Topiramate effects lipolysis in 3T3-L1 adipocytes
Studies have shown that topiramate (TPM)-induced weight loss can be dependent on the central nervous system (CNS). However, the direct action of TPM on adipose tissue has not been tested previously. Thus, the present study aimed to examine whether TPM modulates lipolysis in 3T3-L1. The 3T3-L1 cells...
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creator | MARTINS, GABRIELA POLTRONIERI CAMPAGNARO SOUZA, CAMILA OLIVEIRA MARQUES, SCHEROLIN LUCIANO, THAIS FERNANDES DA SILVA PIERI, BRUNO LUIZ ROSA, JOSÉ CÉSAR DA SILVA, ADELINO SANCHEZ RAMOS PAULI, JOSÉ RODRIGO CINTRA, DENNYS ESPER ROPELLE, EDUARDO ROCHETE RODRIGUES, BRUNO DE LIRA, FABIO SANTOS DE SOUZA, CLAUDIO TEODORO |
description | Studies have shown that topiramate (TPM)-induced weight loss can be dependent on the central nervous system (CNS). However, the direct action of TPM on adipose tissue has not been tested previously. Thus, the present study aimed to examine whether TPM modulates lipolysis in 3T3-L1. The 3T3-L1 cells were incubated in 50 µM TPM for 30 min. The β-adrenergic stimulator, isoproterenol, was used as a positive control. The release of lactate dehydrogenase, non-esterified fatty acid, glycerol and incorporation of 14C-palmitate to lipid were analyzed. The phosphorylation of protein kinase A (PKA), hormone-sensitive lipase (HSL), adipocyte triglyceride lipase (ATGL) and perilipin A, as well as the protein levels of comparative genetic identification 58 (CGI-58) were assessed. The levels of glycerol and non-esterified fatty acid increased markedly when the cells were treated with TPM. The TPM effects were similar to the isoproterenol positive control. Additionally, TPM reduced lipogenesis. These results were observed without any change in cell viability. Finally, the phosphorylation of PKA, HSL, ATGL and perilipin A, as well as the protein levels of CGI-58 were increased compared to the control cells. These results were similar to those observed in the cells treated with isoproterenol. The present results show that TPM increased the phosphorylation of pivotal lipolytic enzymes, which induced lipolysis in 3T3-L1 adipocytes, suggesting that this drug may act directly in the adipose tissue independent from its effect on the CNS. |
doi_str_mv | 10.3892/br.2015.514 |
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However, the direct action of TPM on adipose tissue has not been tested previously. Thus, the present study aimed to examine whether TPM modulates lipolysis in 3T3-L1. The 3T3-L1 cells were incubated in 50 µM TPM for 30 min. The β-adrenergic stimulator, isoproterenol, was used as a positive control. The release of lactate dehydrogenase, non-esterified fatty acid, glycerol and incorporation of 14C-palmitate to lipid were analyzed. The phosphorylation of protein kinase A (PKA), hormone-sensitive lipase (HSL), adipocyte triglyceride lipase (ATGL) and perilipin A, as well as the protein levels of comparative genetic identification 58 (CGI-58) were assessed. The levels of glycerol and non-esterified fatty acid increased markedly when the cells were treated with TPM. The TPM effects were similar to the isoproterenol positive control. Additionally, TPM reduced lipogenesis. These results were observed without any change in cell viability. Finally, the phosphorylation of PKA, HSL, ATGL and perilipin A, as well as the protein levels of CGI-58 were increased compared to the control cells. These results were similar to those observed in the cells treated with isoproterenol. The present results show that TPM increased the phosphorylation of pivotal lipolytic enzymes, which induced lipolysis in 3T3-L1 adipocytes, suggesting that this drug may act directly in the adipose tissue independent from its effect on the CNS.