Regulation of O-GlcNAcylation on endothelial nitric oxide synthase by glucose deprivation and identification of its O-GlcNAcylation sites

As an energy-sensitive post-translational modification, O-GlcNAcylation plays a major role in endothelial nitric oxide synthase (eNOS) activity regulation. However, effects of glucose deprivation on eNOS O-GlcNAcylation and the presence of novel O-GlcNAcylation sites of eNOS under glucose deprivatio...

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Published in:	Scientific reports Vol. 10; no. 1; p. 19364
Main Authors:	He, An, Hu, Shupeng, Pi, Qiangzhong, Guo, Yongzheng, Long, Yang, Luo, Suxin, Xia, Yong
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 09.11.2020 Nature Publishing Group
Subjects:	631/45 631/45/320 692/4019 692/4019/592 Acylation Animals Aorta Cattle Cell culture Endothelial cells Endothelial Cells - enzymology Glucose Glucose - metabolism Glucose - pharmacology HEK293 Cells High-performance liquid chromatography Humanities and Social Sciences Humans Immunoblotting Immunoprecipitation Liquid chromatography multidisciplinary Mutation Nitric oxide Nitric Oxide Synthase Type III - metabolism Nitric-oxide synthase O-GlcNAcylation Phosphorylation Post-translation Protein Processing, Post-Translational Rats Science Science (multidisciplinary) Serine Thorax Translation Variance analysis
ISSN:	2045-2322, 2045-2322
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Abstract	As an energy-sensitive post-translational modification, O-GlcNAcylation plays a major role in endothelial nitric oxide synthase (eNOS) activity regulation. However, effects of glucose deprivation on eNOS O-GlcNAcylation and the presence of novel O-GlcNAcylation sites of eNOS under glucose deprivation remain unknown. Hence, we aim to determine the effects of glucose deprivation on O-GlcNAcylation and novel O-GlcNAcylation sites of eNOS. Bovine aortic endothelial cells (BAECs) and Sprague–Dawley rats were induced by glucose deprivation and their eNOS O-GlcNAcylation was subjected to immunoblotting. eNOS and transfected eNOS were purified by pull-down assay and immunoprecipitation respectively. Novel O-GlcNAcylation sites of eNOS were predicted by HPLC–MS and MS/MS Ion and determined by immunoblotting. eNOS activity was detected by Elisa and isotope labeling method. In BAECs and rat thoracic aorta, low glucose-associated activation of eNOS was accompanied by elevated O-GlcNAcylation, which did not affect O - linked serine phosphorylation at 1179/1177 residues. Changes in this post-translational modification were associated with increased O-GlcNAc transferase (OGT) expression and were reversed by AMPK knockdown. Immunoblot analysis of cells expressing His-tagged wild-type human eNOS and human eNOS carrying a mutation at the Ser1177 phosphorylation site confirmed an increase in O-GlcNAcylation by glucose deprivation. A marked increase in O-GlcNAcylation indicated that eNOS contained novel O-GlcNAcylation sites that were activated by glucose deprivation. Immunoblot analysis of cells expressing His-tagged human eNOS carrying a mutation at Ser738 and Ser867 confirmed an increase in O-GlcNAcylation by glucose deprivation. Conversely, in His-tagged human eNOS carrying a mutation at Thr866, O-GlcNAcylation was unaffected by glucose deprivation. Differences in culture conditions were identified using two-way analysis of variance (ANOVA), one-way ANOVA, and unpaired Student’s t -test. Glucose deprivation increases O-GlcNAcylation and activity of eNOS, potentially by the AMPK-OGT pathway, suggesting that Thr866 is a novel O-GlcNAcylation site involved in glucose-deprivation mediated eNOS activation.
