Endogenous CSE/Hydrogen Sulfide System Regulates the Effects of Glucocorticoids and Insulin on Muscle Protein Synthesis
Aims. Insulin and glucocorticoids play crucial roles in skeletal muscle protein turnover. Fast-twitch glycolytic fibres are more susceptible to atrophy than slow-twitch oxidative fibres. Based on accumulating evidence, hydrogen sulfide (H2S) is a physiological mediator of this process. The regulator...
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| creator | Lin, Hai Wang, Xiaojuan Jiao, Hongchao Wang, Hui Li, Kelin Wang, Ruxia Zhao, Jingpeng |
| description | Aims. Insulin and glucocorticoids play crucial roles in skeletal muscle protein turnover. Fast-twitch glycolytic fibres are more susceptible to atrophy than slow-twitch oxidative fibres. Based on accumulating evidence, hydrogen sulfide (H2S) is a physiological mediator of this process. The regulatory effect of H2S on protein synthesis in fast-twitch fibres was evaluated. Results. A NaHS (sodium hydrosulfide) injection simultaneously increased the diameter of M. pectoralis major (i.e., fast-twitch glycolytic fibres) and activated the mammalian target of the rapamycin (mTOR)/p70S6 kinase (p70S6K) pathway. Dexamethasone (DEX) inhibited protein synthesis, downregulated mTOR and p70S6K phosphorylation, and suppressed the expression of the cystathionine γ-lyase (CSE) protein in myoblasts. The precursor of H2S, L-cysteine, completely abolished the inhibitory effects of DEX. The CSE inhibitor DL-propargylglycine (PAG) completely abrogated the effects of RU486 on blocking the suppressive effects of DEX. The H2S donor NaHS increased the H2S concentrations and abrogated the inhibitory effects of DEX on protein synthesis. Insulin increased protein synthesis and upregulated CSE expression. However, PAG abrogated the stimulatory effects of insulin on protein synthesis and the activity of the mTOR/p70S6K pathway. Innovation. These results demonstrated that CSE/H2S regulated protein synthesis in fast-twitch muscle fibres, and glucocorticoids and insulin regulated protein synthesis in an endogenous CSE/H2S system-dependent manner. Conclusions. The results from the present study suggest that the endogenous CSE/H2S system regulates fast-twitch glycolytic muscle degeneration and regeneration. |
| doi_str_mv | 10.1155/2019/9752698 |
| format | Article |
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Insulin and glucocorticoids play crucial roles in skeletal muscle protein turnover. Fast-twitch glycolytic fibres are more susceptible to atrophy than slow-twitch oxidative fibres. Based on accumulating evidence, hydrogen sulfide (H2S) is a physiological mediator of this process. The regulatory effect of H2S on protein synthesis in fast-twitch fibres was evaluated. Results. A NaHS (sodium hydrosulfide) injection simultaneously increased the diameter of M. pectoralis major (i.e., fast-twitch glycolytic fibres) and activated the mammalian target of the rapamycin (mTOR)/p70S6 kinase (p70S6K) pathway. Dexamethasone (DEX) inhibited protein synthesis, downregulated mTOR and p70S6K phosphorylation, and suppressed the expression of the cystathionine γ-lyase (CSE) protein in myoblasts. The precursor of H2S, L-cysteine, completely abolished the inhibitory effects of DEX. The CSE inhibitor DL-propargylglycine (PAG) completely abrogated the effects of RU486 on blocking the suppressive effects of DEX. The H2S donor NaHS increased the H2S concentrations and abrogated the inhibitory effects of DEX on protein synthesis. Insulin increased protein synthesis and upregulated CSE expression. However, PAG abrogated the stimulatory effects of insulin on protein synthesis and the activity of the mTOR/p70S6K pathway. Innovation. These results demonstrated that CSE/H2S regulated protein synthesis in fast-twitch muscle fibres, and glucocorticoids and insulin regulated protein synthesis in an endogenous CSE/H2S system-dependent manner. Conclusions. The results from the present study suggest that the endogenous CSE/H2S system regulates fast-twitch glycolytic muscle degeneration and regeneration.