Characterization of oxalate as a catabolite of dichloroacetate responsible for the inhibition of gluconeogenesis and pyruvate carboxylation in rat liver cells
In isolated hepatocytes, dichloroacetate decreased glucose synthesis from lactate, pyruvate and alanine, but not from substrates which bypass pyruvate carboxylase (propionate, glycerol). It was also found to inhibit pyruvate carboxylation in isolated mitochondria, but only after a preincubation peri...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1978-12, Vol.85 (3), p.1180-1185 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Demaugre, France Cepanec, Claude Leroux, Jean-Paul |
| description | In isolated hepatocytes, dichloroacetate decreased glucose synthesis from lactate, pyruvate and alanine, but not from substrates which bypass pyruvate carboxylase (propionate, glycerol). It was also found to inhibit pyruvate carboxylation in isolated mitochondria, but only after a preincubation period, and had no effect on partially purified pyruvate carboxylase. Hepatocytes and liver mitochondria metabolized [
14C] dichloroacetate to oxalate which inhibits pyruvate carboxylase and mimics, without preincubation, the effects of dichloroacetate in mitochondrial pyruvate carboxylation. Thus, oxalate appears to be responsible for the inhibition of gluconeogenesis by dichloroacetate at the level of pyruvate carboxylation. |
| doi_str_mv | 10.1016/0006-291X(78)90666-6 |
| format | Article |
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14C] dichloroacetate to oxalate which inhibits pyruvate carboxylase and mimics, without preincubation, the effects of dichloroacetate in mitochondrial pyruvate carboxylation. Thus, oxalate appears to be responsible for the inhibition of gluconeogenesis by dichloroacetate at the level of pyruvate carboxylation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(78)90666-6</identifier><identifier>PMID: 736958</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetates - pharmacology ; Animals ; Dichloroacetic Acid - metabolism ; Dichloroacetic Acid - pharmacology ; Fasting ; Gluconeogenesis - drug effects ; In Vitro Techniques ; Kinetics ; Liver - drug effects ; Liver - metabolism ; Mitochondria, Liver - metabolism ; Oxalates - metabolism ; Oxalates - pharmacology ; Pyruvate Carboxylase - metabolism ; Pyruvates - metabolism ; Rats</subject><ispartof>Biochemical and biophysical research communications, 1978-12, Vol.85 (3), p.1180-1185</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-d5ef7b4ec2b72863854de67329dd6d24ef339b04b969077eb3782ca5ecb816d33</citedby><cites>FETCH-LOGICAL-c356t-d5ef7b4ec2b72863854de67329dd6d24ef339b04b969077eb3782ca5ecb816d33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(78)90666-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/736958$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Demaugre, France</creatorcontrib><creatorcontrib>Cepanec, Claude</creatorcontrib><creatorcontrib>Leroux, Jean-Paul</creatorcontrib><title>Characterization of oxalate as a catabolite of dichloroacetate responsible for the inhibition of gluconeogenesis and pyruvate carboxylation in rat liver cells</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>In isolated hepatocytes, dichloroacetate decreased glucose synthesis from lactate, pyruvate and alanine, but not from substrates which bypass pyruvate carboxylase (propionate, glycerol). It was also found to inhibit pyruvate carboxylation in isolated mitochondria, but only after a preincubation period, and had no effect on partially purified pyruvate carboxylase. Hepatocytes and liver mitochondria metabolized [
14C] dichloroacetate to oxalate which inhibits pyruvate carboxylase and mimics, without preincubation, the effects of dichloroacetate in mitochondrial pyruvate carboxylation. Thus, oxalate appears to be responsible for the inhibition of gluconeogenesis by dichloroacetate at the level of pyruvate carboxylation.