AbstractList	As an energy-sensitive post-translational modification, O-GlcNAcylation plays a major role in endothelial nitric oxide synthase (eNOS) activity regulation. However, effects of glucose deprivation on eNOS O-GlcNAcylation and the presence of novel O-GlcNAcylation sites of eNOS under glucose deprivation remain unknown. Hence, we aim to determine the effects of glucose deprivation on O-GlcNAcylation and novel O-GlcNAcylation sites of eNOS. Bovine aortic endothelial cells (BAECs) and Sprague-Dawley rats were induced by glucose deprivation and their eNOS O-GlcNAcylation was subjected to immunoblotting. eNOS and transfected eNOS were purified by pull-down assay and immunoprecipitation respectively. Novel O-GlcNAcylation sites of eNOS were predicted by HPLC-MS and MS/MS Ion and determined by immunoblotting. eNOS activity was detected by Elisa and isotope labeling method. In BAECs and rat thoracic aorta, low glucose-associated activation of eNOS was accompanied by elevated O-GlcNAcylation, which did not affect O-linked serine phosphorylation at 1179/1177 residues. Changes in this post-translational modification were associated with increased O-GlcNAc transferase (OGT) expression and were reversed by AMPK knockdown. Immunoblot analysis of cells expressing His-tagged wild-type human eNOS and human eNOS carrying a mutation at the Ser1177 phosphorylation site confirmed an increase in O-GlcNAcylation by glucose deprivation. A marked increase in O-GlcNAcylation indicated that eNOS contained novel O-GlcNAcylation sites that were activated by glucose deprivation. Immunoblot analysis of cells expressing His-tagged human eNOS carrying a mutation at Ser738 and Ser867 confirmed an increase in O-GlcNAcylation by glucose deprivation. Conversely, in His-tagged human eNOS carrying a mutation at Thr866, O-GlcNAcylation was unaffected by glucose deprivation. Differences in culture conditions were identified using two-way analysis of variance (ANOVA), one-way ANOVA, and unpaired Student's t-test. Glucose deprivation increases O-GlcNAcylation and activity of eNOS, potentially by the AMPK-OGT pathway, suggesting that Thr866 is a novel O-GlcNAcylation site involved in glucose-deprivation mediated eNOS activation.As an energy-sensitive post-translational modification, O-GlcNAcylation plays a major role in endothelial nitric oxide synthase (eNOS) activity regulation. However, effects of glucose deprivation on eNOS O-GlcNAcylation and the presence of novel O-GlcNAcylation sites of eNOS under glucose deprivation remain unknown. Hence, we aim to determine the effects of glucose deprivation on O-GlcNAcylation and novel O-GlcNAcylation sites of eNOS. Bovine aortic endothelial cells (BAECs) and Sprague-Dawley rats were induced by glucose deprivation and their eNOS O-GlcNAcylation was subjected to immunoblotting. eNOS and transfected eNOS were purified by pull-down assay and immunoprecipitation respectively. Novel O-GlcNAcylation sites of eNOS were predicted by HPLC-MS and MS/MS Ion and determined by immunoblotting. eNOS activity was detected by Elisa and isotope labeling method. In BAECs and rat thoracic aorta, low glucose-associated activation of eNOS was accompanied by elevated O-GlcNAcylation, which did not affect O-linked serine phosphorylation at 1179/1177 residues. Changes in this post-translational modification were associated with increased O-GlcNAc transferase (OGT) expression and were reversed by AMPK knockdown. Immunoblot analysis of cells expressing His-tagged wild-type human eNOS and human eNOS carrying a mutation at the Ser1177 phosphorylation site confirmed an increase in O-GlcNAcylation by glucose deprivation. A marked increase in O-GlcNAcylation indicated that eNOS contained novel O-GlcNAcylation sites that were activated by glucose deprivation. Immunoblot analysis of cells expressing His-tagged human eNOS carrying a mutation at Ser738 and Ser867 confirmed an increase in O-GlcNAcylation by glucose deprivation. Conversely, in His-tagged human eNOS carrying a mutation at Thr866, O-GlcNAcylation was unaffected by glucose deprivation. Differences in culture conditions were identified using two-way analysis of variance (ANOVA), one-way ANOVA, and unpaired Student's t-test. Glucose deprivation increases O-GlcNAcylation and activity of eNOS, potentially by the AMPK-OGT pathway, suggesting that Thr866 is a novel O-GlcNAcylation site involved in glucose-deprivation mediated eNOS