Advanced glycation end products-induced insulin resistance involves repression of skeletal muscle GLUT4 expression
Little is known about advanced glycation end products (AGEs) participation in glucose homeostasis, a process in which skeletal muscle glucose transporter GLUT4 ( Scl2a4 gene) plays a key role. This study investigated (1) the in vivo and in vitro effects of AGEs on Slc2a4 /GLUT4 expression in skeleta...
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| Veröffentlicht in: | Scientific reports 2018-05, Vol.8 (1), p.8109-11, Article 8109 |
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| creator | Pinto-Junior, Danilo C. Silva, Karolline S. Michalani, Maria L. Yonamine, Caio Y. Esteves, João V. Fabre, Nelly T. Thieme, Karina Catanozi, Sérgio Okamoto, Maristela M. Seraphim, Patricia M. Corrêa-Giannella, Maria L. Passarelli, Marisa Machado, Ubiratan F. |
| description | Little is known about advanced glycation end products (AGEs) participation in glucose homeostasis, a process in which skeletal muscle glucose transporter GLUT4 (
Scl2a4
gene) plays a key role. This study investigated (1) the
in vivo
and
in vitro
effects of AGEs on
Slc2a4
/GLUT4 expression in skeletal muscle of healthy rats, and (2) the potential involvement of endoplasmic reticulum and inflammatory stress in the observed regulations. For
in viv
o analysis, rats were treated with advanced glycated rat albumin (AGE-albumin) for 12 weeks; for
in vitro
analysis, soleus muscles from normal rats were incubated with bovine AGE-albumin for 2.5 to 7.5 hours.
In vivo
, AGE-albumin induced whole-body insulin resistance; decreased (~30%)
Slc2a4
mRNA and GLUT4 protein content; and increased (~30%) the nuclear content of nuclear factor NF-kappa-B p50 subunit (NFKB1), and cellular content of 78 kDa glucose-regulated protein (GRP78).
In vitro
, incubation with AGE-albumin decreased (~50%) the
Slc2a4
/GLUT4 content; and increased cellular content of GRP78/94, phosphorylated-IKK-alpha/beta, nuclear content of NFKB1 and RELA, and the nuclear protein binding into
Slc2a4
promoter NFKB-binding site. The data reveal that AGEs impair glucose homeostasis in non-diabetic states of increased AGEs concentration; an effect that involves activation of endoplasmic reticulum- and inflammatory-stress and repression of
Slc2a4
/GLUT4 expression. |
| doi_str_mv | 10.1038/s41598-018-26482-6 |
| format | Article |
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Scl2a4
gene) plays a key role. This study investigated (1) the
in vivo
and
in vitro
effects of AGEs on
Slc2a4
/GLUT4 expression in skeletal muscle of healthy rats, and (2) the potential involvement of endoplasmic reticulum and inflammatory stress in the observed regulations. For
in viv
o analysis, rats were treated with advanced glycated rat albumin (AGE-albumin) for 12 weeks; for
in vitro
analysis, soleus muscles from normal rats were incubated with bovine AGE-albumin for 2.5 to 7.5 hours.
In vivo
, AGE-albumin induced whole-body insulin resistance; decreased (~30%)
Slc2a4
mRNA and GLUT4 protein content; and increased (~30%) the nuclear content of nuclear factor NF-kappa-B p50 subunit (NFKB1), and cellular content of 78 kDa glucose-regulated protein (GRP78).
