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Characterization of a dCTP Transport Activity Reconstituted from Human Mitochondria
A protein fraction of mitochondria from human acute lymphocytic leukemia cells, which could be reconstituted into proteoliposomes to have dCTP transport activity, has been partially purified by hydroxyapatite and blue Sepharose chromatography. The dCTP transport activity in proteoliposomes was time-...
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| Published in: | The Journal of biological chemistry 1999-02, Vol.274 (8), p.4620-4625 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c357t-4bd42f5d4afa45858e211f7a24b65a4cbeaf9149a44f3d7452892393676317dc3 |
| container_end_page | 4625 |
| container_issue | 8 |
| container_start_page | 4620 |
| container_title | The Journal of biological chemistry |
| container_volume | 274 |
| creator | Bridges, E G Jiang, Z Cheng, Y C |
| description | A protein fraction of mitochondria from human acute lymphocytic leukemia cells, which could be reconstituted into proteoliposomes
to have dCTP transport activity, has been partially purified by hydroxyapatite and blue Sepharose chromatography. The dCTP
transport activity in proteoliposomes was time-dependent and could be activated by Ca 2+ and to a lesser extent by Mg 2+ . None of the other divalent cations tested could activate the transport activity. The K
m value of dCTP in the presence of Ca 2+ was shown to be 3 μ m . dCDP but not dCMP or dCyd could inhibit the transport activity. Other deoxynucleoside triphosphates could also inhibit the
uptake of dCTP with the potency dGTP = dATP > TTP. Although ATP could competitively inhibit dCTP uptake with a K
i value of 8 μ m , the reconstituted dCTP uptake activity was not sensitive to the ATP/ADP carrier inhibitor atractyloside or the sulfhydryl
reagent N -ethylmaleimide. This suggests that the dCTP transport system studied is not the same as the ATP/ADP carrier. In conclusion,
these studies describe the first functionally reconstituted mitochondrial carrier that displays an efficient transport activity
for dCTP. |
| doi_str_mv | 10.1074/jbc.274.8.4620 |
| format | article |
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transport activity in proteoliposomes was time-dependent and could be activated by Ca 2+ and to a lesser extent by Mg 2+ . None of the other divalent cations tested could activate the transport activity. The K
m value of dCTP in the presence of Ca 2+ was shown to be 3 μ m . dCDP but not dCMP or dCyd could inhibit the transport activity. Other deoxynucleoside triphosphates could also inhibit the
uptake of dCTP with the potency dGTP = dATP > TTP. Although ATP could competitively inhibit dCTP uptake with a K
i value of 8 μ m , the reconstituted dCTP uptake activity was not sensitive to the ATP/ADP carrier inhibitor atractyloside or the sulfhydryl
reagent N -ethylmaleimide. This suggests that the dCTP transport system studied is not the same as the ATP/ADP carrier. In conclusion,
these studies describe the first functionally reconstituted mitochondrial carrier that displays an efficient transport activity
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to have dCTP transport activity, has been partially purified by hydroxyapatite and blue Sepharose chromatography. The dCTP
transport activity in proteoliposomes was time-dependent and could be activated by Ca 2+ and to a lesser extent by Mg 2+ . None of the other divalent cations tested could activate the transport activity. The K
m value of dCTP in the presence of Ca 2+ was shown to be 3 μ m . dCDP but not dCMP or dCyd could inhibit the transport activity. Other deoxynucleoside triphosphates could also inhibit the
uptake of dCTP with the potency dGTP = dATP > TTP. Although ATP could competitively inhibit dCTP uptake with a K
i value of 8 μ m , the reconstituted dCTP uptake activity was not sensitive to the ATP/ADP carrier inhibitor atractyloside or the sulfhydryl
reagent N -ethylmaleimide. This suggests that the dCTP transport system studied is not the same as the ATP/ADP carrier. In conclusion,
these studies describe the first functionally reconstituted mitochondrial carrier that displays an efficient transport activity
