δ-aminolaevulinate synthase expression in muscle after contractions and recovery
The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior...
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Veröffentlicht in: | Biochemical journal 1993-04, Vol.291 (1), p.219-223 |
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description | The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist. |
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T. M ; ESSIG, D. A ; HOOD, D. A</creator><creatorcontrib>TAKAHASHI, M ; MCCURDY, D. T. M ; ESSIG, D. A ; HOOD, D. A</creatorcontrib><description>The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2910219</identifier><identifier>PMID: 8385933</identifier><language>eng</language><publisher>Colchester: Portland Press</publisher><subject>5-Aminolevulinate Synthetase - genetics ; 5-Aminolevulinate Synthetase - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Blotting, Northern ; Electric Stimulation ; Electron Transport Complex IV - metabolism ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. 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T. M</creatorcontrib><creatorcontrib>ESSIG, D. A</creatorcontrib><creatorcontrib>HOOD, D. A</creatorcontrib><title>δ-aminolaevulinate synthase expression in muscle after contractions and recovery</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist.</description><subject>5-Aminolevulinate Synthetase - genetics</subject><subject>5-Aminolevulinate Synthetase - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Electric Stimulation</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Male</subject><subject>Muscle Contraction - physiology</subject><subject>Muscles - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>RNA, Messenger - metabolism</subject><subject>Transferases</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkM1q3DAUhUVpSSc_iz5AwYsSyMLt1Y9laVMIoU0CgVJo1-JavtMo2NJUsofMe_U5-kx1yDA0q7v4Ps49HMbecfjIQYlP3YOwHAS3r9iKqxZq0wrzmq1AaFXrBbxlx6U8AHAFCo7YkZGmsVKu2Pe_f2ocQ0wD0nYeQsSJqrKL0z0Wquhxk6mUkGIVYjXOxQ9U4XqiXPkUp4x-WlipMPZVJp-2lHen7M0ah0Jn-3vCfn798uPqpr77dn17dXlXe8mVrdvWgtScd8r2WmktDPeih8Z62S2tO6NIa7TSgG971RjkjZAkseut1xxaecI-P-du5m6k3tNTn8Ftchgx71zC4F6SGO7dr7R1nEvRQLMEnO8Dcvo9U5ncGIqnYcBIaS6ubbRpjIFFvHgWfU6lZFofnnBwT_u7w_6L-_7_VgdzP_jCP-w5Fo_DOmP0oRw01SoAq-U_Gm2Oig</recordid><startdate>19930401</startdate><enddate>19930401</enddate><creator>TAKAHASHI, M</creator><creator>MCCURDY, D. T. M</creator><creator>ESSIG, D. A</creator><creator>HOOD, D. A</creator><general>Portland Press</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><scope>5PM</scope></search><sort><creationdate>19930401</creationdate><title>δ-aminolaevulinate synthase expression in muscle after contractions and recovery</title><author>TAKAHASHI, M ; MCCURDY, D. T. M ; ESSIG, D. A ; HOOD, D. A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3149-77903611b49d6466281c2d059c3b264b84e66a9380c7d458a1523e3abd9c61073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>5-Aminolevulinate Synthetase - genetics</topic><topic>5-Aminolevulinate Synthetase - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Electric Stimulation</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Male</topic><topic>Muscle Contraction - physiology</topic><topic>Muscles - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>RNA, Messenger - metabolism</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TAKAHASHI, M</creatorcontrib><creatorcontrib>MCCURDY, D. T. M</creatorcontrib><creatorcontrib>ESSIG, D. A</creatorcontrib><creatorcontrib>HOOD, D. A</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TAKAHASHI, M</au><au>MCCURDY, D. T. M</au><au>ESSIG, D. A</au><au>HOOD, D. A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>δ-aminolaevulinate synthase expression in muscle after contractions and recovery</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1993-04-01</date><risdate>1993</risdate><volume>291</volume><issue>1</issue><spage>219</spage><epage>223</epage><pages>219-223</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist.</abstract><cop>Colchester</cop><pub>Portland Press</pub><pmid>8385933</pmid><doi>10.1042/bj2910219</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 5-Aminolevulinate Synthetase - genetics 5-Aminolevulinate Synthetase - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blotting, Northern Electric Stimulation Electron Transport Complex IV - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gene Expression Male Muscle Contraction - physiology Muscles - metabolism Rats Rats, Sprague-Dawley RNA, Messenger - metabolism Transferases |
title | δ-aminolaevulinate synthase expression in muscle after contractions and recovery |
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