Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins
Multidrug resistance-associated protein (MRP) and canalicular multispecific organic anion transporter (cMOAT) are transporter proteins that pump organic anions across cellular membranes and have been linked to resistance to cytotoxic drugs. We previously identified MOAT-B, an MRP/cMOAT-related trans...
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| Veröffentlicht in: | JNCI : Journal of the National Cancer Institute 1998-11, Vol.90 (22), p.1735-1741 |
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| creator | BELINSKY, M. G BAIN, L. J BALSARA, B. B TESTA, J. R KRUH, G. D |
| description | Multidrug resistance-associated protein (MRP) and canalicular multispecific organic anion transporter (cMOAT) are transporter proteins that pump organic anions across cellular membranes and have been linked to resistance to cytotoxic drugs. We previously identified MOAT-B, an MRP/cMOAT-related transporter, by use of a polymerase chain reaction approach. However, analysis of expressed sequence tag (EST) databases indicated that there might be additional MRP/cMOAT-related transporters. To further define the MRP/cMOAT subfamily of transporters, we used EST probes to isolate complementary DNAs for two related transporter proteins, MOAT-C and MOAT-D.
MOAT-C and MOAT-D expression patterns in human tissues were determined by RNA blot analysis, and chromosomal localization of the genes was determined by fluorescence in situ hybridization.
MOAT-C is predicted to encode a 1437-amino-acid protein that, among eukaryotic transporters, is most closely related to MRP, cMOAT, and MOAT-B (about 36% identity). However, MOAT-C is less related to MRP and cMOAT than MRP and cMOAT are to each other (about 48% identity). Like MOAT-B, MOAT-C lacks an N-terminal membrane-spanning domain, indicating that the topology of this protein is similarly distinct from that of MRP and cMOAT. MOAT-D is predicted to encode a 1527-amino-acid protein that is the closest known relative of MRP (about 58% identity). MOAT-D is also highly related to cMOAT (about 47% identity). The presence of an N-terminal membrane-spanning domain indicates that the topology of MOAT-D is quite similar to that of MRP and cMOAT. MOAT-C transcripts are widely expressed in human tissues; however, MOAT-D transcript expression is more restricted. The MOAT-C and MOAT-D genes are located at chromosomes 3q27 and 17q21.3, respectively.
On the basis of amino acid identity and protein topology, the MRP/cMOAT transporter subfamily falls into two groups; the first group consists of MRP, cMOAT, and MOAT-D, and the second group consists of MOAT-B and MOAT-C. |
| doi_str_mv | 10.1093/jnci/90.22.1735 |
| format | Article |
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MOAT-C and MOAT-D expression patterns in human tissues were determined by RNA blot analysis, and chromosomal localization of the genes was determined by fluorescence in situ hybridization.
MOAT-C is predicted to encode a 1437-amino-acid protein that, among eukaryotic transporters, is most closely related to MRP, cMOAT, and MOAT-B (about 36% identity). However, MOAT-C is less related to MRP and cMOAT than MRP and cMOAT are to each other (about 48% identity). Like MOAT-B, MOAT-C lacks an N-terminal membrane-spanning domain, indicating that the topology of this protein is similarly distinct from that of MRP and cMOAT. MOAT-D is predicted to encode a 1527-amino-acid protein that is the closest known relative of MRP (about 58% identity). MOAT-D is also highly related to cMOAT (about 47% identity). The presence of an N-terminal membrane-spanning domain indicates that the topology of MOAT-D is quite similar to that of MRP and cMOAT. MOAT-C transcripts are widely expressed in human tissues; however, MOAT-D transcript expression is more restricted. The MOAT-C and MOAT-D genes are located at chromosomes 3q27 and 17q21.3, respectively.