for dCTP.</description><subject>Biological Transport</subject><subject>Calcium - metabolism</subject><subject>Chromatography, Ion Exchange</subject><subject>Deoxycytosine Nucleotides - isolation & purification</subject><subject>Deoxycytosine Nucleotides - metabolism</subject><subject>Humans</subject><subject>Mitochondria - metabolism</subject><subject>Precursor Cell Lymphoblastic Leukemia-Lymphoma - metabolism</subject><subject>Proteolipids - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpNkE1LxDAURYMoOo5u3QnBhbvWJk2aZCmDXzCi6AjuQpomNjJtxiRV9NfbYQbxbd7innfhHQBOUJGjgpGL91rnmJGc56TCxQ6YoIKXWUnR6y6YFAVGmcCUH4DDGN-LcYhA-2BfCM4rwSbgedaqoHQywf2o5HwPvYUKNrPFI1wE1ceVDwle6uQ-XfqGT0b7PiaXhmQaaIPv4O3QqR7eu-R16_smOHUE9qxaRnO83VPwcn21mN1m84ebu9nlPNMlZSkjdUOwpQ1RVhHKKTcYIcsUJnVFFdG1UVYgIhQhtmwYoZgLXIqyYlWJWKPLKTjf9K6C_xhMTLJzUZvlUvXGD1FWgjKGERvBfAPq4GMMxspVcJ0K3xIVcm1RjhblaFFyubY4Hpxum4e6M80fvtU25mebvHVv7ZcLRtZufN90_0t-AaXseXA</recordid><startdate>19990219</startdate><enddate>19990219</enddate><creator>Bridges, E G</creator><creator>Jiang, Z</creator><creator>Cheng, Y C</creator><general>American Society for Biochemistry and Molecular Biology</general><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>7X8</scope></search><sort><creationdate>19990219</creationdate><title>Characterization of a dCTP Transport Activity Reconstituted from Human Mitochondria</title><author>Bridges, E G ; Jiang, Z ; Cheng, Y C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-4bd42f5d4afa45858e211f7a24b65a4cbeaf9149a44f3d7452892393676317dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Biological Transport</topic><topic>Calcium - metabolism</topic><topic>Chromatography, Ion Exchange</topic><topic>Deoxycytosine Nucleotides - isolation & purification</topic><topic>Deoxycytosine Nucleotides - metabolism</topic><topic>Humans</topic><topic>Mitochondria - metabolism</topic><topic>Precursor Cell Lymphoblastic Leukemia-Lymphoma - metabolism</topic><topic>Proteolipids - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bridges, E G</creatorcontrib><creatorcontrib>Jiang, Z</creatorcontrib><creatorcontrib>Cheng, Y C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bridges, E G</au><au>Jiang, Z</au><au>Cheng, Y C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a dCTP Transport Activity Reconstituted from Human Mitochondria</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-02-19</date><risdate>1999</risdate><volume>274</volume><issue>8</issue><spage>4620</spage><epage>4625</epage><pages>4620-4625</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A protein fraction of mitochondria from human acute lymphocytic leukemia cells, which could be reconstituted into proteoliposomes
to have dCTP transport activity, has been partially purified by hydroxyapatite and blue Sepharose chromatography. The dCTP
transport activity in proteoliposomes was time-dependent and could be activated by Ca 2+ and to a lesser extent by Mg 2+ . None of the other divalent cations tested could activate the transport activity. The K
m value of dCTP in the presence of Ca 2+ was shown to be 3 μ m . dCDP but not dCMP or dCyd could inhibit the transport activity. Other deoxynucleoside triphosphates could also inhibit the
uptake of dCTP with the potency dGTP = dATP > TTP. Although ATP could competitively inhibit dCTP uptake with a K
i value of 8 μ m , the reconstituted dCTP uptake activity was not sensitive to the ATP/ADP carrier inhibitor atractyloside or the sulfhydryl
reagent N -ethylmaleimide. This suggests that the dCTP transport system studied is not the same as the ATP/ADP carrier. In conclusion,
these studies describe the first functionally reconstituted mitochondrial carrier that displays an efficient transport activity
for dCTP.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9988697</pmid><doi>10.1074/jbc.274.8.4620</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1999-02, Vol.274 (8), p.4620-4625 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69577217 |
| source | Elsevier ScienceDirect Journals |
| subjects | Biological Transport Calcium - metabolism Chromatography, Ion Exchange Deoxycytosine Nucleotides - isolation & purification Deoxycytosine Nucleotides - metabolism Humans Mitochondria - metabolism Precursor Cell Lymphoblastic Leukemia-Lymphoma - metabolism Proteolipids - metabolism |
| title | Characterization of a dCTP Transport Activity Reconstituted from Human Mitochondria |
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