Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. We have isolated a full-length cDNA copy of 4.3 kilobase pairs encoding the ATP-citrate lyase mRNA by screening rat liver cDNA library using oligonucleotide probes designed from peptide seq...
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| Veröffentlicht in: | The Journal of biological chemistry 1990-01, Vol.265 (3), p.1430-1435 |
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| container_title | The Journal of biological chemistry |
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| creator | Elshourbagy, N A Near, J C Kmetz, P J Sathe, G M Southan, C Strickler, J E Gross, M Young, J F Wells, T N Groot, P H |
| description | ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. We have isolated
a full-length cDNA copy of 4.3 kilobase pairs encoding the ATP-citrate lyase mRNA by screening rat liver cDNA library using
oligonucleotide probes designed from peptide sequences obtained from the purified rat enzyme. Expression of this cDNA in bacteria,
followed by immunoblotting with antibody directed against the ATP citrate-lyase, further demonstrated the identity of this
clone. Nucleic acid sequence data indicate that the cDNA contains the complete coding region for the enzyme, which is 1100
amino acids in length with a calculated molecular weight of 121,293. RNA blot analysis indicated an mRNA species of about
4.3 kilobase pairs in livers of chow-fed rats. Rats maintained on low fat, high carbohydrate diets exhibited a striking increase
(50-fold) in the level of liver ATP citrate-lyase mRNA as compared with the control animals maintained on a normal diet. The
tissue distribution of this mRNA in chow-fed animals revealed a relatively high abundance of the message in liver and adrenal,
moderate levels were found in lung, brain, and large intestine with only trace amounts of the message in small intestine,
stomach, testis, spleen, pancreas, kidney, and heart. During rat development, the ATP citrate-lyase mRNA was relatively high
in the liver at parturition, followed by a reduction in its level during suckling. Higher amounts of the mRNA were detected
again in adult animals. The isolation and characterization of the mRNA for ATP citrate-lyase will allow further studies on
the reaction mechanism and metabolic regulation of this key enzyme in lipogenesis and cholesterogenesis. |
| doi_str_mv | 10.1016/s0021-9258(19)40033-1 |
| format | Article |
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a full-length cDNA copy of 4.3 kilobase pairs encoding the ATP-citrate lyase mRNA by screening rat liver cDNA library using
oligonucleotide probes designed from peptide sequences obtained from the purified rat enzyme. Expression of this cDNA in bacteria,
followed by immunoblotting with antibody directed against the ATP citrate-lyase, further demonstrated the identity of this
clone. Nucleic acid sequence data indicate that the cDNA contains the complete coding region for the enzyme, which is 1100
amino acids in length with a calculated molecular weight of 121,293. RNA blot analysis indicated an mRNA species of about
4.3 kilobase pairs in livers of chow-fed rats. Rats maintained on low fat, high carbohydrate diets exhibited a striking increase
(50-fold) in the level of liver ATP citrate-lyase mRNA as compared with the control animals maintained on a normal diet. The
tissue distribution of this mRNA in chow-fed animals revealed a relatively high abundance of the message in liver and adrenal,
moderate levels were found in lung, brain, and large intestine with only trace amounts of the message in small intestine,
stomach, testis, spleen, pancreas, kidney, and heart. During rat development, the ATP citrate-lyase mRNA was relatively high
in the liver at parturition, followed by a reduction in its level during suckling. Higher amounts of the mRNA were detected
again in adult animals. The isolation and characterization of the mRNA for ATP citrate-lyase will allow further studies on
