The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H + transport
The impact of uncoupling protein (UCP) 1, UCP3 and UCP3s expressed in yeast on oxidative phosphorylation, membrane potential and H + transport is determined. Intracellular ATP synthesis is inhibited by UCP3, much more than by UCP1, while similar levels of UCP3 and UCP1 exist in the mitochondrial fra...
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| Veröffentlicht in: | FEBS letters 2000-09, Vol.480 (2), p.265-270 |
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| creator | Heidkaemper, Dörthe Winkler, Edith Müller, Veronika Frischmuth, Karina Liu, Quingyun Caskey, Thomas Klingenberg, Martin |
| description | The impact of uncoupling protein (UCP) 1, UCP3 and UCP3s expressed in yeast on oxidative phosphorylation, membrane potential and H
+ transport is determined. Intracellular ATP synthesis is inhibited by UCP3, much more than by UCP1, while similar levels of UCP3 and UCP1 exist in the mitochondrial fractions. Measurements of membrane potential and H
+ efflux in isolated mitochondria show that, different from UCP1, with UCP3 and UCP3s there is a priori a preponderant uncoupling not inhibited by GDP. The results are interpreted to show that UCP3 and UCP3s in yeast mitochondria are in a deranged state causing uncontrolled uncoupling, which does not represent their physiological function. |
| doi_str_mv | 10.1016/S0014-5793(00)01949-9 |
| format | Article |
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+ transport is determined. Intracellular ATP synthesis is inhibited by UCP3, much more than by UCP1, while similar levels of UCP3 and UCP1 exist in the mitochondrial fractions. Measurements of membrane potential and H
+ efflux in isolated mitochondria show that, different from UCP1, with UCP3 and UCP3s there is a priori a preponderant uncoupling not inhibited by GDP. The results are interpreted to show that UCP3 and UCP3s in yeast mitochondria are in a deranged state causing uncontrolled uncoupling, which does not represent their physiological function.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(00)01949-9</identifier><identifier>PMID: 11034342</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Biological Transport ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; CCCP, carbonylcyanide m-chlorophenylhydrazone ; Cell Fractionation ; Cricetinae ; disC3, 3,3′-dipropylthiacarbocyanine ; FACS, fluorescent activating cell sorting ; Gene Expression ; GP, 1-glycerophosphate ; Guanosine Triphosphate - metabolism ; H +-transport ; Humans ; Hydrogen - metabolism ; Ion Channels ; LA, lauric acid ; Membrane potential ; Mitochondria ; Mitochondria - metabolism ; Mitochondria - physiology ; Mitochondrial Proteins ; Oxidation-Reduction ; Oxidative phosphorylation ; Phosphorylation ; Saccharomyces cerevisiae ; UCP, uncoupling protein ; Uncoupling protein ; Uncoupling Protein 3</subject><ispartof>FEBS letters, 2000-09, Vol.480 (2), p.265-270</ispartof><rights>2000 Federation of European Biochemical Societies</rights><rights>FEBS Letters 480 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4739-d494b62792d9e867e4e34be6ef87f22c8482d2b2c1452de428d35acf2e5233903</citedby><cites>FETCH-LOGICAL-c4739-d494b62792d9e867e4e34be6ef87f22c8482d2b2c1452de428d35acf2e5233903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2800%2901949-9$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(00)01949-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11034342$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heidkaemper, Dörthe</creatorcontrib><creatorcontrib>Winkler, Edith</creatorcontrib><creatorcontrib>Müller, Veronika</creatorcontrib><creatorcontrib>Frischmuth, Karina</creatorcontrib><creatorcontrib>Liu, Quingyun</creatorcontrib><creatorcontrib>Caskey, Thomas</creatorcontrib><creatorcontrib>Klingenberg, Martin</creatorcontrib><title>The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H + transport</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The impact of uncoupling protein (UCP) 1, UCP3 and UCP3s expressed in yeast on oxidative phosphorylation, membrane potential and H
+ transport is determined. Intracellular ATP synthesis is inhibited by UCP3, much more than by UCP1, while similar levels of UCP3 and UCP1 exist in the mitochondrial fractions. Measurements of membrane potential and H
+ efflux in isolated mitochondria show that, different from UCP1, with UCP3 and UCP3s there is a priori a preponderant uncoupling not inhibited by GDP. The results are interpreted to show that UCP3 and UCP3s in yeast mitochondria are in a deranged state causing uncontrolled uncoupling, which does not represent their physiological function.