Human adenovirus 36 decreases fatty acid oxidation and increases de novo lipogenesis in primary cultured human skeletal muscle cells by promoting Cidec/FSP27 expression

Background: It has been well documented that human adenovirus type 36 (Ad-36) is associated with obesity. However, the underlying molecular mechanism of Ad-36 inducing obesity remains unknown. We sought to investigate the effect of Ad-36 infection on Cidec, AMPK pathway and lipid metabolism in prima...

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Veröffentlicht in:International Journal of Obesity 2010-09, Vol.34 (9), p.1355-1364
Hauptverfasser: Wang, Z.Q, Yu, Y, Zhang, X.H, Floyd, E.Z, Cefalu, W.T
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Yu, Y
Zhang, X.H
Floyd, E.Z
Cefalu, W.T
description Background: It has been well documented that human adenovirus type 36 (Ad-36) is associated with obesity. However, the underlying molecular mechanism of Ad-36 inducing obesity remains unknown. We sought to investigate the effect of Ad-36 infection on Cidec, AMPK pathway and lipid metabolism in primary cultured human skeletal muscle cells. Methods: Cidec/fat-specific protein 27 (FSP27), fatty acid oxidation, AMPK signaling and the abundance of proteins involved in lipid synthesis were determined in muscle cells infected with various doses (1.9–7.6 MOI) of Ad-36 and non-lipogenic adenovirus type 2 (Ad-2) as a negative control as well as an uninfected control. Cidec/FSP27 siRNA transfection was performed in Ad-36-infected muscle cells. Results: Our data show that Ad-36 significantly reduced fatty acid oxidation in a dose-dependent manner (all P values are
doi_str_mv 10.1038/ijo.2010.77
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However, the underlying molecular mechanism of Ad-36 inducing obesity remains unknown. We sought to investigate the effect of Ad-36 infection on Cidec, AMPK pathway and lipid metabolism in primary cultured human skeletal muscle cells. Methods: Cidec/fat-specific protein 27 (FSP27), fatty acid oxidation, AMPK signaling and the abundance of proteins involved in lipid synthesis were determined in muscle cells infected with various doses (1.9–7.6 MOI) of Ad-36 and non-lipogenic adenovirus type 2 (Ad-2) as a negative control as well as an uninfected control. Cidec/FSP27 siRNA transfection was performed in Ad-36-infected muscle cells. Results: Our data show that Ad-36 significantly reduced fatty acid oxidation in a dose-dependent manner (all P values are &lt;0.01), but Ad-2 did not affect fatty acid oxidation. Ad-36 substantially increased Cidec/FSP27, ACC, sterol regulatory element-binding protein 1c (SREBP-1c), SREBP-2 and 3-hydroxy-3-methylglutaryl-CoA reductase protein abundance, but significantly reduced AMPK activity, mitochondrial mass and uncoupling protein 3 (UCP3) abundance in comparison with control cells (all P values are &lt;0.01). Oil Red O staining revealed that there was substantial fat accumulation in the Ad-36-infected muscle cells. Furthermore, Cidec/FSP27 siRNA transfection significantly reduced FSP27 expression and partially restored AMPK signaling, increased UCP3 and decreased SERBP 1c and perilipin proteins in Ad-36-infected muscle cells. Interestingly, neither Ad-36 nor Ad-2 affected peroxisome proliferator-activated receptor γ protein expression in muscle cells. Conclusion: This study suggests that Ad-36 induced lipid droplets in the cultured skeletal muscle cells and this process may be mediated by promoting Cidec/FSP27 expression.