In vitro
, incubation with AGE-albumin decreased (~50%) the
Slc2a4
/GLUT4 content; and increased cellular content of GRP78/94, phosphorylated-IKK-alpha/beta, nuclear content of NFKB1 and RELA, and the nuclear protein binding into
Slc2a4
promoter NFKB-binding site. The data reveal that AGEs impair glucose homeostasis in non-diabetic states of increased AGEs concentration; an effect that involves activation of endoplasmic reticulum- and inflammatory-stress and repression of
Slc2a4
/GLUT4 expression.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-018-26482-6</identifier><identifier>PMID: 29802324</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/95 ; 38/39 ; 38/77 ; 45 ; 59 ; 631/443/319 ; 631/80/2023 ; 82 ; 82/29 ; 82/80 ; 96/95 ; Advanced glycosylation end products ; Age ; Albumin ; Diabetes mellitus ; Endoplasmic reticulum ; Glucose ; Glucose transporter ; Glycosylation ; Homeostasis ; Humanities and Social Sciences ; IKK protein ; Inflammation ; Insulin ; Insulin resistance ; mRNA ; multidisciplinary ; Muscles ; Musculoskeletal system ; NF-κB protein ; Proteins ; RelA protein ; Science ; Science (multidisciplinary) ; Skeletal muscle</subject><ispartof>Scientific reports, 2018-05, Vol.8 (1), p.8109-11, Article 8109</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-3daf324a28def3d7db5c7673f6e713859fbc01ce93325c9dd1b00af9ebecb3f23</citedby><cites>FETCH-LOGICAL-c540t-3daf324a28def3d7db5c7673f6e713859fbc01ce93325c9dd1b00af9ebecb3f23</cites><orcidid>0000-0003-2145-6640 ; 0000-0001-8274-000X</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/PMC5970140/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5970140/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29802324$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pinto-Junior, Danilo C.</creatorcontrib><creatorcontrib>Silva, Karolline S.</creatorcontrib><creatorcontrib>Michalani, Maria L.</creatorcontrib><creatorcontrib>Yonamine, Caio Y.</creatorcontrib><creatorcontrib>Esteves, João V.</creatorcontrib><creatorcontrib>Fabre, Nelly T.</creatorcontrib><creatorcontrib>Thieme, Karina</creatorcontrib><creatorcontrib>Catanozi, Sérgio</creatorcontrib><creatorcontrib>Okamoto, Maristela M.</creatorcontrib><creatorcontrib>Seraphim, Patricia M.</creatorcontrib><creatorcontrib>Corrêa-Giannella, Maria L.</creatorcontrib><creatorcontrib>Passarelli, Marisa</creatorcontrib><creatorcontrib>Machado, Ubiratan F.</creatorcontrib><title>Advanced glycation end products-induced insulin resistance involves repression of skeletal muscle GLUT4 expression</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Little is known about advanced glycation end products (AGEs) participation in glucose homeostasis, a process in which skeletal muscle glucose transporter GLUT4 (
Scl2a4
gene) plays a key role. This study investigated (1) the
in vivo
and
in vitro
effects of AGEs on
Slc2a4
/GLUT4 expression in skeletal muscle of healthy rats, and (2) the potential involvement of endoplasmic reticulum and inflammatory stress in the observed regulations. For
in viv
o analysis, rats were treated with advanced glycated rat albumin (AGE-albumin) for 12 weeks; for
in vitro
analysis, soleus muscles from normal rats were incubated with bovine AGE-albumin for 2.5 to 7.5 hours.
In vivo
, AGE-albumin induced whole-body insulin resistance; decreased (~30%)
Slc2a4
mRNA and GLUT4 protein content; and increased (~30%) the nuclear content of nuclear factor NF-kappa-B p50 subunit (NFKB1), and cellular content of 78 kDa glucose-regulated protein (GRP78).
In vitro
, incubation with AGE-albumin decreased (~50%) the
Slc2a4
/GLUT4 content; and increased cellular content of GRP78/94, phosphorylated-IKK-alpha/beta, nuclear content of NFKB1 and RELA, and the nuclear protein binding into
Slc2a4
promoter NFKB-binding site. The data reveal that AGEs impair glucose homeostasis in non-diabetic states of increased AGEs concentration; an effect that involves activation of endoplasmic reticulum- and inflammatory-stress and repression of
Slc2a4
/GLUT4 expression.</description><subject>13/95</subject><subject>38/39</subject><subject>38/77</subject><subject>45</subject><subject>59</subject><subject>631/443/319</subject><subject>631/80/2023</subject><subject>82</subject><subject>82/29</subject><subject>82/80</subject><subject>96/95</subject><subject>Advanced glycosylation end products</subject><subject>Age</subject><subject>Albumin</subject><subject>Diabetes mellitus</subject><subject>Endoplasmic reticulum</subject><subject>Glucose</subject><subject>Glucose transporter</subject><subject>Glycosylation</subject><subject>Homeostasis</subject><subject>Humanities and Social Sciences</subject><subject>IKK protein</subject><subject>Inflammation</subject><subject>Insulin</subject><subject>Insulin resistance</subject><subject>mRNA</subject><subject>multidisciplinary</subject><subject>Muscles</subject><subject>Musculoskeletal system</subject><subject>NF-κB protein</subject><subject>Proteins</subject><subject>RelA 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glycation end products-induced insulin resistance involves repression of skeletal muscle GLUT4 expression</title><author>Pinto-Junior, Danilo C. ; Silva, Karolline S. ; Michalani, Maria L. ; Yonamine, Caio Y. ; Esteves, João V. ; Fabre, Nelly T. ; Thieme, Karina ; Catanozi, Sérgio ; Okamoto, Maristela