Molecular Identification and Characterization of Novel Human and Mouse Concentrative Na+-Nucleoside Cotransporter Proteins (hCNT3 and mCNT3) Broadly Selective for Purine and Pyrimidine Nucleosides (System cib)
The human concentrative (Na+-linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (systemcit) and purine nucleosides (system cif), respectively. Both have homologs in other mammalian species and belong to a gene family (CNT) that also includes hfCNT, a...
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Published in | The Journal of biological chemistry Vol. 276; no. 4; pp. 2914 - 2927 |
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Main Authors | , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
26.01.2001
American Society for Biochemistry and Molecular Biology |
Subjects | |
Online Access | Get full text |
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Abstract | The human concentrative (Na+-linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (systemcit) and purine nucleosides (system cif), respectively. Both have homologs in other mammalian species and belong to a gene family (CNT) that also includes hfCNT, a newly identified broad specificity pyrimidine and purine Na+-nucleoside symporter (system cib) from the ancient marine vertebrate, the Pacific hagfish (Eptatretus stouti). We now report the cDNA cloning and characterization of cib homologs of hfCNT from human mammary gland, differentiated human myeloid HL-60 cells, and mouse liver. The 691- and 703-residue human and mouse proteins, designated hCNT3 and mCNT3, respectively, were 79% identical in amino acid sequence and contained 13 putative transmembrane helices. hCNT3 was 48, 47, and 57% identical to hCNT1, hCNT2, and hfCNT, respectively. When produced in Xenopus oocytes, both proteins exhibited Na+-dependentcib-type functional activities. hCNT3 was electrogenic, and a sigmoidal dependence of uridine influx on Na+concentration indicated a Na+:uridine coupling ratio of at least 2:1 for both hCNT3 and mCNT3 (cf 1:1 for hCNT1/2). Phorbol myristate acetate-induced differentiation of HL-60 cells led to the parallel appearance of cib-type activity and hCNT3 mRNA. Tissues containing hCNT3 transcripts included pancreas, bone marrow, trachea, mammary gland, liver, prostrate, and regions of intestine, brain, and heart. The hCNT3 gene mapped to chromosome 9q22.2 and included an upstream phorbol myristate acetate response element. |
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AbstractList | The human concentrative (Na+-linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (systemcit) and purine nucleosides (system cif), respectively. Both have homologs in other mammalian species and belong to a gene family (CNT) that also includes hfCNT, a newly identified broad specificity pyrimidine and purine Na+-nucleoside symporter (system cib) from the ancient marine vertebrate, the Pacific hagfish (Eptatretus stouti). We now report the cDNA cloning and characterization of cib homologs of hfCNT from human mammary gland, differentiated human myeloid HL-60 cells, and mouse liver. The 691- and 703-residue human and mouse proteins, designated hCNT3 and mCNT3, respectively, were 79% identical in amino acid sequence and contained 13 putative transmembrane helices. hCNT3 was 48, 47, and 57% identical to hCNT1, hCNT2, and hfCNT, respectively. When produced in Xenopus oocytes, both proteins exhibited Na+-dependentcib-type functional activities. hCNT3 was electrogenic, and a sigmoidal dependence of uridine influx on Na+concentration indicated a Na+:uridine coupling ratio of at least 2:1 for both hCNT3 and mCNT3 (cf 1:1 for hCNT1/2). Phorbol myristate acetate-induced differentiation of HL-60 cells led to the parallel appearance of cib-type activity and hCNT3 mRNA. Tissues containing hCNT3 transcripts included pancreas, bone marrow, trachea, mammary gland, liver, prostrate, and regions of intestine, brain, and heart. The hCNT3 gene mapped to chromosome 9q22.2 and included an upstream phorbol myristate acetate response element. The human concentrative (Na + -linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (system cit ) and purine nucleosides (system cif ), respectively. Both have homologs in other mammalian species and belong to a gene family (CNT) that also includes hfCNT, a newly identified broad specificity pyrimidine and purine Na + -nucleoside symporter (system cib ) from the ancient marine vertebrate, the Pacific hagfish ( Eptatretus stouti ). We now report the cDNA cloning and characterization of cib homologs of hfCNT from human mammary gland, differentiated human myeloid HL-60 cells, and mouse liver. The 691- and 703-residue human and mouse proteins, designated hCNT3 and mCNT3, respectively, were 79% identical in amino acid sequence and contained 13 putative transmembrane helices. hCNT3 was 48, 47, and 57% identical to hCNT1, hCNT2, and hfCNT, respectively. When produced in Xenopus oocytes, both proteins exhibited Na + -dependent cib -type functional activities. hCNT3 was electrogenic, and a sigmoidal dependence of uridine influx on Na + concentration indicated a Na + :uridine coupling ratio of at least 2:1 for both hCNT3 and mCNT3 ( cf 1:1 for hCNT1/2). Phorbol myristate acetate-induced differentiation of HL-60 cells led to the parallel appearance of cib -type activity and hCNT3 mRNA. Tissues containing hCNT3 transcripts included pancreas, bone marrow, trachea, mammary gland, liver, prostrate, and regions of intestine, brain, and heart. The