Testosterone stimulates glucose uptake and GLUT4 translocation through LKB1/AMPK signaling in 3T3-L1 adipocytes
Decreases in serum testosterone concentrations in aging men are associated with metabolic disorders. Testosterone has been reported to increase GLUT4-dependent glucose uptake in skeletal muscle cells and cardiomyocytes. However, studies on glucose uptake occurring in response to testosterone stimula...
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| Veröffentlicht in: | Endocrine 2016-01, Vol.51 (1), p.174-184 |
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| creator | Mitsuhashi, Kazuteru Senmaru, Takafumi Fukuda, Takuya Yamazaki, Masahiro Shinomiya, Katsuhiko Ueno, Morio Kinoshita, Shigeru Kitawaki, Jo Katsuyama, Masato Tsujikawa, Muneo Obayashi, Hiroshi Nakamura, Naoto Fukui, Michiaki |
| description | Decreases in serum testosterone concentrations in aging men are associated with metabolic disorders. Testosterone has been reported to increase GLUT4-dependent glucose uptake in skeletal muscle cells and cardiomyocytes. However, studies on glucose uptake occurring in response to testosterone stimulation in adipocytes are currently not available. This study was designed to determine the effects of testosterone on glucose uptake in adipocytes. Glucose uptake was assessed with 2-[
3
H] deoxyglucose in 3T3-L1 adipocytes. GLUT4 translocation was evaluated in plasma membrane (PM) sheets and PM fractions by immunofluorescence and immunoblotting, respectively. Activation of GLUT4 translocation-related protein kinases, including Akt, AMPK, LKB1, CaMKI, CaMKII, and Cbl was followed by immunoblotting. Expression levels of androgen receptor (AR) mRNA and AR translocation to the PM were assessed by real-time RT-PCR and immunoblotting, respectively. The results showed that both high-dose (100 nM) testosterone and testosterone-BSA increased glucose uptake and GLUT4 translocation to the PM, independently of the intracellular AR. Testosterone and testosterone-BSA stimulated the phosphorylation of AMPK, LKB1, and CaMKII. The knockdown of LKB1 by siRNA attenuated testosterone- and testosterone-BSA-stimulated AMPK phosphorylation and glucose uptake. These results indicate that high-dose testosterone and testosterone-BSA increase GLUT4-dependent glucose uptake in 3T3-L1 adipocytes by inducing the LKB1/AMPK signaling pathway. |
| doi_str_mv | 10.1007/s12020-015-0666-y |
| format | Article |
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3
H] deoxyglucose in 3T3-L1 adipocytes. GLUT4 translocation was evaluated in plasma membrane (PM) sheets and PM fractions by immunofluorescence and immunoblotting, respectively. Activation of GLUT4 translocation-related protein kinases, including Akt, AMPK, LKB1, CaMKI, CaMKII, and Cbl was followed by immunoblotting. Expression levels of androgen receptor (AR) mRNA and AR translocation to the PM were assessed by real-time RT-PCR and immunoblotting, respectively. The results showed that both high-dose (100 nM) testosterone and testosterone-BSA increased glucose uptake and GLUT4 translocation to the PM, independently of the intracellular AR. Testosterone and testosterone-BSA stimulated the phosphorylation of AMPK, LKB1, and CaMKII. The knockdown of LKB1 by siRNA attenuated testosterone- and testosterone-BSA-stimulated AMPK phosphorylation and glucose uptake. These results indicate that high-dose testosterone and testosterone-BSA increase GLUT4-dependent glucose uptake in 3T3-L1 adipocytes by inducing the LKB1/AMPK signaling pathway.