M. ; Seraphim, Patricia M. ; Corrêa-Giannella, Maria L. ; Passarelli, Marisa ; Machado, Ubiratan F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c540t-3daf324a28def3d7db5c7673f6e713859fbc01ce93325c9dd1b00af9ebecb3f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>13/95</topic><topic>38/39</topic><topic>38/77</topic><topic>45</topic><topic>59</topic><topic>631/443/319</topic><topic>631/80/2023</topic><topic>82</topic><topic>82/29</topic><topic>82/80</topic><topic>96/95</topic><topic>Advanced glycosylation end products</topic><topic>Age</topic><topic>Albumin</topic><topic>Diabetes mellitus</topic><topic>Endoplasmic reticulum</topic><topic>Glucose</topic><topic>Glucose transporter</topic><topic>Glycosylation</topic><topic>Homeostasis</topic><topic>Humanities and Social Sciences</topic><topic>IKK protein</topic><topic>Inflammation</topic><topic>Insulin</topic><topic>Insulin resistance</topic><topic>mRNA</topic><topic>multidisciplinary</topic><topic>Muscles</topic><topic>Musculoskeletal system</topic><topic>NF-κB protein</topic><topic>Proteins</topic><topic>RelA protein</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Skeletal muscle</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pinto-Junior, Danilo C.</creatorcontrib><creatorcontrib>Silva, Karolline S.</creatorcontrib><creatorcontrib>Michalani, Maria L.</creatorcontrib><creatorcontrib>Yonamine, Caio Y.</creatorcontrib><creatorcontrib>Esteves, João V.</creatorcontrib><creatorcontrib>Fabre, Nelly T.</creatorcontrib><creatorcontrib>Thieme, Karina</creatorcontrib><creatorcontrib>Catanozi, Sérgio</creatorcontrib><creatorcontrib>Okamoto, Maristela M.</creatorcontrib><creatorcontrib>Seraphim, Patricia M.</creatorcontrib><creatorcontrib>Corrêa-Giannella, Maria L.</creatorcontrib><creatorcontrib>Passarelli, Marisa</creatorcontrib><creatorcontrib>Machado, Ubiratan F.</creatorcontrib><collection>Springer Nature OA Free Journals</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>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science 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titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pinto-Junior, Danilo C.</au><au>Silva, Karolline S.</au><au>Michalani, Maria L.</au><au>Yonamine, Caio Y.</au><au>Esteves, João V.</au><au>Fabre, Nelly T.</au><au>Thieme, Karina</au><au>Catanozi, Sérgio</au><au>Okamoto, Maristela M.</au><au>Seraphim, Patricia M.</au><au>Corrêa-Giannella, Maria L.</au><au>Passarelli, Marisa</au><au>Machado, Ubiratan F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Advanced glycation end products-induced insulin resistance involves repression of skeletal muscle GLUT4 expression</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2018-05-25</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>8109</spage><epage>11</epage><pages>8109-11</pages><artnum>8109</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Little is known about advanced glycation end products (AGEs) participation in glucose homeostasis, a process in which skeletal muscle glucose transporter GLUT4 (
Scl2a4
gene) plays a key role. This study investigated (1) the
in vivo
and
in vitro
effects of AGEs on
Slc2a4
/GLUT4 expression in skeletal muscle of healthy rats, and (2) the potential involvement of endoplasmic reticulum and inflammatory stress in the observed regulations. For
in viv
o analysis, rats were treated with advanced glycated rat albumin (AGE-albumin) for 12 weeks; for
in vitro
analysis, soleus muscles from normal rats were incubated with bovine AGE-albumin for 2.5 to 7.5 hours.
In vivo
, AGE-albumin induced whole-body insulin resistance; decreased (~30%)
Slc2a4
mRNA and GLUT4 protein content; and increased (~30%) the nuclear content of nuclear factor NF-kappa-B p50 subunit (NFKB1), and cellular content of 78 kDa glucose-regulated protein (GRP78).
In vitro
, incubation with AGE-albumin decreased (~50%) the
Slc2a4
/GLUT4 content; and increased cellular content of GRP78/94, phosphorylated-IKK-alpha/beta, nuclear content of NFKB1 and RELA, and the nuclear protein binding into
Slc2a4
promoter NFKB-binding site. The data reveal that AGEs impair glucose homeostasis in non-diabetic states of increased AGEs concentration; an effect that involves activation of endoplasmic reticulum- and inflammatory-stress and repression of
Slc2a4
/GLUT4 expression.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29802324</pmid><doi>10.1038/s41598-018-26482-6</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0003-2145-6640</orcidid><orcidid>https://orcid.org/0000-0001-8274-000X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Nature Free; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; Springer Nature OA Free Journals |
| subjects | 13/95 38/39 38/77 45 59 631/443/319 631/80/2023 82 82/29 82/80 96/95 Advanced glycosylation end products Age Albumin Diabetes mellitus Endoplasmic reticulum Glucose Glucose transporter Glycosylation Homeostasis Humanities and Social Sciences IKK protein Inflammation Insulin Insulin resistance mRNA multidisciplinary Muscles Musculoskeletal system NF-κB protein Proteins RelA protein Science Science (multidisciplinary) Skeletal muscle |
| title | Advanced glycation end products-induced insulin resistance involves repression of skeletal muscle GLUT4 expression |
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