the reaction mechanism and metabolic regulation of this key enzyme in lipogenesis and cholesterogenesis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)40033-1</identifier><identifier>PMID: 2295639</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphate - metabolism ; Age Factors ; Amino Acid Sequence ; Animals ; ATP Citrate (pro-S)-Lyase - genetics ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Coenzyme A - metabolism ; Diet ; DNA - genetics ; genes ; Liver - enzymology ; Molecular Sequence Data ; Molecular Weight ; Peptide Fragments - analysis ; Rats ; Restriction Mapping ; RNA, Messenger - genetics ; Tissue Distribution</subject><ispartof>The Journal of biological chemistry, 1990-01, Vol.265 (3), p.1430-1435</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3901-7f5f2992d5385015dcb6a215abd9268741af68760c3c426be7fd9c4992edd5413</citedby><cites>FETCH-LOGICAL-c3901-7f5f2992d5385015dcb6a215abd9268741af68760c3c426be7fd9c4992edd5413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2295639$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Elshourbagy, N A</creatorcontrib><creatorcontrib>Near, J C</creatorcontrib><creatorcontrib>Kmetz, P J</creatorcontrib><creatorcontrib>Sathe, G M</creatorcontrib><creatorcontrib>Southan, C</creatorcontrib><creatorcontrib>Strickler, J E</creatorcontrib><creatorcontrib>Gross, M</creatorcontrib><creatorcontrib>Young, J F</creatorcontrib><creatorcontrib>Wells, T N</creatorcontrib><creatorcontrib>Groot, P H</creatorcontrib><title>Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. We have isolated
a full-length cDNA copy of 4.3 kilobase pairs encoding the ATP-citrate lyase mRNA by screening rat liver cDNA library using
oligonucleotide probes designed from peptide sequences obtained from the purified rat enzyme. Expression of this cDNA in bacteria,
followed by immunoblotting with antibody directed against the ATP citrate-lyase, further demonstrated the identity of this
clone. Nucleic acid sequence data indicate that the cDNA contains the complete coding region for the enzyme, which is 1100
amino acids in length with a calculated molecular weight of 121,293. RNA blot analysis indicated an mRNA species of about
4.3 kilobase pairs in livers of chow-fed rats. Rats maintained on low fat, high carbohydrate diets exhibited a striking increase
(50-fold) in the level of liver ATP citrate-lyase mRNA as compared with the control animals maintained on a normal diet. The
tissue distribution of this mRNA in chow-fed animals revealed a relatively high abundance of the message in liver and adrenal,
moderate levels were found in lung, brain, and large intestine with only trace amounts of the message in small intestine,
stomach, testis, spleen, pancreas, kidney, and heart. During rat development, the ATP citrate-lyase mRNA was relatively high
in the liver at parturition, followed by a reduction in its level during suckling. Higher amounts of the mRNA were detected
again in adult animals. The isolation and characterization of the mRNA for ATP citrate-lyase will allow further studies on
the reaction mechanism and metabolic regulation of this key enzyme in lipogenesis and cholesterogenesis.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Age Factors</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>ATP Citrate (pro-S)-Lyase - genetics</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Cloning, Molecular</subject><subject>Coenzyme A - metabolism</subject><subject>Diet</subject><subject>DNA - genetics</subject><subject>genes</subject><subject>Liver - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - analysis</subject><subject>Rats</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - genetics</subject><subject>Tissue Distribution</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kdtu1DAQhi0EKkvhESpZXCCQmuJD7F1frsqpUimoFIk7y7EnWSPHLnaiah-i70ySXXVuZqz5vxn5H4TOKLmghMqPhRBGK8XE5j1VH2pCOK_oM7SiZMMrLuif52j1JHmJXpXyl0xRK3qCThhTQnK1Qo-3ZsDbu5_Y-iGbAaqwNwUu8PcUwI7BZGxDij522ESHC_wbIVqYHibsiy84tdjgdgyhChC7YYftp5vtou1v56IZozMLURZhtINPccach-Ecp9yZeL4ApoPX6EVrQoE3x3yKfn_5fHf5rbr-8fXqcntdWa4IrdataJlSzAm-EYQKZxtpGBWmcYrJzbqmpp2SJJbbmskG1q1Ttp4IcE7UlJ-id4e59zlNPyqD7n2xEIKJkMaiqailrDmfhOIgtDmVkqHV99n3Ju81JXo-g_41e6xnjzVVejmDnhecHReMTQ_uiTr6PvXfHvo73-0efAbd-GR30GsmhZ4m1Jzw_4qQjYI</recordid><startdate>19900125</startdate><enddate>19900125</enddate><creator>Elshourbagy, N A</creator><creator>Near, J C</creator><creator>Kmetz, P J</creator><creator>Sathe, G M</creator><creator>Southan, C</creator><creator>Strickler, J E</creator><creator>Gross, M</creator><creator>Young, J