</description><identifier>ISSN: 1942-0900</identifier><identifier>EISSN: 1942-0994</identifier><identifier>DOI: 10.1155/2019/9752698</identifier><identifier>PMID: 31089421</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Adipocytes ; Alkynes - pharmacology ; Amino acids ; Animals ; Atrophy ; Cell growth ; Chickens ; Cystathionine gamma-Lyase - metabolism ; Cysteine - pharmacology ; Dexamethasone - pharmacology ; Endocrinology ; Gene expression ; Glucocorticoids - pharmacology ; Glucose ; Glycine - analogs & derivatives ; Glycine - pharmacology ; Homocysteine ; Hydrogen ; Hydrogen Sulfide - metabolism ; Injections, Intraperitoneal ; Insulin - pharmacology ; Insulin resistance ; Kinases ; Medical research ; Metabolism ; Mifepristone - pharmacology ; Muscle Proteins - biosynthesis ; Musculoskeletal system ; Myoblasts - drug effects ; Myoblasts - metabolism ; Nutrition research ; Phosphorylation ; Phosphorylation - drug effects ; Physiology ; Protein Biosynthesis - drug effects ; Protein synthesis ; Proteins ; Receptors, Glucocorticoid - metabolism ; Ribosomal Protein S6 Kinases, 70-kDa - metabolism ; Sarcopenia ; Signal Transduction - drug effects ; Sulfur ; TOR Serine-Threonine Kinases - metabolism</subject><ispartof>Oxidative medicine and cellular longevity, 2019-01, Vol.2019 (2019), p.1-15</ispartof><rights>Copyright © 2019 Ruxia Wang et al.</rights><rights>Copyright © 2019 Ruxia Wang et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. http://creativecommons.org/licenses/by/4.0</rights><rights>Copyright © 2019 Ruxia Wang et al. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-d1e3727267e655cdcebbed874a9ffcff10ca8ea4aed902a7afd00c14bbc428773</citedby><cites>FETCH-LOGICAL-c401t-d1e3727267e655cdcebbed874a9ffcff10ca8ea4aed902a7afd00c14bbc428773</cites><orcidid>0000-0002-0878-137X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6476024/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6476024/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31089421$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Abdel-Daim, Mohamed M.</contributor><contributor>Mohamed M Abdel-Daim</contributor><creatorcontrib>Lin, Hai</creatorcontrib><creatorcontrib>Wang, Xiaojuan</creatorcontrib><creatorcontrib>Jiao, Hongchao</creatorcontrib><creatorcontrib>Wang, Hui</creatorcontrib><creatorcontrib>Li, Kelin</creatorcontrib><creatorcontrib>Wang, Ruxia</creatorcontrib><creatorcontrib>Zhao, Jingpeng</creatorcontrib><title>Endogenous CSE/Hydrogen Sulfide System Regulates the Effects of Glucocorticoids and Insulin on Muscle Protein Synthesis</title><title>Oxidative medicine and cellular longevity</title><addtitle>Oxid Med Cell Longev</addtitle><description>Aims. Insulin and glucocorticoids play crucial roles in skeletal muscle protein turnover. Fast-twitch glycolytic fibres are more susceptible to atrophy than slow-twitch oxidative fibres. Based on accumulating evidence, hydrogen sulfide (H2S) is a physiological mediator of this process. The regulatory effect of H2S on protein synthesis in fast-twitch fibres was evaluated. Results. A NaHS (sodium hydrosulfide) injection simultaneously increased the diameter of M. pectoralis major (i.e., fast-twitch glycolytic fibres) and activated the mammalian target of the rapamycin (mTOR)/p70S6 kinase (p70S6K) pathway. Dexamethasone (DEX) inhibited protein synthesis, downregulated mTOR and p70S6K phosphorylation, and suppressed the expression of the cystathionine γ-lyase (CSE) protein in myoblasts. The precursor of H2S, L-cysteine, completely abolished the inhibitory effects of DEX. The CSE inhibitor DL-propargylglycine (PAG) completely abrogated the effects of RU486 on blocking the suppressive effects of DEX. The H2S donor NaHS increased the H2S concentrations and abrogated the inhibitory effects of DEX on protein synthesis. Insulin increased protein synthesis and upregulated CSE expression. However, PAG abrogated the stimulatory effects of insulin on protein synthesis and the activity of the mTOR/p70S6K pathway. Innovation. These results demonstrated that CSE/H2S regulated protein synthesis in fast-twitch muscle fibres, and glucocorticoids and insulin regulated protein synthesis in an endogenous CSE/H2S system-dependent manner. Conclusions. The results from the present study suggest that the endogenous CSE/H2S system regulates fast-twitch glycolytic muscle degeneration and regeneration.