinum anticancer drugs, e.g. cisplatin and carboplatin. To study the effects of several metal-binding residues/motifs of hCTR1 on the transport of both Cu + and cisplatin, we have constructed Hela cells that stably express a series of hCTR1 variant proteins including H22-24A, NHA, C189S, hCTR1ΔC, H139R and Y156A, and compared their abilities to regulate the accumulation and cytotoxicity of these metal compounds. Our results demonstrated that the cells expressing the hCTR1 mutants of histidine-rich motifs in the N-terminus (H22-24A, NHA) resulted in a higher basal copper level in the steady state compared to those expressing wild-type protein. However, the cellular accumulation of both copper and cisplatin in these variants was found at a similar level to that of wild type when incubated with an excess of metal compounds (100 μM). The cells expressing hCTR1 variants of H139R and Y156A exhibit lower capacities towards accumulation of copper but not cisplatin. Significantly, cells with the C189S variant partially retained the ability of the wild-type hCTR1 protein to accumulate both copper and cisplatin, while for cells expressing the C-terminus truncated variant of hCTR1 (hCTR1ΔC) this ability was absolutely abolished, suggesting that this motif is crucial for the function of the transporter. This journal is © 2012 The Royal Society of Chemistry.
Persistent Identifierhttp://hdl.handle.net/10722/159379
ISSN
2015 Impact Factor: 3.54
2015 SCImago Journal Rankings: 1.120
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDu, Xen_HK
dc.contributor.authorWang, Xen_HK
dc.contributor.authorLi, Hen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2012-08-16T05:48:57Z-
dc.date.available2012-08-16T05:48:57Z-
dc.date.issued2012en_HK
dc.identifier.citationMetallomics, 2012, v. 4 n. 7, p. 679-685en_HK
dc.identifier.issn1756-5901en_HK
dc.identifier.urihttp://hdl.handle.net/10722/159379-
dc.description.abstractCopper transporter 1 (CTR1) is a transmembrane protein that imports copper(i) into yeast and mammalian cells. Surprisingly, the protein also mediates the uptake of platinum anticancer drugs, e.g. cisplatin and carboplatin. To study the effects of several metal-binding residues/motifs of hCTR1 on the transport of both Cu + and cisplatin, we have constructed Hela cells that stably express a series of hCTR1 variant proteins including H22-24A, NHA, C189S, hCTR1ΔC, H139R and Y156A, and compared their abilities to regulate the accumulation and cytotoxicity of these metal compounds. Our results demonstrated that the cells expressing the hCTR1 mutants of histidine-rich motifs in the N-terminus (H22-24A, NHA) resulted in a higher basal copper level in the steady state compared to those expressing wild-type protein. However, the cellular accumulation of both copper and cisplatin in these variants was found at a similar level to that of wild type when incubated with an excess of metal compounds (100 μM). The cells expressing hCTR1 variants of H139R and Y156A exhibit lower capacities towards accumulation of copper but not cisplatin. Significantly, cells with the C189S variant partially retained the ability of the wild-type hCTR1 protein to accumulate both copper and cisplatin, while for cells expressing the C-terminus truncated variant of hCTR1 (hCTR1ΔC) this ability was absolutely abolished, suggesting that this motif is crucial for the function of the transporter. This journal is © 2012 The Royal Society of Chemistry.en_HK
dc.languageengen_US
dc.publisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/Publishing/Journals/MT/About.aspen_HK
dc.relation.ispartofMetallomicsen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleComparison between copper and cisplatin transport mediated by human copper transporter 1 (hCTR1)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1756-5901&volume=4&spage=679 &epage=685&date=2012&atitle=Comparison+between+copper+and+cisplatin+transport+mediated+by+human+copper+transporter+1+(hCtr1)en_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/c2mt20021jen_HK
dc.identifier.pmid22552365-
dc.identifier.scopuseid_2-s2.0-84863683148en_HK
dc.identifier.hkuros205082en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84863683148&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume4en_HK
dc.identifier.issue7en_HK
dc.identifier.spage679en_HK
dc.identifier.epage685en_HK
dc.identifier.isiWOS:000305884200013-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridDu, X=37062963400en_HK
dc.identifier.scopusauthoridWang, X=35333341400en_HK
dc.identifier.scopusauthoridLi, H=37063577200en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK

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