activation. As an energy-sensitive post-translational modification, O-GlcNAcylation plays a major role in endothelial nitric oxide synthase (eNOS) activity regulation. However, effects of glucose deprivation on eNOS O-GlcNAcylation and the presence of novel O-GlcNAcylation sites of eNOS under glucose deprivation remain unknown. Hence, we aim to determine the effects of glucose deprivation on O-GlcNAcylation and novel O-GlcNAcylation sites of eNOS. Bovine aortic endothelial cells (BAECs) and Sprague-Dawley rats were induced by glucose deprivation and their eNOS O-GlcNAcylation was subjected to immunoblotting. eNOS and transfected eNOS were purified by pull-down assay and immunoprecipitation respectively. Novel O-GlcNAcylation sites of eNOS were predicted by HPLC-MS and MS/MS Ion and determined by immunoblotting. eNOS activity was detected by Elisa and isotope labeling method. In BAECs and rat thoracic aorta, low glucose-associated activation of eNOS was accompanied by elevated O-GlcNAcylation, which did not affect O-linked serine phosphorylation at 1179/1177 residues. Changes in this post-translational modification were associated with increased O-GlcNAc transferase (OGT) expression and were reversed by AMPK knockdown. Immunoblot analysis of cells expressing His-tagged wild-type human eNOS and human eNOS carrying a mutation at the Ser1177 phosphorylation site confirmed an increase in O-GlcNAcylation by glucose deprivation. A marked increase in O-GlcNAcylation indicated that eNOS contained novel O-GlcNAcylation sites that were activated by glucose deprivation. Immunoblot analysis of cells expressing His-tagged human eNOS carrying a mutation at Ser738 and Ser867 confirmed an increase in O-GlcNAcylation by glucose deprivation. Conversely, in His-tagged human eNOS carrying a mutation at Thr866, O-GlcNAcylation was unaffected by glucose deprivation. Differences in culture conditions were identified using two-way analysis of variance (ANOVA), one-way ANOVA, and unpaired Student's t-test. Glucose deprivation increases O-GlcNAcylation and activity of eNOS, potentially by the AMPK-OGT pathway, suggesting that Thr866 is a novel O-GlcNAcylation site involved in glucose-deprivation mediated eNOS activation. As an energy-sensitive post-translational modification, O-GlcNAcylation plays a major role in endothelial nitric oxide synthase (eNOS) activity regulation. However, effects of glucose deprivation on eNOS O-GlcNAcylation and the presence of novel O-GlcNAcylation sites of eNOS under glucose deprivation remain unknown. Hence, we aim to determine the effects of glucose deprivation on O-GlcNAcylation and novel O-GlcNAcylation sites of eNOS. Bovine aortic endothelial cells (BAECs) and Sprague–Dawley rats were induced by glucose deprivation and their eNOS O-GlcNAcylation was subjected to immunoblotting. eNOS and transfected eNOS were purified by pull-down assay and immunoprecipitation respectively. Novel O-GlcNAcylation sites of eNOS were predicted by HPLC–MS and MS/MS Ion and determined by immunoblotting. eNOS activity was detected by Elisa and isotope labeling method. In BAECs and rat thoracic aorta, low glucose-associated activation of eNOS was accompanied by elevated O-GlcNAcylation, which did not affect O - linked serine phosphorylation at 1179/1177 residues. Changes in this post-translational modification were associated with increased O-GlcNAc transferase (OGT) expression and were reversed by AMPK knockdown. Immunoblot analysis of cells expressing His-tagged wild-type human eNOS and human eNOS carrying a mutation at the Ser1177 phosphorylation site confirmed an increase in O-GlcNAcylation by glucose deprivation. A marked increase in O-GlcNAcylation indicated that eNOS contained novel O-GlcNAcylation sites that were activated by glucose deprivation. Immunoblot analysis of cells expressing His-tagged human eNOS carrying a mutation at Ser738 and Ser867 confirmed an increase in O-GlcNAcylation by glucose deprivation. Conversely, in His-tagged human eNOS carrying a mutation at Thr866, O-GlcNAcylation was unaffected by glucose deprivation. Differences in culture conditions were identified using two-way analysis of variance (ANOVA), one-way ANOVA, and unpaired Student’s t -test. Glucose deprivation increases O-GlcNAcylation and activity of eNOS, potentially by the AMPK-OGT pathway, suggesting that Thr866 is a novel O-GlcNAcylation site involved in glucose-deprivation mediated eNOS activation.