</description><subject>Adipocytes</subject><subject>Alkynes - pharmacology</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Atrophy</subject><subject>Cell growth</subject><subject>Chickens</subject><subject>Cystathionine gamma-Lyase - metabolism</subject><subject>Cysteine - pharmacology</subject><subject>Dexamethasone - pharmacology</subject><subject>Endocrinology</subject><subject>Gene expression</subject><subject>Glucocorticoids - pharmacology</subject><subject>Glucose</subject><subject>Glycine - analogs & derivatives</subject><subject>Glycine - pharmacology</subject><subject>Homocysteine</subject><subject>Hydrogen</subject><subject>Hydrogen Sulfide - metabolism</subject><subject>Injections, Intraperitoneal</subject><subject>Insulin - pharmacology</subject><subject>Insulin resistance</subject><subject>Kinases</subject><subject>Medical research</subject><subject>Metabolism</subject><subject>Mifepristone - pharmacology</subject><subject>Muscle Proteins - biosynthesis</subject><subject>Musculoskeletal system</subject><subject>Myoblasts - drug effects</subject><subject>Myoblasts - metabolism</subject><subject>Nutrition research</subject><subject>Phosphorylation</subject><subject>Phosphorylation - drug effects</subject><subject>Physiology</subject><subject>Protein Biosynthesis - drug effects</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>Receptors, Glucocorticoid - metabolism</subject><subject>Ribosomal Protein S6 Kinases, 70-kDa - metabolism</subject><subject>Sarcopenia</subject><subject>Signal Transduction - drug effects</subject><subject>Sulfur</subject><subject>TOR Serine-Threonine Kinases - metabolism</subject><issn>1942-0900</issn><issn>1942-0994</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkctvEzEQxi0Eog-4cUaWONIQ2-td716QUBTaSkUgAmfLa48TVxu7-EGV_x5HCQFunOb1m29G-hB6Rck7Stt2zggd5oNoWTf0T9A5HTibkWHgT085IWfoIqV7QrqGcfocnTWU9HVGz9Hj0puwBh9KwovVcn6zM3Ff41WZrDOAV7uUYYu_wrpMKkPCeQN4aS3onHCw-HoqOugQs9PBmYSVN_jWpzI5j4PHn0rSE-AvMWSondXO1_3k0gv0zKopwctjvETfPy6_LW5md5-vbxcf7maaE5pnhkIjmGCdgK5ttdEwjmB6wdVgrbaWEq16UFyBGQhTQllDiKZ8HDVnvRDNJXp_0H0o4xbqvs9RTfIhuq2KOxmUk_9OvNvIdfgpOy46wngVeHMUiOFHgZTlfSjR158lY5RVrOlZpa4OlI4hpQj2dIESubdJ7m2SR5sq_vrvr07wb18q8PYAbJw36tH9pxxUBqz6QzPSdU3b_AKZTaet</recordid><startdate>20190101</startdate><enddate>20190101</enddate><creator>Lin, Hai</creator><creator>Wang, Xiaojuan</creator><creator>Jiao, Hongchao</creator><creator>Wang, Hui</creator><creator>Li, Kelin</creator><creator>Wang, Ruxia</creator><creator>Zhao, Jingpeng</creator><general>Hindawi Publishing Corporation</general><general>Hindawi</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0878-137X</orcidid></search><sort><creationdate>20190101</creationdate><title>Endogenous CSE/Hydrogen Sulfide System Regulates the Effects of Glucocorticoids and Insulin on Muscle Protein Synthesis</title><author>Lin, Hai ; Wang, Xiaojuan ; Jiao, Hongchao ; Wang, Hui ; Li, Kelin ; Wang, Ruxia ; Zhao, Jingpeng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-d1e3727267e655cdcebbed874a9ffcff10ca8ea4aed902a7afd00c14bbc428773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Adipocytes</topic><topic>Alkynes - pharmacology</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Atrophy</topic><topic>Cell growth</topic><topic>Chickens</topic><topic>Cystathionine gamma-Lyase - metabolism</topic><topic>Cysteine - pharmacology</topic><topic>Dexamethasone - pharmacology</topic><topic>Endocrinology</topic><topic>Gene expression</topic><topic>Glucocorticoids - pharmacology</topic><topic>Glucose</topic><topic>Glycine - analogs & derivatives</topic><topic>Glycine - pharmacology</topic><topic>Homocysteine</topic><topic>Hydrogen</topic><topic>Hydrogen Sulfide - metabolism</topic><topic>Injections, Intraperitoneal</topic><topic>Insulin - pharmacology</topic><topic>Insulin resistance</topic><topic>Kinases</topic><topic>Medical research</topic><topic>Metabolism</topic><topic>Mifepristone - pharmacology</topic><topic>Muscle Proteins - biosynthesis</topic><topic>Musculoskeletal system</topic><topic>Myoblasts - drug effects</topic><topic>Myoblasts - metabolism</topic><topic>Nutrition research</topic><topic>Phosphorylation</topic><topic>Phosphorylation - drug effects</topic><topic>Physiology</topic><topic>Protein Biosynthesis - drug effects</topic><topic>Protein synthesis</topic><topic>Proteins</topic><topic>Receptors, Glucocorticoid - metabolism</topic><topic>Ribosomal Protein S6 Kinases, 70-kDa - metabolism</topic><topic>Sarcopenia</topic><topic>Signal Transduction - drug effects</topic><topic>Sulfur</topic><topic>TOR Serine-Threonine