The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria. Implications for our understanding of mitochondrial cytopathies in man
We have studied the control by complex III of both succinate-cytochrome c reductase and of oxidative flux measured polarographically in rat muscle and liver mitochondria using the specific inhibitor, myxothiazol, to induce partial inhibitions of complex III activity. Complex III exerted a low degree...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-02, Vol.269 (5), p.3523-3528 |
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| creator | TAYLOR, R. W BIRCH-MACHIN, M. A BARTLETT, K LOWERSON, S. A TURNBULL, D. M |
| description | We have studied the control by complex III of both succinate-cytochrome c reductase and of oxidative flux measured polarographically
in rat muscle and liver mitochondria using the specific inhibitor, myxothiazol, to induce partial inhibitions of complex III
activity. Complex III exerted a low degree of control on electron flux through succinate-cytochrome c reductase, and a 30-50%
decrease in complex III activity remained undetected by this assay. However, when overall oxidative flux was measured polarographically
there was a considerable difference in the effect of lowered complex III activity on this pathway between rat muscle and liver
mitochondria. Small changes in complex III activity (approximately 5% inhibition) in muscle mitochondria caused marked changes
in succinate-stimulated respiration, whereas in liver mitochondria complex III had to be inhibited by about 45% before changes
in maximum oxidation rates could be detected. These differences between muscle and liver mitochondria occurred despite rat
liver mitochondria having at least a 4-fold lower complex III activity. This suggests that when considering the biochemical
consequences of defects of the respiratory chain an important factor is the degree to which an individual complex can be lowered
before major changes in overall flux occur. In addition, since many patients with respiratory chain disease present with predominantly
muscle symptoms, this latter finding suggests that an understanding of the control of mitochondrial oxidations by different
tissues may be important when considering the tissue-specific nature of defects of the respiratory chain. |
| doi_str_mv | 10.1016/S0021-9258(17)41894-1 |
| format | Article |
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in rat muscle and liver mitochondria using the specific inhibitor, myxothiazol, to induce partial inhibitions of complex III
activity. Complex III exerted a low degree of control on electron flux through succinate-cytochrome c reductase, and a 30-50%
decrease in complex III activity remained undetected by this assay. However, when overall oxidative flux was measured polarographically
there was a considerable difference in the effect of lowered complex III activity on this pathway between rat muscle and liver
mitochondria. Small changes in complex III activity (approximately 5% inhibition) in muscle mitochondria caused marked changes
in succinate-stimulated respiration, whereas in liver mitochondria complex III had to be inhibited by about 45% before changes
in maximum oxidation rates could be detected. These differences between muscle and liver mitochondria occurred despite rat
liver mitochondria having at least a 4-fold lower complex III activity. This suggests that when considering the biochemical
consequences of defects of the respiratory chain an important factor is the degree to which an individual complex can be lowered
before major changes in overall flux occur. In addition, since many patients with respiratory chain disease present with predominantly
muscle symptoms, this latter finding suggests that an understanding of the control of mitochondrial oxidations by different
tissues may be important when considering the tissue-specific nature of defects of the respiratory chain.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)41894-1</identifier><identifier>PMID: 8106394</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Antifungal Agents - pharmacology ; Biological and medical sciences ; Cell structures and functions ; Cytochrome b Group - metabolism ; Electron Transport Complex III - antagonists & inhibitors ; Electron Transport Complex III - metabolism ; Fundamental and applied biological sciences. Psychology ; Humans ; Kinetics ; Methacrylates ; Mitochondria and cell respiration ; Mitochondria, Liver - enzymology ; Mitochondria, Liver - metabolism ; Mitochondria, Muscle - enzymology ; Mitochondria, Muscle - metabolism ; Mitochondrial Myopathies - enzymology ; Mitochondrial Myopathies - metabolism ; Molecular and cellular biology ; NAD(P)H Dehydrogenase (Quinone) - metabolism ; Oxidation-Reduction ; Oxygen Consumption ; Rats ; Species Specificity ; Thiazoles - pharmacology</subject><ispartof>The Journal of biological chemistry, 1994-02, Vol.269 (5), p.3523-3528</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c407t-557eaaa6414dc206dd1ca79e4c2780d553141e7cb1b33ca25bf84c82fb74a7893</citedby><cites>FETCH-LOGICAL-c407t-557eaaa6414dc206dd1ca79e4c2780d553141e7cb1b33ca25bf84c82fb74a7893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4001362$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8106394$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TAYLOR, R. W</creatorcontrib><creatorcontrib>BIRCH-MACHIN, M. A</creatorcontrib><creatorcontrib>BARTLETT, K</creatorcontrib><creatorcontrib>LOWERSON, S. A</creatorcontrib><creatorcontrib>TURNBULL, D. M</creatorcontrib><title>The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria. Implications for our understanding of mitochondrial cytopathies in man</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have studied the control by complex III of both succinate-cytochrome c reductase and of oxidative flux measured polarographically
in rat muscle and liver mitochondria using the specific inhibitor, myxothiazol, to induce partial inhibitions of complex III
activity. Complex III exerted a low degree of control on electron flux through succinate-cytochrome c reductase, and a 30-50%
decrease in complex III activity remained undetected by this assay. However, when overall oxidative flux was measured polarographically
there was a considerable difference in the effect of lowered complex III activity on this pathway between rat muscle and liver
mitochondria. Small changes in complex III activity (approximately 5% inhibition) in muscle mitochondria caused marked changes
in succinate-stimulated respiration, whereas in liver mitochondria complex III had to be inhibited by about 45% before changes
in maximum oxidation rates could be detected. These differences between muscle and liver mitochondria occurred despite rat
liver mitochondria having at least a 4-fold lower complex III activity. This suggests that when considering the biochemical
consequences of defects of the respiratory chain an important factor is the degree to which an individual complex can be lowered
before major changes in overall flux occur. In addition, since many patients with respiratory chain disease present with predominantly
muscle symptoms, this latter finding suggests that an understanding of the control of mitochondrial oxidations by different
tissues may be important when considering the tissue-specific nature of defects of the respiratory chain.</description><subject>Animals</subject><subject>Antifungal Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Cytochrome b Group - metabolism</subject><subject>Electron Transport Complex III - antagonists & inhibitors</subject><subject>Electron Transport Complex III - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Methacrylates</subject><subject>Mitochondria and cell respiration</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Mitochondria, Liver - metabolism</subject><subject>Mitochondria, Muscle - enzymology</subject><subject>Mitochondria, Muscle - metabolism</subject><subject>Mitochondrial Myopathies - enzymology</subject><subject>Mitochondrial Myopathies - metabolism</subject><subject>Molecular and cellular biology</subject><subject>NAD(P)H Dehydrogenase (Quinone) - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Oxygen Consumption</subject><subject>Rats</subject><subject>Species Specificity</subject><subject>Thiazoles - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkd1q3DAQhUVpSDdpHyEgSinphVONJVnyZQn9MQR60RR6J2RZjlVsaSvZbfZ5-qLRZs1CyNwMzHxnDsxB6ALIFRCoPv4gpISiLrm8BPGBgaxZAS_QBoikBeXw6yXaHJFX6Cyl3yQXq-EUnUogFa3ZBv2_HSw2wc8xjDj0eHJzMEPwXXQ6D-5dp2cXfMLtLmPTdrT3uGka7DyOesbTksxosfYdHt1fG5_or3CTBc6sF_oQcVgiXnxnY5qzxvm7555mN4etngdn095l0v41Oun1mOybtZ-jn18-315_K26-f22uP90UhhExF5wLq7WuGLDOlKTqOjBa1JaZUkjScU6BgRWmhZZSo0ve9pIZWfatYFrImp6j94e72xj-LDbNanLJ2HHU3oYlKVFRXglZZZAfQBNDStH2ahvdpONOAVH7cNRjOGr_eQVCPYajIOsuVoOlnWx3VK1p5P27da-T0WMftTcuHTFGCNCqzNjbAza4u-Gfi1a1Lj_QTqqsasUV5SWlD-x8poc</recordid><startdate>19940204</startdate><enddate>19940204</enddate><creator>TAYLOR, R. W</creator><creator>BIRCH-MACHIN, M. A</creator><creator>BARTLETT, K</creator><creator>LOWERSON, S. A</creator><creator>TURNBULL, D. M</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>19940204</creationdate><title>The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria. Implications for our understanding of mitochondrial