</description><identifier>ISSN: 2049-9434</identifier><identifier>EISSN: 2049-9442</identifier><identifier>DOI: 10.3892/br.2015.514</identifier><identifier>PMID: 26623024</identifier><language>eng</language><publisher>England: D.A. Spandidos</publisher><subject>3T3-L1 adipocytes ; Adipocytes ; Adipose tissue ; Central nervous system ; Enzymes ; Esterification ; Fat cells ; Fatty acids ; Fluorides ; Glycerol ; Immunoglobulins ; Insulin ; Isoproterenol ; Kinases ; L-Lactate dehydrogenase ; Lactate dehydrogenase ; Lactic acid ; Lipase ; Lipids ; Lipogenesis ; Lipolysis ; Membranes ; Obesity ; Palmitic acid ; Phosphorylation ; Physiological aspects ; Protein kinase A ; Proteins ; Rodents ; Software ; Topiramate ; Weight control ; Weight loss</subject><ispartof>Biomedical reports, 2015-11, Vol.3 (6), p.827-830</ispartof><rights>Copyright © 2015, Spandidos Publications</rights><rights>COPYRIGHT 2015 Spandidos Publications</rights><rights>Copyright Spandidos Publications UK Ltd. 2015</rights><rights>Copyright © 2015, Spandidos Publications 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-d5f252c16a03f0abc6f2e65b96487346e379d73fb934c6d9edfeb0dab64021fd3</citedby><cites>FETCH-LOGICAL-c500t-d5f252c16a03f0abc6f2e65b96487346e379d73fb934c6d9edfeb0dab64021fd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660592/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660592/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,5556,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26623024$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MARTINS, GABRIELA POLTRONIERI CAMPAGNARO</creatorcontrib><creatorcontrib>SOUZA, CAMILA OLIVEIRA</creatorcontrib><creatorcontrib>MARQUES, SCHEROLIN</creatorcontrib><creatorcontrib>LUCIANO, THAIS FERNANDES</creatorcontrib><creatorcontrib>DA SILVA PIERI, BRUNO LUIZ</creatorcontrib><creatorcontrib>ROSA, JOSÉ CÉSAR</creatorcontrib><creatorcontrib>DA SILVA, ADELINO SANCHEZ RAMOS</creatorcontrib><creatorcontrib>PAULI, JOSÉ RODRIGO</creatorcontrib><creatorcontrib>CINTRA, DENNYS ESPER</creatorcontrib><creatorcontrib>ROPELLE, EDUARDO ROCHETE</creatorcontrib><creatorcontrib>RODRIGUES, BRUNO</creatorcontrib><creatorcontrib>DE LIRA, FABIO SANTOS</creatorcontrib><creatorcontrib>DE SOUZA, CLAUDIO TEODORO</creatorcontrib><title>Topiramate effects lipolysis in 3T3-L1 adipocytes</title><title>Biomedical reports</title><addtitle>Biomed Rep</addtitle><description>Studies have shown that topiramate (TPM)-induced weight loss can be dependent on the central nervous system (CNS). However, the direct action of TPM on adipose tissue has not been tested previously. Thus, the present study aimed to examine whether TPM modulates lipolysis in 3T3-L1. The 3T3-L1 cells were incubated in 50 µM TPM for 30 min. The β-adrenergic stimulator, isoproterenol, was used as a positive control. The release of lactate dehydrogenase, non-esterified fatty acid, glycerol and incorporation of 14C-palmitate to lipid were analyzed. The phosphorylation of protein kinase A (PKA), hormone-sensitive lipase (HSL), adipocyte triglyceride lipase (ATGL) and perilipin A, as well as the protein levels of comparative genetic identification 58 (CGI-58) were assessed. The levels of glycerol and non-esterified fatty acid increased markedly when the cells were treated with TPM. The TPM effects were similar to the isoproterenol positive control. Additionally, TPM reduced lipogenesis. These results were observed without any change in cell viability. Finally, the phosphorylation of PKA, HSL, ATGL and perilipin A, as well as the protein levels of CGI-58 were increased compared to the control cells. These results were similar to those observed in the cells treated with isoproterenol. The present results show that TPM increased the phosphorylation of pivotal lipolytic enzymes, which induced lipolysis in 3T3-L1 adipocytes, suggesting that this drug may act directly in the adipose tissue independent from its effect on the CNS.</description><subject>3T3-L1 adipocytes</subject><subject>Adipocytes</subject><subject>Adipose tissue</subject><subject>Central nervous system</subject><subject>Enzymes</subject><subject>Esterification</subject><subject>Fat cells</subject><subject>Fatty acids</subject><subject>Fluorides</subject><subject>Glycerol</subject><subject>Immunoglobulins</subject><subject>Insulin</subject><subject>Isoproterenol</subject><subject>Kinases</subject><subject>L-Lactate dehydrogenase</subject><subject>Lactate dehydrogenase</subject><subject>Lactic acid</subject><subject>Lipase</subject><subject>Lipids</subject><subject>Lipogenesis</subject><subject>Lipolysis</subject><subject>Membranes</subject><subject>Obesity</subject><subject>Palmitic acid</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Protein