On the basis of amino acid identity and protein topology, the MRP/cMOAT transporter subfamily falls into two groups; the first group consists of MRP, cMOAT, and MOAT-D, and the second group consists of MOAT-B and MOAT-C.</description><identifier>ISSN: 0027-8874</identifier><identifier>EISSN: 1460-2105</identifier><identifier>DOI: 10.1093/jnci/90.22.1735</identifier><identifier>PMID: 9827529</identifier><identifier>CODEN: JNCIEQ</identifier><language>eng</language><publisher>Cary, NC: Oxford University Press</publisher><subject>Amino Acid Sequence ; Anion Transport Proteins ; Antineoplastic agents ; ATP-Binding Cassette Transporters - chemistry ; ATP-Binding Cassette Transporters - genetics ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Chromosomes, Human, Pair 17 - genetics ; Chromosomes, Human, Pair 3 - genetics ; Deoxyribonucleic acid ; DNA ; DNA, Neoplasm - analysis ; DNA, Neoplasm - isolation & purification ; Drug resistance ; Female ; Gene Expression Regulation, Neoplastic ; General aspects ; Humans ; Leukemia - genetics ; Medical sciences ; Molecular Sequence Data ; Multidrug Resistance-Associated Proteins ; Neoplasm Proteins - chemistry ; Neoplasm Proteins - genetics ; Ovarian Neoplasms - genetics ; Pharmacology. Drug treatments ; Proteins ; Sequence Analysis, DNA</subject><ispartof>JNCI : Journal of the National Cancer Institute, 1998-11, Vol.90 (22), p.1735-1741</ispartof><rights>1999 INIST-CNRS</rights><rights>Copyright Superintendent of Documents Nov 18, 1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-448c48393613853b5a90618da5bf14162c6eb109cb2c88b8a9d36c88939c43b73</citedby><cites>FETCH-LOGICAL-c455t-448c48393613853b5a90618da5bf14162c6eb109cb2c88b8a9d36c88939c43b73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1598004$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9827529$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BELINSKY, M. G</creatorcontrib><creatorcontrib>BAIN, L. J</creatorcontrib><creatorcontrib>BALSARA, B. B</creatorcontrib><creatorcontrib>TESTA, J. R</creatorcontrib><creatorcontrib>KRUH, G. D</creatorcontrib><title>Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins</title><title>JNCI : Journal of the National Cancer Institute</title><addtitle>J Natl Cancer Inst</addtitle><description>Multidrug resistance-associated protein (MRP) and canalicular multispecific organic anion transporter (cMOAT) are transporter proteins that pump organic anions across cellular membranes and have been linked to resistance to cytotoxic drugs. We previously identified MOAT-B, an MRP/cMOAT-related transporter, by use of a polymerase chain reaction approach. However, analysis of expressed sequence tag (EST) databases indicated that there might be additional MRP/cMOAT-related transporters. To further define the MRP/cMOAT subfamily of transporters, we used EST probes to isolate complementary DNAs for two related transporter proteins, MOAT-C and MOAT-D.
MOAT-C and MOAT-D expression patterns in human tissues were determined by RNA blot analysis, and chromosomal localization of the genes was determined by fluorescence in situ hybridization.
MOAT-C is predicted to encode a 1437-amino-acid protein that, among eukaryotic transporters, is most closely related to MRP, cMOAT, and MOAT-B (about 36% identity). However, MOAT-C is less related to MRP and cMOAT than MRP and cMOAT are to each other (about 48% identity). Like MOAT-B, MOAT-C lacks an N-terminal membrane-spanning domain, indicating that the topology of this protein is similarly distinct from that of MRP and cMOAT. MOAT-D is predicted to encode a 1527-amino-acid protein that is the closest known relative of MRP (about 58% identity). MOAT-D is also highly related to cMOAT (about 47% identity). The presence of an N-terminal membrane-spanning domain indicates that the topology of MOAT-D is quite similar to that of MRP and cMOAT. MOAT-C transcripts are widely expressed in human tissues; however, MOAT-D transcript expression is more restricted. The MOAT-C and MOAT-D genes are located at chromosomes 3q27 and 17q21.3, respectively.
On the basis of amino acid identity and protein topology, the MRP/cMOAT transporter subfamily falls into two groups; the first group consists of MRP, cMOAT, and MOAT-D, and the second group consists of MOAT-B and MOAT-C.</description><subject>Amino Acid Sequence</subject><subject>Anion Transport Proteins</subject><subject>Antineoplastic agents</subject><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>ATP-Binding Cassette Transporters - genetics</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Chromosomes, Human, Pair 17 - genetics</subject><subject>Chromosomes, Human, Pair 3 - genetics</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA, Neoplasm - analysis</subject><subject>DNA, Neoplasm - isolation & purification</subject><subject>Drug resistance</subject><subject>Female</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>General aspects</subject><subject>Humans</subject><subject>Leukemia - genetics</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Multidrug Resistance-Associated