cytopathies in man</title><author>TAYLOR, R. W ; BIRCH-MACHIN, M. A ; BARTLETT, K ; LOWERSON, S. A ; TURNBULL, D. M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c407t-557eaaa6414dc206dd1ca79e4c2780d553141e7cb1b33ca25bf84c82fb74a7893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Antifungal Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Cytochrome b Group - metabolism</topic><topic>Electron Transport Complex III - antagonists & inhibitors</topic><topic>Electron Transport Complex III - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Methacrylates</topic><topic>Mitochondria and cell respiration</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Mitochondria, Liver - metabolism</topic><topic>Mitochondria, Muscle - enzymology</topic><topic>Mitochondria, Muscle - metabolism</topic><topic>Mitochondrial Myopathies - enzymology</topic><topic>Mitochondrial Myopathies - metabolism</topic><topic>Molecular and cellular biology</topic><topic>NAD(P)H Dehydrogenase (Quinone) - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Oxygen Consumption</topic><topic>Rats</topic><topic>Species Specificity</topic><topic>Thiazoles - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TAYLOR, R. W</creatorcontrib><creatorcontrib>BIRCH-MACHIN, M. A</creatorcontrib><creatorcontrib>BARTLETT, K</creatorcontrib><creatorcontrib>LOWERSON, S. A</creatorcontrib><creatorcontrib>TURNBULL, D. M</creatorcontrib><collection>Pascal-Francis</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TAYLOR, R. W</au><au>BIRCH-MACHIN, M. A</au><au>BARTLETT, K</au><au>LOWERSON, S. A</au><au>TURNBULL, D. M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria. Implications for our understanding of mitochondrial cytopathies in man</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-02-04</date><risdate>1994</risdate><volume>269</volume><issue>5</issue><spage>3523</spage><epage>3528</epage><pages>3523-3528</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have studied the control by complex III of both succinate-cytochrome c reductase and of oxidative flux measured polarographically
in rat muscle and liver mitochondria using the specific inhibitor, myxothiazol, to induce partial inhibitions of complex III
activity. Complex III exerted a low degree of control on electron flux through succinate-cytochrome c reductase, and a 30-50%
decrease in complex III activity remained undetected by this assay. However, when overall oxidative flux was measured polarographically
there was a considerable difference in the effect of lowered complex III activity on this pathway between rat muscle and liver
mitochondria. Small changes in complex III activity (approximately 5% inhibition) in muscle mitochondria caused marked changes
in succinate-stimulated respiration, whereas in liver mitochondria complex III had to be inhibited by about 45% before changes
in maximum oxidation rates could be detected. These differences between muscle and liver mitochondria occurred despite rat
liver mitochondria having at least a 4-fold lower complex III activity. This suggests that when considering the biochemical
consequences of defects of the respiratory chain an important factor is the degree to which an individual complex can be lowered
before major changes in overall flux occur. In addition, since many patients with respiratory chain disease present with predominantly
muscle symptoms, this latter finding suggests that an understanding of the control of mitochondrial oxidations by different
tissues may be important when considering the tissue-specific nature of defects of the respiratory chain.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8106394</pmid><doi>10.1016/S0021-9258(17)41894-1</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antifungal Agents - pharmacology Biological and medical sciences Cell structures and functions Cytochrome b Group - metabolism Electron Transport Complex III - antagonists & inhibitors Electron Transport Complex III - metabolism Fundamental and applied biological sciences. Psychology Humans Kinetics Methacrylates Mitochondria and cell respiration Mitochondria, Liver - enzymology Mitochondria, Liver - metabolism Mitochondria, Muscle - enzymology Mitochondria, Muscle - metabolism Mitochondrial Myopathies - enzymology Mitochondrial Myopathies - metabolism Molecular and cellular biology NAD(P)H Dehydrogenase (Quinone) - metabolism Oxidation-Reduction Oxygen Consumption Rats Species Specificity Thiazoles - pharmacology |
| title | The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria. Implications for our understanding of mitochondrial cytopathies in man |
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