</description><identifier>ISSN: 0307-0565</identifier><identifier>EISSN: 1476-5497</identifier><identifier>DOI: 10.1038/ijo.2010.77</identifier><identifier>PMID: 20440297</identifier><identifier>CODEN: IJOBDP</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/443/319/2723 ; 631/80/86 ; 692/698/1671/1668/1973 ; 692/699/255/2514 ; Adenovirus diseases ; Adenoviruses ; Adenoviruses, Human - genetics ; Adenoviruses, Human - metabolism ; Adipocytes ; Biological and medical sciences ; Biological oxidation (Metabolism) ; Biomedical research ; Body fat ; cell culture ; Cells, Cultured ; Complications and side effects ; de novo lipogenesis ; Epidemiology ; fatty acid composition ; Fatty acids ; Fatty Acids - genetics ; Fatty Acids - metabolism ; Genetic aspects ; Glucose ; Health aspects ; Health Promotion and Disease Prevention ; Human adenovirus D ; human cell lines ; Humans ; Insulin resistance ; Internal Medicine ; Lipid Metabolism ; lipid peroxidation ; Lipids ; lipogenesis ; Lipogenesis - genetics ; Lipogenesis - physiology ; Medical sciences ; Medicine ; Medicine &amp; Public Health ; Metabolic Diseases ; Metabolism ; Muscle cells ; Muscle, Skeletal - metabolism ; Muscle, Skeletal - virology ; Musculoskeletal system ; Obesity ; Obesity - genetics ; Obesity - metabolism ; Obesity - virology ; original-article ; Oxidation ; Oxidation-Reduction ; Physiological aspects ; Protein expression ; protein synthesis ; Proteins ; Proteins - genetics ; Proteins - metabolism ; Public Health ; Risk factors ; Signal Transduction ; skeletal muscle ; Triglycerides</subject><ispartof>International Journal of Obesity, 2010-09, Vol.34 (9), p.1355-1364</ispartof><rights>Macmillan Publishers Limited 2010</rights><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2010 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Sep 2010</rights><rights>2010 Macmillan Publishers Limited All rights reserved 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c596t-5bbbdf28b466dbbd9d8c4d88a52d75db73d45cd15ef249daeeda67686e5828ce3</citedby><cites>FETCH-LOGICAL-c596t-5bbbdf28b466dbbd9d8c4d88a52d75db73d45cd15ef249daeeda67686e5828ce3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ijo.2010.77$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ijo.2010.77$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=23234444$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20440297$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Z.Q</creatorcontrib><creatorcontrib>Yu, Y</creatorcontrib><creatorcontrib>Zhang, X.H</creatorcontrib><creatorcontrib>Floyd, E.Z</creatorcontrib><creatorcontrib>Cefalu, W.T</creatorcontrib><title>Human adenovirus 36 decreases fatty acid oxidation and increases de novo lipogenesis in primary cultured human skeletal muscle cells by promoting Cidec/FSP27 expression</title><title>International Journal of Obesity</title><addtitle>Int J Obes</addtitle><addtitle>Int J Obes (Lond)</addtitle><description>Background: It has been well documented that human adenovirus type 36 (Ad-36) is associated with obesity. However, the underlying molecular mechanism of Ad-36 inducing obesity remains unknown. We sought to investigate the effect of Ad-36 infection on Cidec, AMPK pathway and lipid metabolism in primary cultured human skeletal muscle cells. Methods: Cidec/fat-specific protein 27 (FSP27), fatty acid oxidation, AMPK signaling and the abundance of proteins involved in lipid synthesis were determined in muscle cells infected with various doses (1.9–7.6 MOI) of Ad-36 and non-lipogenic adenovirus type 2 (Ad-2) as a negative control as well as an uninfected control. Cidec/FSP27 siRNA transfection was performed in Ad-36-infected muscle cells. Results: Our data show that Ad-36 significantly reduced fatty acid oxidation in a dose-dependent manner (all P values are &lt;0.01), but Ad-2 did not affect fatty acid oxidation. Ad-36 substantially increased Cidec/FSP27, ACC, sterol regulatory element-binding protein 1c (SREBP-1c), SREBP-2 and 3-hydroxy-3-methylglutaryl-CoA reductase protein abundance, but significantly reduced AMPK activity, mitochondrial mass and uncoupling protein 3 (UCP3) abundance in comparison with control cells (all P values are &lt;0.01). Oil Red O staining revealed that there was substantial fat accumulation in the Ad-36-infected muscle cells. Furthermore, Cidec/FSP27 siRNA transfection significantly reduced FSP27 expression and partially restored AMPK signaling, increased UCP3 and decreased SERBP 1c and perilipin proteins in Ad-36-infected muscle cells. Interestingly, neither Ad-36 nor Ad-2 affected peroxisome proliferator-activated receptor γ protein expression in muscle cells. 