Proteins</subject><subject>Neoplasm Proteins - chemistry</subject><subject>Neoplasm Proteins - genetics</subject><subject>Ovarian Neoplasms - genetics</subject><subject>Pharmacology. Drug treatments</subject><subject>Proteins</subject><subject>Sequence Analysis, DNA</subject><issn>0027-8874</issn><issn>1460-2105</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkMtLAzEQxoMoWh9nT8Ii4sltJ6_d5FjqE1oU0XNI0ixu2UdNdhH9683aouBcZuD75pvkh9AphjEGSSerxpYTCWNCxjinfAeNMMsgJRj4LhoBkDwVImcH6DCEFcSShO2jfSlIzokcITd7017bzvnyS3dl2yRtkSwepy_pLNHNcjNeXyWN-0hqVxvnw-Do3lyyeH6a2EFPQm8KXZfV54_kdRPWrY-Rydq3nSubcIz2Cl0Fd7LtR-j19uZldp_OH-8eZtN5ahnnXcqYsExQSTNMBaeGawkZFkvNTYEZzojNnInftoZYIYzQckmzOEkqLaMmp0focpMbD7_3LnSqLoN1VaUb1_ZB5QA5lQDReP7PuGp738S3KRLZ4ZxLEU2Tjcn6NgTvCrX2Za39p8KgBvpqoK8kxB010I8bZ9vY3tRu-evf4o76xVbXweqqiKhsGf5i41UARr8Bfe2KgQ</recordid><startdate>19981118</startdate><enddate>19981118</enddate><creator>BELINSKY, M. G</creator><creator>BAIN, L. J</creator><creator>BALSARA, B. B</creator><creator>TESTA, J. R</creator><creator>KRUH, G. D</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>7X8</scope></search><sort><creationdate>19981118</creationdate><title>Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins</title><author>BELINSKY, M. G ; BAIN, L. J ; BALSARA, B. B ; TESTA, J. R ; KRUH, G. 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Drug treatments</topic><topic>Proteins</topic><topic>Sequence Analysis, DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BELINSKY, M. G</creatorcontrib><creatorcontrib>BAIN, L. J</creatorcontrib><creatorcontrib>BALSARA, B. B</creatorcontrib><creatorcontrib>TESTA, J. R</creatorcontrib><creatorcontrib>KRUH, G. 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B</au><au>TESTA, J. R</au><au>KRUH, G. D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins</atitle><jtitle>JNCI : Journal of the National Cancer Institute</jtitle><addtitle>J Natl Cancer Inst</addtitle><date>1998-11-18</date><risdate>1998</risdate><volume>90</volume><issue>22</issue><spage>1735</spage><epage>1741</epage><pages>1735-1741</pages><issn>0027-8874</issn><eissn>1460-2105</eissn><coden>JNCIEQ</coden><abstract>Multidrug resistance-associated protein (MRP) and canalicular multispecific organic anion transporter (cMOAT) are transporter proteins that pump organic anions across cellular membranes and have been linked to resistance to cytotoxic drugs. We previously identified MOAT-B, an MRP/cMOAT-related transporter, by use of a polymerase chain reaction approach. However, analysis of expressed sequence tag (EST) databases indicated that there might be additional MRP/cMOAT-related transporters. To further define the MRP/cMOAT subfamily of transporters, we used EST probes to isolate complementary DNAs for two related transporter proteins, MOAT-C and MOAT-D.
MOAT-C and MOAT-D expression patterns in human tissues were determined by RNA blot analysis, and chromosomal localization of the genes was determined by fluorescence in situ hybridization.
MOAT-C is predicted to encode a 1437-amino-acid protein that, among eukaryotic transporters, is most closely related to MRP, cMOAT, and MOAT-B (about 36% identity). However, MOAT-C is less related to MRP and cMOAT than MRP and cMOAT are to each other (about 48% identity). Like MOAT-B, MOAT-C lacks an N-terminal membrane-spanning domain, indicating that the topology of this protein is similarly distinct from that of MRP and cMOAT. MOAT-D is predicted to encode a 1527-amino-acid protein that is the closest known relative of MRP (about 58% identity). MOAT-D is also highly related to cMOAT (about 47% identity). The presence of an N-terminal membrane-spanning domain indicates that the topology of MOAT-D is quite similar to that of MRP and cMOAT. MOAT-C transcripts are widely expressed in human tissues; however, MOAT-D transcript expression is more restricted. The MOAT-C and MOAT-D genes are located at chromosomes 3q27 and 17q21.3, respectively.
On the basis of amino acid identity and protein topology, the MRP/cMOAT transporter subfamily falls into two groups; the first group consists of MRP, cMOAT, and MOAT-D, and the second group consists of MOAT-B and MOAT-C.</abstract><cop>Cary, NC</cop><pub>Oxford University Press</pub><pmid>9827529</pmid><doi>10.1093/jnci/90.22.1735</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Anion Transport Proteins Antineoplastic agents ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - genetics Chromosomes, Human, Pair 17 - genetics Chromosomes, Human, Pair 3 - genetics Deoxyribonucleic acid DNA DNA, Neoplasm - analysis DNA, Neoplasm - isolation & purification Drug resistance Female Gene Expression Regulation, Neoplastic General aspects Humans Leukemia - genetics Medical sciences Molecular Sequence Data Multidrug Resistance-Associated Proteins Neoplasm Proteins - chemistry Neoplasm Proteins - genetics Ovarian Neoplasms - genetics Pharmacology. Drug treatments Proteins Sequence Analysis, DNA |
| title | Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins |
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