</description><identifier>ISSN: 1355-008X</identifier><identifier>EISSN: 1559-0100</identifier><identifier>DOI: 10.1007/s12020-015-0666-y</identifier><identifier>PMID: 26100787</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>3T3-L1 Cells ; Adipocytes - drug effects ; Adipocytes - metabolism ; AMP-Activated Protein Kinases - physiology ; Animals ; Carbohydrate Metabolism - drug effects ; Diabetes ; Endocrinology ; Glucose - pharmacokinetics ; Glucose Transporter Type 4 - metabolism ; Humanities and Social Sciences ; Internal Medicine ; Medicine ; Medicine & Public Health ; Mice ; multidisciplinary ; Original Article ; Phosphorylation - drug effects ; Protein Transport - drug effects ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Serine-Threonine Kinases - physiology ; Science ; Signal Transduction - drug effects ; Testosterone - pharmacology</subject><ispartof>Endocrine, 2016-01, Vol.51 (1), p.174-184</ispartof><rights>Springer Science+Business Media New York 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c480t-431cfecf371c3b824c2df81d017e5d927e5c212ca2e178ab83db17d3cf9dcf8b3</citedby><cites>FETCH-LOGICAL-c480t-431cfecf371c3b824c2df81d017e5d927e5c212ca2e178ab83db17d3cf9dcf8b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12020-015-0666-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12020-015-0666-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26100787$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mitsuhashi, Kazuteru</creatorcontrib><creatorcontrib>Senmaru, Takafumi</creatorcontrib><creatorcontrib>Fukuda, Takuya</creatorcontrib><creatorcontrib>Yamazaki, Masahiro</creatorcontrib><creatorcontrib>Shinomiya, Katsuhiko</creatorcontrib><creatorcontrib>Ueno, Morio</creatorcontrib><creatorcontrib>Kinoshita, Shigeru</creatorcontrib><creatorcontrib>Kitawaki, Jo</creatorcontrib><creatorcontrib>Katsuyama, Masato</creatorcontrib><creatorcontrib>Tsujikawa, Muneo</creatorcontrib><creatorcontrib>Obayashi, Hiroshi</creatorcontrib><creatorcontrib>Nakamura, Naoto</creatorcontrib><creatorcontrib>Fukui, Michiaki</creatorcontrib><title>Testosterone stimulates glucose uptake and GLUT4 translocation through LKB1/AMPK signaling in 3T3-L1 adipocytes</title><title>Endocrine</title><addtitle>Endocrine</addtitle><addtitle>Endocrine</addtitle><description>Decreases in serum testosterone concentrations in aging men are associated with metabolic disorders. Testosterone has been reported to increase GLUT4-dependent glucose uptake in skeletal muscle cells and cardiomyocytes. However, studies on glucose uptake occurring in response to testosterone stimulation in adipocytes are currently not available. This study was designed to determine the effects of testosterone on glucose uptake in adipocytes. Glucose uptake was assessed with 2-[
3
H] deoxyglucose in 3T3-L1 adipocytes. GLUT4 translocation was evaluated in plasma membrane (PM) sheets and PM fractions by immunofluorescence and immunoblotting, respectively. Activation of GLUT4 translocation-related protein kinases, including Akt, AMPK, LKB1, CaMKI, CaMKII, and Cbl was followed by immunoblotting. Expression levels of androgen receptor (AR) mRNA and AR translocation to the PM were assessed by real-time RT-PCR and immunoblotting, respectively. The results showed that both high-dose (100 nM) testosterone and testosterone-BSA increased glucose uptake and GLUT4 translocation to the PM, independently of the intracellular AR. Testosterone and testosterone-BSA stimulated the phosphorylation of AMPK, LKB1, and CaMKII. The knockdown of LKB1 by siRNA attenuated testosterone- and testosterone-BSA-stimulated AMPK phosphorylation and glucose uptake. These results indicate that high-dose testosterone and testosterone-BSA increase GLUT4-dependent glucose uptake in 3T3-L1 adipocytes by inducing the LKB1/AMPK signaling pathway.