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Activation of PPARγ negatively regulates O-GlcNAcylation of Sp1
O-GlcNAcylation is a kind of post-translational modification and many nuclear and cytoplasmic proteins are O-GlcNAcylated. In this study, we demonstrated that thiazolidinediones (TZDs), which are used as insulin sensitizer, specifically inhibited the O-GlcNAcylation of Sp1 but did not affect the O-G...
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| Published in: | Biochemical and biophysical research communications 2008-08, Vol.372 (4), p.713-718 |
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| Main Authors: | , , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c331t-3a2d81769494a6736290f89f8291725db2dad7f36180f14efc54fade815ce32d3 |
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| cites | cdi_FETCH-LOGICAL-c331t-3a2d81769494a6736290f89f8291725db2dad7f36180f14efc54fade815ce32d3 |
| container_end_page | 718 |
| container_issue | 4 |
| container_start_page | 713 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 372 |
| creator | Chung, Sung Soo Kim, Ji Hyun Park, Ho Seon Choi, Hye Hun Lee, Kyeong Won Cho, Young Min Lee, Hong Kyu Park, Kyong Soo |
| description | O-GlcNAcylation is a kind of post-translational modification and many nuclear and cytoplasmic proteins are
O-GlcNAcylated. In this study, we demonstrated that thiazolidinediones (TZDs), which are used as insulin sensitizer, specifically inhibited the
O-GlcNAcylation of Sp1 but did not affect the
O-GlcNAcylation of the total proteins in cell culture systems and mouse models. This effect was mediated by peroxisome proliferator activated receptor γ (PPARγ) activation and probably by synthesis of a specific protein induced by PPARγ activation. In addition, we demonstrated that the
O-GlcNAcylation sites in the zinc-finger domain were involved in the transcriptional activation of Sp1 and that rosiglitazone, a member of TZDs, affected Sp1 transcriptional activity partially by regulating the
O-GlcNAcylation level of these sites. Considering the role of hexosamine biosynthesis pathway in hyperglycemia-induced insulin resistance and Sp1 in the hyperglycemia-induced gene expression, the regulation of Sp1
O-GlcNAcylation by TZDs may help to explain the function of TZDs as a treatment for insulin resistance and diabetes. |
| doi_str_mv | 10.1016/j.bbrc.2008.05.096 |
| format | article |
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O-GlcNAcylated. In this study, we demonstrated that thiazolidinediones (TZDs), which are used as insulin sensitizer, specifically inhibited the
O-GlcNAcylation of Sp1 but did not affect the
O-GlcNAcylation of the total proteins in cell culture systems and mouse models. This effect was mediated by peroxisome proliferator activated receptor γ (PPARγ) activation and probably by synthesis of a specific protein induced by PPARγ activation. In addition, we demonstrated that the
O-GlcNAcylation sites in the zinc-finger domain were involved in the transcriptional activation of Sp1 and that rosiglitazone, a member of TZDs, affected Sp1 transcriptional activity partially by regulating the
O-GlcNAcylation level of these sites. Considering the role of hexosamine biosynthesis pathway in hyperglycemia-induced insulin resistance and Sp1 in the hyperglycemia-induced gene expression, the regulation of Sp1
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O-GlcNAcylated. In this study, we demonstrated that thiazolidinediones (TZDs), which are used as insulin sensitizer, specifically inhibited the
O-GlcNAcylation of Sp1 but did not affect the
O-GlcNAcylation of the total proteins in cell culture systems and mouse models. This effect was mediated by peroxisome proliferator activated receptor γ (PPARγ) activation and probably by synthesis of a specific protein induced by PPARγ activation. In addition, we demonstrated that the
O-GlcNAcylation sites in the zinc-finger domain were involved in the transcriptional activation of Sp1 and that rosiglitazone, a member of TZDs, affected Sp1 transcriptional activity partially by regulating the
O-GlcNAcylation level of these sites. Considering the role of hexosamine biosynthesis pathway in hyperglycemia-induced insulin resistance and Sp1 in the hyperglycemia-induced gene expression, the regulation of Sp1