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Public Health</subject><subject>Metabolic Diseases</subject><subject>Metabolism</subject><subject>Muscle cells</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Muscle, Skeletal - virology</subject><subject>Musculoskeletal system</subject><subject>Obesity</subject><subject>Obesity - genetics</subject><subject>Obesity - metabolism</subject><subject>Obesity - virology</subject><subject>original-article</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Physiological aspects</subject><subject>Protein expression</subject><subject>protein synthesis</subject><subject>Proteins</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Public Health</subject><subject>Risk factors</subject><subject>Signal Transduction</subject><subject>skeletal muscle</subject><subject>Triglycerides</subject><issn>0307-0565</issn><issn>1476-5497</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkk1v1DAQhiMEoqVw4g4WCDjAbh1_xMkFqVpRilQJpNKz5diTXS-OvdhJ1f1H_Ey87PZjUeNDbM8z76sZT1G8LPG0xLQ-tsswJTifhHhUHJZMVBPOGvG4OMQUiwnmFT8onqW0xBhzjsnT4oBgxjBpxGHx52zslUfKgA9XNo4J0QoZ0BFUgoQ6NQxrpLQ1KFxbowYbMuwNsv4GMYByakDOrsIcPCSbchStou1VXCM9umGMYNDin1H6BQ4G5VA_Ju0AaXAuoXad-dCHwfo5mtnsf3x68YMIBNerCCll1-fFk065BC92_6Pi8vTLz9nZ5Pz712-zk_OJ5k01THjbtqYjdcuqyuRtY2rNTF0rTozgphXUMK5NyaEjrDEKwKhKVHUFvCa1BnpUfN7qrsa2B6PBD1E5uStHBmXlfsTbhZyHK0mbitS0yQIfdgIx_B4hDbK3aVOm8hDGJAVnGBPGRCbf_Ecuwxh9ri5DmJa4ESxDb7fQXDmQ1nchu-qNpDwhtMYNo7zM1PQBKi8DvdXBQ2fz_V7C-3sJC1BuWKTgxs0Dp33w4xbUMaQUobttRYnlZv5knj-5mT8pNiW9ut-9W_Zm4DLwbgeopJXrovLapjuOEsryl7lPWy7lkJ9DvOvNw76vt3inglTzmCUvL3KQ4rIhuKlq-hd_tv2h</recordid><startdate>20100901</startdate><enddate>20100901</enddate><creator>Wang, Z.Q</creator><creator>Yu, Y</creator><creator>Zhang, X.H</creator><creator>Floyd, E.Z</creator><creator>Cefalu, W.T</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>FBQ</scope><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>3V.</scope><scope>7T2</scope><scope>7TK</scope><scope>7TS</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100901</creationdate><title>Human adenovirus 36 decreases fatty acid oxidation and increases de novo lipogenesis in primary cultured human skeletal muscle cells by promoting Cidec/FSP27 expression</title><author>Wang, Z.Q ; Yu, Y ; Zhang, X.H ; Floyd, E.Z ; Cefalu, W.T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c596t-5bbbdf28b466dbbd9d8c4d88a52d75db73d45cd15ef249daeeda67686e5828ce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>631/443/319/2723</topic><topic>631/80/86</topic><topic>692/698/1671/1668/1973</topic><topic>692/699/255/2514</topic><topic>Adenovirus diseases</topic><topic>Adenoviruses</topic><topic>Adenoviruses, Human - genetics</topic><topic>Adenoviruses, Human - metabolism</topic><topic>Adipocytes</topic><topic>Biological and medical sciences</topic><topic>Biological oxidation (Metabolism)</topic><topic>Biomedical research</topic><topic>Body fat</topic><topic>cell culture</topic><topic>Cells, Cultured</topic><topic>Complications and side effects</topic><topic>de novo lipogenesis</topic><topic>Epidemiology</topic><topic>fatty acid composition</topic><topic>Fatty acids</topic><topic>Fatty Acids - genetics</topic><topic>Fatty Acids - metabolism</topic><topic>Genetic aspects</topic><topic>Glucose</topic><topic>Health aspects</topic><topic>Health Promotion and Disease Prevention</topic><topic>Human adenovirus D</topic><topic>human cell lines</topic><topic>Humans</topic><topic>Insulin resistance</topic><topic>Internal Medicine</topic><topic>Lipid Metabolism</topic><topic>lipid peroxidation</topic><topic>Lipids</topic><topic>lipogenesis</topic><topic>Lipogenesis - genetics</topic><topic>Lipogenesis - physiology</topic><topic>Medical sciences</topic><topic>Medicine</topic><topic>Medicine &amp; 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However, the underlying molecular mechanism of Ad-36 inducing obesity