kinase A</subject><subject>Proteins</subject><subject>Rodents</subject><subject>Software</subject><subject>Topiramate</subject><subject>Weight control</subject><subject>Weight loss</subject><issn>2049-9434</issn><issn>2049-9442</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNptkU1rGzEQhkVoSULqU-5loZdCWVffXl0CqWnSgKEQnLPQSiNXYXe1ldYB__vKJHGaEM1BYvTMK828CJ0TPGeNot_bNKeYiLkg_AidUsxVrTinHw5nxk_QLOd7XJZaYCqaY3RCpaQMU36KyDqOIZneTFCB92CnXHVhjN0uh1yFoWJrVq9IZVxJ2t0E-RP66E2XYfa0n6G7q5_r5a969fv6Znm5qq3AeKqd8FRQS6TBzGPTWukpSNEqyZsF4xLYQrkF861i3EqnwHlosTOt5JgS79gZunjUHbdtD87CMCXT6TGF3qSdjibo1zdD-KM38UFzKbFQtAh8fRJI8e8W8qT7kC10nRkgbrMmTRkDJ5KJgn55g97HbRpKe5oohhVtlFAv1MZ0oMPgY3nX7kX1JWeKMNEwUqj5O1QJB32wcQAfSv5VwbfHAptizgn8oUeC9d5k3Sa9N1kXkwv9-f-xHNhnS19-mUczuOBiPjA_bmtcYi_zD24eqtQ</recordid><startdate>20151101</startdate><enddate>20151101</enddate><creator>MARTINS, GABRIELA POLTRONIERI CAMPAGNARO</creator><creator>SOUZA, CAMILA OLIVEIRA</creator><creator>MARQUES, SCHEROLIN</creator><creator>LUCIANO, THAIS FERNANDES</creator><creator>DA SILVA PIERI, BRUNO LUIZ</creator><creator>ROSA, JOSÉ CÉSAR</creator><creator>DA SILVA, ADELINO SANCHEZ RAMOS</creator><creator>PAULI, JOSÉ RODRIGO</creator><creator>CINTRA, DENNYS ESPER</creator><creator>ROPELLE, EDUARDO ROCHETE</creator><creator>RODRIGUES, BRUNO</creator><creator>DE LIRA, FABIO SANTOS</creator><creator>DE SOUZA, CLAUDIO TEODORO</creator><general>D.A. Spandidos</general><general>Spandidos Publications</general><general>Spandidos Publications UK Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20151101</creationdate><title>Topiramate effects lipolysis in 3T3-L1 adipocytes</title><author>MARTINS, GABRIELA POLTRONIERI CAMPAGNARO ; SOUZA, CAMILA OLIVEIRA ; MARQUES, SCHEROLIN ; LUCIANO, THAIS FERNANDES ; DA SILVA PIERI, BRUNO LUIZ ; ROSA, JOSÉ CÉSAR ; DA SILVA, ADELINO SANCHEZ RAMOS ; PAULI, JOSÉ RODRIGO ; CINTRA, DENNYS ESPER ; ROPELLE, EDUARDO ROCHETE ; 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However, the direct action of TPM on adipose tissue has not been tested previously. Thus, the present study aimed to examine whether TPM modulates lipolysis in 3T3-L1. The 3T3-L1 cells were incubated in 50 µM TPM for 30 min. The β-adrenergic stimulator, isoproterenol, was used as a positive control. The release of lactate dehydrogenase, non-esterified fatty acid, glycerol and incorporation of 14C-palmitate to lipid were analyzed. The phosphorylation of protein kinase A (PKA), hormone-sensitive lipase (HSL), adipocyte triglyceride lipase (ATGL) and perilipin A, as well as the protein levels of comparative genetic identification 58 (CGI-58) were assessed. The levels of glycerol and non-esterified fatty acid increased markedly when the cells were treated with TPM. The TPM effects were similar to the isoproterenol positive control. Additionally, TPM reduced lipogenesis. These results were observed without any change in cell viability. Finally, the phosphorylation of PKA, HSL, ATGL and perilipin A, as well as the protein levels of CGI-58 were increased compared to the control cells. These results were similar to those observed in the cells treated with isoproterenol. The present results show that TPM increased the phosphorylation of pivotal lipolytic enzymes, which induced lipolysis in 3T3-L1 adipocytes, suggesting that this drug may act directly in the adipose tissue independent from its effect on the CNS.</abstract><cop>England</cop><pub>D.A. Spandidos</pub><pmid>26623024</pmid><doi>10.3892/br.2015.514</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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source | Spandidos Publications Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
subjects | 3T3-L1 adipocytes Adipocytes Adipose tissue Central nervous system Enzymes Esterification Fat cells Fatty acids Fluorides Glycerol Immunoglobulins Insulin Isoproterenol Kinases L-Lactate dehydrogenase Lactate dehydrogenase Lactic acid Lipase Lipids Lipogenesis Lipolysis Membranes Obesity Palmitic acid Phosphorylation Physiological aspects Protein kinase A Proteins Rodents Software Topiramate Weight control Weight loss |
title | Topiramate effects lipolysis in 3T3-L1 adipocytes |
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