O-GlcNAcylation by TZDs may help to explain the function of TZDs as a treatment for insulin resistance and diabetes.</description><subject>O-GlcNAcylation</subject><subject>PPARγ</subject><subject>Sp1</subject><subject>Thiazolidinediones</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNp9kM9Kw0AQhxdRsFZfwFNO3hJnN8kmCx4MxVah2OIf8LZsd2fLljSpu2mhz-V7-EymVDx6Ghh-34-Zj5BrCgkFym9XyWLhdcIAygTyBAQ_IQMKAmJGITslAwDgMRP045xchLACoDTjYkDuK925nepc20Stjebz6uX7K2pw2a92WO8jj8ttrToM0Sye1Pq50vv6L_66oZfkzKo64NXvHJL38cPb6DGeziZPo2oa6zSlXZwqZkpacJGJTPEi5UyALYUt-5sKlpsFM8oUNuW0BEsztDrPrDJY0lxjykw6JDfH3o1vP7cYOrl2QWNdqwbbbZAMSgEFK_ogOwa1b0PwaOXGu7Xye0lBHmTJlTzIkgdZEnLZy-qhuyOE_Qs7h14G7bDRaJxH3UnTuv_wH2Kmci4</recordid><startdate>20080808</startdate><enddate>20080808</enddate><creator>Chung, Sung Soo</creator><creator>Kim, Ji Hyun</creator><creator>Park, Ho Seon</creator><creator>Choi, Hye Hun</creator><creator>Lee, Kyeong Won</creator><creator>Cho, Young Min</creator><creator>Lee, Hong Kyu</creator><creator>Park, Kyong Soo</creator><general>Elsevier Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20080808</creationdate><title>Activation of PPARγ negatively regulates O-GlcNAcylation of Sp1</title><author>Chung, Sung Soo ; Kim, Ji Hyun ; Park, Ho Seon ; Choi, Hye Hun ; Lee, Kyeong Won ; Cho, Young Min ; Lee, Hong Kyu ; Park, Kyong Soo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c331t-3a2d81769494a6736290f89f8291725db2dad7f36180f14efc54fade815ce32d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>O-GlcNAcylation</topic><topic>PPARγ</topic><topic>Sp1</topic><topic>Thiazolidinediones</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chung, Sung Soo</creatorcontrib><creatorcontrib>Kim, Ji Hyun</creatorcontrib><creatorcontrib>Park, Ho Seon</creatorcontrib><creatorcontrib>Choi, Hye Hun</creatorcontrib><creatorcontrib>Lee, Kyeong Won</creatorcontrib><creatorcontrib>Cho, Young Min</creatorcontrib><creatorcontrib>Lee, Hong Kyu</creatorcontrib><creatorcontrib>Park, Kyong Soo</creatorcontrib><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chung, Sung Soo</au><au>Kim, Ji Hyun</au><au>Park, Ho Seon</au><au>Choi, Hye Hun</au><au>Lee, Kyeong Won</au><au>Cho, Young Min</au><au>Lee, Hong Kyu</au><au>Park, Kyong Soo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of PPARγ negatively regulates O-GlcNAcylation of Sp1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><date>2008-08-08</date><risdate>2008</risdate><volume>372</volume><issue>4</issue><spage>713</spage><epage>718</epage><pages>713-718</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>O-GlcNAcylation is a kind of post-translational modification and many nuclear and cytoplasmic proteins are
O-GlcNAcylated. In this study, we demonstrated that thiazolidinediones (TZDs), which are used as insulin sensitizer, specifically inhibited the
O-GlcNAcylation of Sp1 but did not affect the
O-GlcNAcylation of the total proteins in cell culture systems and mouse models. This effect was mediated by peroxisome proliferator activated receptor γ (PPARγ) activation and probably by synthesis of a specific protein induced by PPARγ activation. In addition, we demonstrated that the
O-GlcNAcylation sites in the zinc-finger domain were involved in the transcriptional activation of Sp1 and that rosiglitazone, a member of TZDs, affected Sp1 transcriptional activity partially by regulating the
O-GlcNAcylation level of these sites. Considering the role of hexosamine biosynthesis pathway in hyperglycemia-induced insulin resistance and Sp1 in the hyperglycemia-induced gene expression, the regulation of Sp1
O-GlcNAcylation by TZDs may help to explain the function of TZDs as a treatment for insulin resistance and diabetes.</abstract><pub>Elsevier Inc</pub><doi>10.1016/j.bbrc.2008.05.096</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2008-08, Vol.372 (4), p.713-718 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_20890727 |
| source | ScienceDirect Freedom Collection 2022-2024 |
| subjects | O-GlcNAcylation PPARγ Sp1 Thiazolidinediones |
| title | Activation of PPARγ negatively regulates O-GlcNAcylation of Sp1 |
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