Kinases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, Hai</creatorcontrib><creatorcontrib>Wang, Xiaojuan</creatorcontrib><creatorcontrib>Jiao, Hongchao</creatorcontrib><creatorcontrib>Wang, Hui</creatorcontrib><creatorcontrib>Li, Kelin</creatorcontrib><creatorcontrib>Wang, Ruxia</creatorcontrib><creatorcontrib>Zhao, Jingpeng</creatorcontrib><collection>الدوريات العلمية والإحصائية - e-Marefa Academic and Statistical Periodicals</collection><collection>معرفة - المحتوى العربي الأكاديمي المتكامل - e-Marefa Academic Complete</collection><collection>Hindawi Publishing Complete</collection><collection>Hindawi Publishing Subscription Journals</collection><collection>Hindawi Publishing 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>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oxidative medicine and cellular longevity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lin, Hai</au><au>Wang, Xiaojuan</au><au>Jiao, Hongchao</au><au>Wang, Hui</au><au>Li, Kelin</au><au>Wang, Ruxia</au><au>Zhao, Jingpeng</au><au>Abdel-Daim, Mohamed M.</au><au>Mohamed M Abdel-Daim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endogenous CSE/Hydrogen Sulfide System Regulates the Effects of Glucocorticoids and Insulin on Muscle Protein Synthesis</atitle><jtitle>Oxidative medicine and cellular longevity</jtitle><addtitle>Oxid Med Cell Longev</addtitle><date>2019-01-01</date><risdate>2019</risdate><volume>2019</volume><issue>2019</issue><spage>1</spage><epage>15</epage><pages>1-15</pages><issn>1942-0900</issn><eissn>1942-0994</eissn><abstract>Aims. Insulin and glucocorticoids play crucial roles in skeletal muscle protein turnover. Fast-twitch glycolytic fibres are more susceptible to atrophy than slow-twitch oxidative fibres. Based on accumulating evidence, hydrogen sulfide (H2S) is a physiological mediator of this process. The regulatory effect of H2S on protein synthesis in fast-twitch fibres was evaluated. Results. A NaHS (sodium hydrosulfide) injection simultaneously increased the diameter of M. pectoralis major (i.e., fast-twitch glycolytic fibres) and activated the mammalian target of the rapamycin (mTOR)/p70S6 kinase (p70S6K) pathway. Dexamethasone (DEX) inhibited protein synthesis, downregulated mTOR and p70S6K phosphorylation, and suppressed the expression of the cystathionine γ-lyase (CSE) protein in myoblasts. The precursor of H2S, L-cysteine, completely abolished the inhibitory effects of DEX. The CSE inhibitor DL-propargylglycine (PAG) completely abrogated the effects of RU486 on blocking the suppressive effects of DEX. The H2S donor NaHS increased the H2S concentrations and abrogated the inhibitory effects of DEX on protein synthesis. Insulin increased protein synthesis and upregulated CSE expression. However, PAG abrogated the stimulatory effects of insulin on protein synthesis and the activity of the mTOR/p70S6K pathway. Innovation. These results demonstrated that CSE/H2S regulated protein synthesis in fast-twitch muscle fibres, and glucocorticoids and insulin regulated protein synthesis in an endogenous CSE/H2S system-dependent manner. Conclusions. The results from the present study suggest that the endogenous CSE/H2S system regulates fast-twitch glycolytic muscle degeneration and regeneration.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>31089421</pmid><doi>10.1155/2019/9752698</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-0878-137X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adipocytes Alkynes - pharmacology Amino acids Animals Atrophy Cell growth Chickens Cystathionine gamma-Lyase - metabolism Cysteine - pharmacology Dexamethasone - pharmacology Endocrinology Gene expression Glucocorticoids - pharmacology Glucose Glycine - analogs & derivatives Glycine - pharmacology Homocysteine Hydrogen Hydrogen Sulfide - metabolism Injections, Intraperitoneal Insulin - pharmacology Insulin resistance Kinases Medical research Metabolism Mifepristone - pharmacology Muscle Proteins - biosynthesis Musculoskeletal system Myoblasts - drug effects Myoblasts - metabolism Nutrition research Phosphorylation Phosphorylation - drug effects Physiology Protein Biosynthesis - drug effects Protein synthesis Proteins Receptors, Glucocorticoid - metabolism Ribosomal Protein S6 Kinases, 70-kDa - metabolism Sarcopenia Signal Transduction - drug effects Sulfur TOR Serine-Threonine Kinases - metabolism |
| title | Endogenous CSE/Hydrogen Sulfide System Regulates the Effects of Glucocorticoids and Insulin on Muscle Protein Synthesis |
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