F</creator><creator>Wells, T N</creator><creator>Groot, P H</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19900125</creationdate><title>Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age</title><author>Elshourbagy, N A ; Near, J C ; Kmetz, P J ; Sathe, G M ; Southan, C ; Strickler, J E ; Gross, M ; Young, J F ; Wells, T N ; Groot, P H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3901-7f5f2992d5385015dcb6a215abd9268741af68760c3c426be7fd9c4992edd5413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Age Factors</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>ATP Citrate (pro-S)-Lyase - genetics</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Cloning, Molecular</topic><topic>Coenzyme A - metabolism</topic><topic>Diet</topic><topic>DNA - genetics</topic><topic>genes</topic><topic>Liver - enzymology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - analysis</topic><topic>Rats</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - genetics</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Elshourbagy, N A</creatorcontrib><creatorcontrib>Near, J C</creatorcontrib><creatorcontrib>Kmetz, P J</creatorcontrib><creatorcontrib>Sathe, G M</creatorcontrib><creatorcontrib>Southan, C</creatorcontrib><creatorcontrib>Strickler, J E</creatorcontrib><creatorcontrib>Gross, M</creatorcontrib><creatorcontrib>Young, J F</creatorcontrib><creatorcontrib>Wells, T N</creatorcontrib><creatorcontrib>Groot, P H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Elshourbagy, N A</au><au>Near, J C</au><au>Kmetz, P J</au><au>Sathe, G M</au><au>Southan, C</au><au>Strickler, J E</au><au>Gross, M</au><au>Young, J F</au><au>Wells, T N</au><au>Groot, P H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-01-25</date><risdate>1990</risdate><volume>265</volume><issue>3</issue><spage>1430</spage><epage>1435</epage><pages>1430-1435</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. We have isolated
a full-length cDNA copy of 4.3 kilobase pairs encoding the ATP-citrate lyase mRNA by screening rat liver cDNA library using
oligonucleotide probes designed from peptide sequences obtained from the purified rat enzyme. Expression of this cDNA in bacteria,
followed by immunoblotting with antibody directed against the ATP citrate-lyase, further demonstrated the identity of this
clone. Nucleic acid sequence data indicate that the cDNA contains the complete coding region for the enzyme, which is 1100
amino acids in length with a calculated molecular weight of 121,293. RNA blot analysis indicated an mRNA species of about
4.3 kilobase pairs in livers of chow-fed rats. Rats maintained on low fat, high carbohydrate diets exhibited a striking increase
(50-fold) in the level of liver ATP citrate-lyase mRNA as compared with the control animals maintained on a normal diet. The
tissue distribution of this mRNA in chow-fed animals revealed a relatively high abundance of the message in liver and adrenal,
moderate levels were found in lung, brain, and large intestine with only trace amounts of the message in small intestine,
stomach, testis, spleen, pancreas, kidney, and heart. During rat development, the ATP citrate-lyase mRNA was relatively high
in the liver at parturition, followed by a reduction in its level during suckling. Higher amounts of the mRNA were detected
again in adult animals. The isolation and characterization of the mRNA for ATP citrate-lyase will allow further studies on
the reaction mechanism and metabolic regulation of this key enzyme in lipogenesis and cholesterogenesis.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2295639</pmid><doi>10.1016/s0021-9258(19)40033-1</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1990-01, Vol.265 (3), p.1430-1435 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15466433 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Age Factors Amino Acid Sequence Animals ATP Citrate (pro-S)-Lyase - genetics Base Sequence Binding Sites Cloning, Molecular Coenzyme A - metabolism Diet DNA - genetics genes Liver - enzymology Molecular Sequence Data Molecular Weight Peptide Fragments - analysis Rats Restriction Mapping RNA, Messenger - genetics Tissue Distribution |
| title | Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age |
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