remains unknown. We sought to investigate the effect of Ad-36 infection on Cidec, AMPK pathway and lipid metabolism in primary cultured human skeletal muscle cells. Methods: Cidec/fat-specific protein 27 (FSP27), fatty acid oxidation, AMPK signaling and the abundance of proteins involved in lipid synthesis were determined in muscle cells infected with various doses (1.9–7.6 MOI) of Ad-36 and non-lipogenic adenovirus type 2 (Ad-2) as a negative control as well as an uninfected control. Cidec/FSP27 siRNA transfection was performed in Ad-36-infected muscle cells. Results: Our data show that Ad-36 significantly reduced fatty acid oxidation in a dose-dependent manner (all P values are &lt;0.01), but Ad-2 did not affect fatty acid oxidation. Ad-36 substantially increased Cidec/FSP27, ACC, sterol regulatory element-binding protein 1c (SREBP-1c), SREBP-2 and 3-hydroxy-3-methylglutaryl-CoA reductase protein abundance, but significantly reduced AMPK activity, mitochondrial mass and uncoupling protein 3 (UCP3) abundance in comparison with control cells (all P values are &lt;0.01). Oil Red O staining revealed that there was substantial fat accumulation in the Ad-36-infected muscle cells. Furthermore, Cidec/FSP27 siRNA transfection significantly reduced FSP27 expression and partially restored AMPK signaling, increased UCP3 and decreased SERBP 1c and perilipin proteins in Ad-36-infected muscle cells. Interestingly, neither Ad-36 nor Ad-2 affected peroxisome proliferator-activated receptor γ protein expression in muscle cells. Conclusion: This study suggests that Ad-36 induced lipid droplets in the cultured skeletal muscle cells and this process may be mediated by promoting Cidec/FSP27 expression.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>20440297</pmid><doi>10.1038/ijo.2010.77</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
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subjects 631/443/319/2723
631/80/86
692/698/1671/1668/1973
692/699/255/2514
Adenovirus diseases
Adenoviruses
Adenoviruses, Human - genetics
Adenoviruses, Human - metabolism
Adipocytes
Biological and medical sciences
Biological oxidation (Metabolism)
Biomedical research
Body fat
cell culture
Cells, Cultured
Complications and side effects
de novo lipogenesis
Epidemiology
fatty acid composition
Fatty acids
Fatty Acids - genetics
Fatty Acids - metabolism
Genetic aspects
Glucose
Health aspects
Health Promotion and Disease Prevention
Human adenovirus D
human cell lines
Humans
Insulin resistance
Internal Medicine
Lipid Metabolism
lipid peroxidation
Lipids
lipogenesis
Lipogenesis - genetics
Lipogenesis - physiology
Medical sciences
Medicine
Medicine & Public Health
Metabolic Diseases
Metabolism
Muscle cells
Muscle, Skeletal - metabolism
Muscle, Skeletal - virology
Musculoskeletal system
Obesity
Obesity - genetics
Obesity - metabolism
Obesity - virology
original-article
Oxidation
Oxidation-Reduction
Physiological aspects
Protein expression
protein synthesis
Proteins
Proteins - genetics
Proteins - metabolism
Public Health
Risk factors
Signal Transduction
skeletal muscle
Triglycerides
title Human adenovirus 36 decreases fatty acid oxidation and increases de novo lipogenesis in primary cultured human skeletal muscle cells by promoting Cidec/FSP27 expression
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T08%3A33%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Human%20adenovirus%2036%20decreases%20fatty%20acid%20oxidation%20and%20increases%20de%20novo%20lipogenesis%20in%20primary%20cultured%20human%20skeletal%20muscle%20cells%20by%20promoting%20Cidec/FSP27%20expression&rft.jtitle=International%20Journal%20of%20Obesity&rft.au=Wang,%20Z.Q&rft.date=2010-09-01&rft.volume=34&rft.issue=9&rft.spage=1355&rft.epage=1364&rft.pages=1355-1364&rft.issn=0307-0565&rft.eissn=1476-5497&rft.coden=IJOBDP&rft_id=info:doi/10.1038/ijo.2010.77&rft_dat=%3Cgale_pubme%3EA238094351%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=750310974&rft_id=info:pmid/20440297&rft_galeid=A238094351&rfr_iscdi=true