</description><subject>3T3-L1 Cells</subject><subject>Adipocytes - drug effects</subject><subject>Adipocytes - metabolism</subject><subject>AMP-Activated Protein Kinases - physiology</subject><subject>Animals</subject><subject>Carbohydrate Metabolism - drug effects</subject><subject>Diabetes</subject><subject>Endocrinology</subject><subject>Glucose - pharmacokinetics</subject><subject>Glucose Transporter Type 4 - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Internal Medicine</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Mice</subject><subject>multidisciplinary</subject><subject>Original Article</subject><subject>Phosphorylation - drug effects</subject><subject>Protein Transport - drug effects</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-Serine-Threonine Kinases - physiology</subject><subject>Science</subject><subject>Signal Transduction - drug effects</subject><subject>Testosterone - pharmacology</subject><issn>1355-008X</issn><issn>1559-0100</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9P3DAQxa2KqvxpP0AvlY9cAmM7ib1HioAigtrDIvVmObYTQrP21uMc9tvXq6UcucyMZt570vwI-crgggHIS2QcOFTAmgratq12H8gJa5pV2QAclVk05QLq9zE5RXwB4Jy38hM55u3er-QJiWuPOWL2KQZPMU-bZTbZIx3nxUb0dNlm88dTExy9657WNc3JBJyjNXmKgebnFJfxmXYP39nl1eOvB4rTGMw8hZFOgYq1qDpGjZu20e5K7mfycTAz-i-v_Yw83d6sr39U3c-7--urrrK1glzVgtnB20FIZkWveG25GxRzwKRv3IqXajnj1nDPpDK9Eq5n0gk7rJwdVC_OyPkhd5vi36X8qDcTWj_PJvi4oGayBSVrqKFI2UFqU0RMftDbNG1M2mkGes9JHzjrwlnvOetd8Xx7jV_6jXdvjv9gi4AfBFhOYfRJv8QlFTD4Tuo_aDmJrw</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Mitsuhashi, Kazuteru</creator><creator>Senmaru, Takafumi</creator><creator>Fukuda, Takuya</creator><creator>Yamazaki, Masahiro</creator><creator>Shinomiya, Katsuhiko</creator><creator>Ueno, Morio</creator><creator>Kinoshita, Shigeru</creator><creator>Kitawaki, Jo</creator><creator>Katsuyama, Masato</creator><creator>Tsujikawa, Muneo</creator><creator>Obayashi, Hiroshi</creator><creator>Nakamura, Naoto</creator><creator>Fukui, Michiaki</creator><general>Springer US</general><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>20160101</creationdate><title>Testosterone stimulates glucose uptake and GLUT4 translocation through LKB1/AMPK signaling in 3T3-L1 adipocytes</title><author>Mitsuhashi, Kazuteru ; Senmaru, Takafumi ; Fukuda, Takuya ; Yamazaki, Masahiro ; Shinomiya, Katsuhiko ; Ueno, Morio ; Kinoshita, Shigeru ; Kitawaki, Jo ; Katsuyama, Masato ; Tsujikawa, Muneo ; Obayashi, Hiroshi ; Nakamura, Naoto ; Fukui, Michiaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c480t-431cfecf371c3b824c2df81d017e5d927e5c212ca2e178ab83db17d3cf9dcf8b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>3T3-L1 Cells</topic><topic>Adipocytes - drug effects</topic><topic>Adipocytes - metabolism</topic><topic>AMP-Activated Protein Kinases - physiology</topic><topic>Animals</topic><topic>Carbohydrate Metabolism - drug effects</topic><topic>Diabetes</topic><topic>Endocrinology</topic><topic>Glucose - pharmacokinetics</topic><topic>Glucose Transporter Type 4 - metabolism</topic><topic>Humanities and Social Sciences</topic><topic>Internal Medicine</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Mice</topic><topic>multidisciplinary</topic><topic>Original Article</topic><topic>Phosphorylation - drug effects</topic><topic>Protein Transport - drug effects</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-Serine-Threonine Kinases - physiology</topic><topic>Science</topic><topic>Signal Transduction - drug effects</topic><topic>Testosterone - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mitsuhashi, Kazuteru</creatorcontrib><creatorcontrib>Senmaru, Takafumi</creatorcontrib><creatorcontrib>Fukuda, Takuya</creatorcontrib><creatorcontrib>Yamazaki, Masahiro</creatorcontrib><creatorcontrib>Shinomiya, Katsuhiko</creatorcontrib><creatorcontrib>Ueno, Morio</creatorcontrib><creatorcontrib>Kinoshita, Shigeru</creatorcontrib><creatorcontrib>Kitawaki, Jo</creatorcontrib><creatorcontrib>Katsuyama, Masato</creatorcontrib><creatorcontrib>Tsujikawa, Muneo</creatorcontrib><creatorcontrib>Obayashi, Hiroshi</creatorcontrib><creatorcontrib>Nakamura, Naoto</creatorcontrib><creatorcontrib>Fukui, Michiaki</creatorcontrib><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>Endocrine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mitsuhashi, Kazuteru</au><au>Senmaru, Takafumi</au><au>Fukuda, Takuya</au><au>Yamazaki, Masahiro</au><au>Shinomiya, Katsuhiko</au><au>Ueno, Morio</au><au>Kinoshita, Shigeru</au><au>Kitawaki, Jo</au><au>Katsuyama, Masato</au><au>Tsujikawa, Muneo</au><au>Obayashi, Hiroshi</au><au>Nakamura, Naoto</au><au>Fukui, Michiaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Testosterone stimulates glucose uptake and GLUT4 translocation through LKB1/AMPK signaling in 3T3-L1 adipocytes</atitle><jtitle>Endocrine</jtitle><stitle>Endocrine</stitle><addtitle>Endocrine</addtitle><date>2016-01-01</date><risdate>2016</risdate><volume>51</volume><issue>1</issue><spage>174</spage><epage>184</epage><pages>174-184</pages><issn>1355-008X</issn><eissn>1559-0100</eissn><abstract>Decreases in serum testosterone concentrations in aging men are associated with metabolic disorders. Testosterone has been reported to increase GLUT4-dependent glucose uptake in skeletal muscle cells and cardiomyocytes. However, studies on glucose uptake occurring in response to testosterone stimulation in adipocytes are currently not available. This study was designed to determine the effects of testosterone on glucose uptake in adipocytes. Glucose uptake was assessed with 2-[
3
H] deoxyglucose in 3T3-L1 adipocytes. GLUT4 translocation was evaluated in plasma membrane (PM) sheets and PM fractions by immunofluorescence and immunoblotting, respectively. Activation of GLUT4 translocation-related protein kinases, including Akt, AMPK, LKB1, CaMKI, CaMKII, and Cbl was followed by immunoblotting. Expression levels of androgen receptor (AR) mRNA and AR translocation to the PM were assessed by real-time RT-PCR and immunoblotting, respectively. The results showed that both high-dose (100 nM) testosterone and testosterone-BSA increased glucose uptake and GLUT4 translocation to the PM, independently of the intracellular AR. Testosterone and testosterone-BSA stimulated the phosphorylation of AMPK, LKB1, and CaMKII. The knockdown of LKB1 by siRNA attenuated testosterone- and testosterone-BSA-stimulated AMPK phosphorylation and glucose uptake. These results indicate that high-dose testosterone and testosterone-BSA increase GLUT4-dependent glucose uptake in 3T3-L1 adipocytes by inducing the LKB1/AMPK signaling pathway.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>26100787</pmid><doi>10.1007/s12020-015-0666-y</doi><tpages>11</tpages></addata></record> |
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| subjects | 3T3-L1 Cells Adipocytes - drug effects Adipocytes - metabolism AMP-Activated Protein Kinases - physiology Animals Carbohydrate Metabolism - drug effects Diabetes Endocrinology Glucose - pharmacokinetics Glucose Transporter Type 4 - metabolism Humanities and Social Sciences Internal Medicine Medicine Medicine & Public Health Mice multidisciplinary Original Article Phosphorylation - drug effects Protein Transport - drug effects Protein-Serine-Threonine Kinases - metabolism Protein-Serine-Threonine Kinases - physiology Science Signal Transduction - drug effects Testosterone - pharmacology |
| title | Testosterone stimulates glucose uptake and GLUT4 translocation through LKB1/AMPK signaling in 3T3-L1 adipocytes |
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