</description><subject>Animals</subject><subject>Biological Transport</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>CCCP, carbonylcyanide m-chlorophenylhydrazone</subject><subject>Cell Fractionation</subject><subject>Cricetinae</subject><subject>disC3, 3,3′-dipropylthiacarbocyanine</subject><subject>FACS, fluorescent activating cell sorting</subject><subject>Gene Expression</subject><subject>GP, 1-glycerophosphate</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>H +-transport</subject><subject>Humans</subject><subject>Hydrogen - metabolism</subject><subject>Ion Channels</subject><subject>LA, lauric acid</subject><subject>Membrane potential</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria - physiology</subject><subject>Mitochondrial Proteins</subject><subject>Oxidation-Reduction</subject><subject>Oxidative phosphorylation</subject><subject>Phosphorylation</subject><subject>Saccharomyces cerevisiae</subject><subject>UCP, uncoupling protein</subject><subject>Uncoupling protein</subject><subject>Uncoupling Protein 3</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV1rFDEUhkOxtGvtT1ByJRUZzdd85Erq0rqFgkLb65BJzmja2cmYZGz335vZXexlhUDIOe_7nsMThN5S8okSWn2-IYSKoqwlPyPkA6FSyEIeoAVtal5wUTWv0OKf5Bi9jvGe5HdD5RE6ppRwwQVbIH37C3A79Q_Yd_hu-YNjeBoDxAgWuwFvQMeEDfR9xC6fwfj1CAmGhDsfsMbDZHrwyVnAAX5OvU7ZuMIfcQp6iKMP6Q067HQf4XR_n6C7y4vb5aq4_v7tanl-XRhRc1lYIUVbsVoyK6GpahDARQsVdE3dMWYa0TDLWmaoKJkFwRrLS206BiXjXBJ-gt7vcsfgf08Qk1q7OG-uB_BTVHWW0ZJVWVjuhCb4GAN0agxurcNGUaJmtmrLVs3gFCFqy1bJ7Hu3HzC1a7DPrj3MLFjtBI-uh83_parLi69s25kb8w_l8jzryy4KMrE_DoKKxsFgwLoAJinr3Qvb_gU145vc</recordid><startdate>20000901</startdate><enddate>20000901</enddate><creator>Heidkaemper, Dörthe</creator><creator>Winkler, Edith</creator><creator>Müller, Veronika</creator><creator>Frischmuth, Karina</creator><creator>Liu, Quingyun</creator><creator>Caskey, Thomas</creator><creator>Klingenberg, Martin</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20000901</creationdate><title>The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H + transport</title><author>Heidkaemper, Dörthe ; Winkler, Edith ; Müller, Veronika ; Frischmuth, Karina ; Liu, Quingyun ; Caskey, Thomas ; Klingenberg, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4739-d494b62792d9e867e4e34be6ef87f22c8482d2b2c1452de428d35acf2e5233903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Biological Transport</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>CCCP, carbonylcyanide m-chlorophenylhydrazone</topic><topic>Cell Fractionation</topic><topic>Cricetinae</topic><topic>disC3, 3,3′-dipropylthiacarbocyanine</topic><topic>FACS, fluorescent activating cell sorting</topic><topic>Gene Expression</topic><topic>GP, 1-glycerophosphate</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>H +-transport</topic><topic>Humans</topic><topic>Hydrogen - metabolism</topic><topic>Ion Channels</topic><topic>LA, lauric acid</topic><topic>Membrane potential</topic><topic>Mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondria - physiology</topic><topic>Mitochondrial Proteins</topic><topic>Oxidation-Reduction</topic><topic>Oxidative phosphorylation</topic><topic>Phosphorylation</topic><topic>Saccharomyces cerevisiae</topic><topic>UCP, uncoupling protein</topic><topic>Uncoupling protein</topic><topic>Uncoupling Protein 3</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heidkaemper, Dörthe</creatorcontrib><creatorcontrib>Winkler, Edith</creatorcontrib><creatorcontrib>Müller, Veronika</creatorcontrib><creatorcontrib>Frischmuth, Karina</creatorcontrib><creatorcontrib>Liu, Quingyun</creatorcontrib><creatorcontrib>Caskey, Thomas</creatorcontrib><creatorcontrib>Klingenberg, Martin</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heidkaemper, Dörthe</au><au>Winkler, Edith</au><au>Müller, Veronika</au><au>Frischmuth, Karina</au><au>Liu, Quingyun</au><au>Caskey, Thomas</au><au>Klingenberg, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H + transport</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2000-09-01</date><risdate>2000</risdate><volume>480</volume><issue>2</issue><spage>265</spage><epage>270</epage><pages>265-270</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The impact of uncoupling protein (UCP) 1, UCP3 and UCP3s expressed in yeast on oxidative phosphorylation, membrane potential and H
+ transport is determined. Intracellular ATP synthesis is inhibited by UCP3, much more than by UCP1, while similar levels of UCP3 and UCP1 exist in the mitochondrial fractions. Measurements of membrane potential and H
+ efflux in isolated mitochondria show that, different from UCP1, with UCP3 and UCP3s there is a priori a preponderant uncoupling not inhibited by GDP. The results are interpreted to show that UCP3 and UCP3s in yeast mitochondria are in a deranged state causing uncontrolled uncoupling, which does not represent their physiological function.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11034342</pmid><doi>10.1016/S0014-5793(00)01949-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection |
| subjects | Animals Biological Transport Carrier Proteins - genetics Carrier Proteins - metabolism CCCP, carbonylcyanide m-chlorophenylhydrazone Cell Fractionation Cricetinae disC3, 3,3′-dipropylthiacarbocyanine FACS, fluorescent activating cell sorting Gene Expression GP, 1-glycerophosphate Guanosine Triphosphate - metabolism H +-transport Humans Hydrogen - metabolism Ion Channels LA, lauric acid Membrane potential Mitochondria Mitochondria - metabolism Mitochondria - physiology Mitochondrial Proteins Oxidation-Reduction Oxidative phosphorylation Phosphorylation Saccharomyces cerevisiae UCP, uncoupling protein Uncoupling protein Uncoupling Protein 3 |
| title | The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H + transport |
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