hCNT3 gene mapped to chromosome 9q22.2 and included an upstream phorbol myristate acetate response element. The human concentrative (Na(+)-linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (system cit) and purine nucleosides (system cif), respectively. Both have homologs in other mammalian species and belong to a gene family (CNT) that also includes hfCNT, a newly identified broad specificity pyrimidine and purine Na(+)-nucleoside symporter (system cib) from the ancient marine vertebrate, the Pacific hagfish (Eptatretus stouti). We now report the cDNA cloning and characterization of cib homologs of hfCNT from human mammary gland, differentiated human myeloid HL-60 cells, and mouse liver. The 691- and 703-residue human and mouse proteins, designated hCNT3 and mCNT3, respectively, were 79% identical in amino acid sequence and contained 13 putative transmembrane helices. hCNT3 was 48, 47, and 57% identical to hCNT1, hCNT2, and hfCNT, respectively. When produced in Xenopus oocytes, both proteins exhibited Na(+)-dependent cib-type functional activities. hCNT3 was electrogenic, and a sigmoidal dependence of uridine influx on Na(+) concentration indicated a Na(+):uridine coupling ratio of at least 2:1 for both hCNT3 and mCNT3 (cf 1:1 for hCNT1/2). Phorbol myristate acetate-induced differentiation of HL-60 cells led to the parallel appearance of cib-type activity and hCNT3 mRNA. Tissues containing hCNT3 transcripts included pancreas, bone marrow, trachea, mammary gland, liver, prostate, and regions of intestine, brain, and heart. The hCNT3 gene mapped to chromosome 9q22.2 and included an upstream phorbol myristate acetate response element. |
Author | Young, James D. Cass, Carol E. Loewen, Shaun K. Ritzel, R. Gary Ritzel, Mabel W.L. Ng, Amy M.L. Hyde, Ralph J. Mowles, Delores A. Karpinski, Edward Carpenter, Pat Yao, Sylvia Y.M. Baldwin, Stephen A. Chen, Xing-Zhen Graham, Kathryn Smith, Kyla M. |
Author_xml | – sequence: 1 givenname: Mabel W.L. surname: Ritzel fullname: Ritzel, Mabel W.L. organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 2 givenname: Amy M.L. surname: Ng fullname: Ng, Amy M.L. organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 3 givenname: Sylvia Y.M. surname: Yao fullname: Yao, Sylvia Y.M. organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 4 givenname: Kathryn surname: Graham fullname: Graham, Kathryn organization: Department of Oncology, Edmonton, Alberta T6G 2H7, Canada – sequence: 5 givenname: Shaun K. surname: Loewen fullname: Loewen, Shaun K. organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 6 givenname: Kyla M. surname: Smith fullname: Smith, Kyla M. organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 7 givenname: R. Gary surname: Ritzel fullname: Ritzel, R. Gary organization: Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2H7, Canada – sequence: 8 givenname: Delores A. surname: Mowles fullname: Mowles, Delores A. organization: Department of Oncology, Edmonton, Alberta T6G 2H7, Canada – sequence: 9 givenname: Pat surname: Carpenter fullname: Carpenter, Pat organization: Department of Oncology, Edmonton, Alberta T6G 2H7, Canada – sequence: 10 givenname: Xing-Zhen surname: Chen fullname: Chen, Xing-Zhen organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 11 givenname: Edward surname: Karpinski fullname: Karpinski, Edward organization: Department of Physiology, Edmonton, Alberta T6G 2H7, Canada – sequence: 12 givenname: Ralph J. surname: Hyde fullname: Hyde, Ralph J. organization: School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom – sequence: 13 givenname: Stephen A. surname: Baldwin fullname: Baldwin, Stephen A. organization: School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom – sequence: 14 givenname: Carol E. surname: Cass fullname: Cass, Carol E. organization: Department of Oncology, Edmonton, Alberta T6G 2H7, Canada – sequence: 15 givenname: James D. surname: Young fullname: Young, James D. organization: Membrane Transport Research Group, Edmonton, Alberta T6G 2H7, Canada |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11032837$$D View this record in MEDLINE/PubMed |
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Snippet | The human concentrative (Na+-linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (systemcit) and purine... The human concentrative (Na + -linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (system cit ) and purine... The human concentrative (Na(+)-linked) plasma membrane transport proteins hCNT1 and hCNT2 are selective for pyrimidine nucleosides (system cit) and purine... |
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SubjectTerms | Amino Acid Sequence Animals Biological Transport Carrier Proteins - genetics Carrier Proteins - metabolism Cell Differentiation Dilazep - pharmacology Dipyridamole - pharmacology Electric Conductivity Evolution, Molecular HL-60 Cells Humans Membrane Transport Proteins Mice Models, Molecular Molecular Sequence Data Purine Nucleosides - metabolism Pyrimidine Nucleosides - metabolism Recombinant Proteins - metabolism Sequence Homology, Amino Acid Sodium - metabolism Substrate Specificity Symporters Thioinosine - analogs & derivatives Thioinosine - pharmacology Uridine - metabolism |
Title | Molecular Identification and Characterization of Novel Human and Mouse Concentrative Na+-Nucleoside Cotransporter Proteins (hCNT3 and mCNT3) Broadly Selective for Purine and Pyrimidine Nucleosides (System cib) |
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