</description><subject>Acetates - pharmacology</subject><subject>Animals</subject><subject>Dichloroacetic Acid - metabolism</subject><subject>Dichloroacetic Acid - pharmacology</subject><subject>Fasting</subject><subject>Gluconeogenesis - drug effects</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Liver - drug effects</subject><subject>Liver - metabolism</subject><subject>Mitochondria, Liver - metabolism</subject><subject>Oxalates - metabolism</subject><subject>Oxalates - pharmacology</subject><subject>Pyruvate Carboxylase - metabolism</subject><subject>Pyruvates - metabolism</subject><subject>Rats</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtv3CAUhVHV1zTtP8iCVdUunILBYDaVolFfUqRsUqk7xOM6Q8WYKeBRpj-mv7V2nWaZFULnnI_LPQidU3JBCRUfCCGiaRX98U727xURQjTiCdpQokjTUsKfos2D5SV6VcpPQijlQr1AzyUTqus36M92Z7JxFXL4bWpII04DTncmmgrYFGywM9XYFMN8nyUf3C6mnIyDulgylEMaS7AR8JAyrjvAYdwFG_7DbuPk0gjpFkYoYSaOHh9OeToucWeyTXenuD4dRpxNxTEcIWMHMZbX6NlgYoE39-cZ-v750832a3N1_eXb9vKqcawTtfEdDNJycK2VbS9Y33EPQrJWeS98y2FgTFnCrRKKSAmWyb51pgNneyo8Y2fo7co95PRrglL1PpRlAjNPPhUtOWsF78hs5KvR5VRKhkEfctibfNKU6KUVvaxcLyvXstf_WtFijp3f8ye7B_8QWmuY5Y-rDPMfjwGyLi7A6MCHDK5qn8Lj_L9qwKDO</recordid><startdate>19781214</startdate><enddate>19781214</enddate><creator>Demaugre, France</creator><creator>Cepanec, Claude</creator><creator>Leroux, Jean-Paul</creator><general>Elsevier Inc</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>19781214</creationdate><title>Characterization of oxalate as a catabolite of dichloroacetate responsible for the inhibition of gluconeogenesis and pyruvate carboxylation in rat liver cells</title><author>Demaugre, France ; Cepanec, Claude ; Leroux, Jean-Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-d5ef7b4ec2b72863854de67329dd6d24ef339b04b969077eb3782ca5ecb816d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Acetates - pharmacology</topic><topic>Animals</topic><topic>Dichloroacetic Acid - metabolism</topic><topic>Dichloroacetic Acid - pharmacology</topic><topic>Fasting</topic><topic>Gluconeogenesis - drug effects</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Liver - drug effects</topic><topic>Liver - metabolism</topic><topic>Mitochondria, Liver - metabolism</topic><topic>Oxalates - metabolism</topic><topic>Oxalates - pharmacology</topic><topic>Pyruvate Carboxylase - metabolism</topic><topic>Pyruvates - metabolism</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Demaugre, France</creatorcontrib><creatorcontrib>Cepanec, Claude</creatorcontrib><creatorcontrib>Leroux, Jean-Paul</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Demaugre, France</au><au>Cepanec, Claude</au><au>Leroux, Jean-Paul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of oxalate as a catabolite of dichloroacetate responsible for the inhibition of gluconeogenesis and pyruvate carboxylation in rat liver cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1978-12-14</date><risdate>1978</risdate><volume>85</volume><issue>3</issue><spage>1180</spage><epage>1185</epage><pages>1180-1185</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>In isolated hepatocytes, dichloroacetate decreased glucose synthesis from lactate, pyruvate and alanine, but not from substrates which bypass pyruvate carboxylase (propionate, glycerol). It was also found to inhibit pyruvate carboxylation in isolated mitochondria, but only after a preincubation period, and had no effect on partially purified pyruvate carboxylase. Hepatocytes and liver mitochondria metabolized [
14C] dichloroacetate to oxalate which inhibits pyruvate carboxylase and mimics, without preincubation, the effects of dichloroacetate in mitochondrial pyruvate carboxylation. Thus, oxalate appears to be responsible for the inhibition of gluconeogenesis by dichloroacetate at the level of pyruvate carboxylation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>736958</pmid><doi>10.1016/0006-291X(78)90666-6</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1978-12, Vol.85 (3), p.1180-1185 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Acetates - pharmacology Animals Dichloroacetic Acid - metabolism Dichloroacetic Acid - pharmacology Fasting Gluconeogenesis - drug effects In Vitro Techniques Kinetics Liver - drug effects Liver - metabolism Mitochondria, Liver - metabolism Oxalates - metabolism Oxalates - pharmacology Pyruvate Carboxylase - metabolism Pyruvates - metabolism Rats |
| title | Characterization of oxalate as a catabolite of dichloroacetate responsible for the inhibition of gluconeogenesis and pyruvate carboxylation in rat liver cells |
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