ArticleNumber	19364
Author	Pi, Qiangzhong Guo, Yongzheng Hu, Shupeng Xia, Yong Luo, Suxin He, An Long, Yang
Author_xml	– sequence: 1 givenname: An surname: He fullname: He, An organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University – sequence: 2 givenname: Shupeng surname: Hu fullname: Hu, Shupeng organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University – sequence: 3 givenname: Qiangzhong surname: Pi fullname: Pi, Qiangzhong organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University – sequence: 4 givenname: Yongzheng surname: Guo fullname: Guo, Yongzheng organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University – sequence: 5 givenname: Yang surname: Long fullname: Long, Yang organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University – sequence: 6 givenname: Suxin surname: Luo fullname: Luo, Suxin organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University – sequence: 7 givenname: Yong surname: Xia fullname: Xia, Yong email: cqmu_cardiology@163.com organization: Division of Cardiology, The First Affiliated Hospital of Chongqing Medical University, Institute of Life Science, Chongqing Medical University
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Cites_doi	10.1007/s40256-017-0220-9 10.3389/fphys.2019.00186 10.1161/01.cir.0000023043.02648.51 10.1126/stke.3122005re13 10.1038/35025203 10.2337/db12-0224 10.1089/ars.2016.6904 10.1074/jbc.274.45.32015 10.2337/db07-0115 10.1016/j.vph.2011.11.003 10.1016/j.ab.2017.08.017 10.1093/glycob/cwh151 10.1111/1753-0407.12521 10.1074/jbc.M801222200 10.1172/JCI119156 10.1007/s00125-016-4146-6 10.1074/jbc.M803198200 10.1074/jbc.M113.523068 10.1073/pnas.0502488102 10.1016/j.diabet.2010.09.001 10.1074/jbc.M707328200 10.1016/j.bbi.2009.11.013 10.1093/cvr/27.7.1380 10.1172/JCI11235 10.1042/BST20160404 10.1161/01.CIR.101.6.676 10.1074/jbc.M109.026351 10.1089/10763270050044425 10.1038/nature09932 10.2174/13816128113196660745
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References	Radomski, Vallance, Whitley, Foxwell, Moncada (CR4) 1993; 27 Kuboki (CR28) 2000; 101 Long, Yan, Luo, Liu, Xia (CR21) 2017; 537 Ali, Woodman (CR30) 2019; 10 Shi, Vanhoutte (CR23) 2017; 9 Love, Hanover (CR22) 2005; 2005 Kader (CR3) 2000; 6 Ceriello (CR6) 2012; 61 Aquinogil, Pierce, Perezcervera, Zenteno, Lefebvre (CR16) 2017; 45 Cheung, Hart (CR9) 2008; 283 Du (CR13) 2001; 108 Taylor, Geisler, Chambers, Mcclain (CR19) 2009; 284 Kreppel, Hart (CR20) 1999; 274 Maccallini, Mollica, Amoroso (CR29) 2017; 17 Takemoto (CR2) 1997; 99 Federici (CR27) 2002; 106 Cabou (CR5) 2007; 56 Musicki, Kramer, Becker, Burnett (CR12) 2005; 102 Kang (CR18) 2009; 284 Bullen (CR17) 2014; 289 Issad, Masson, Pagesy (CR24) 2010; 36 Amiel (CR15) 2017; 60 Erkens (CR1) 2017; 26 Xiao (CR8) 2011; 472 Julenius, Molgaard, Gupta, Brunak (CR11) 2005; 15 Heiss, Dirsch (CR7) 2014; 20 Moore (CR14) 2010; 24 Taylor (CR10) 2008; 283 Beleznai, Bagi (CR25) 2012; 56 Lusis (CR26) 2000; 407 KN Kader (76340_CR3) 2000; 6 DC Love (76340_CR22) 2005; 2005 T Beleznai (76340_CR25) 2012; 56 XL Du (76340_CR13) 2001; 108 M Takemoto (76340_CR2) 1997; 99 WD Cheung (76340_CR9) 2008; 283 AJ Lusis (76340_CR26) 2000; 407 C Maccallini (76340_CR29) 2017; 17 JG Kang (76340_CR18) 2009; 284 LK Kreppel (76340_CR20) 1999; 274 Y Shi (76340_CR23) 2017; 9 A Ceriello (76340_CR6) 2012; 61 Y Long (76340_CR21) 2017; 537 B Musicki (76340_CR12) 2005; 102 M Federici (76340_CR27) 2002; 106 RP Taylor (76340_CR19) 2009; 284 RP Taylor (76340_CR10) 2008; 283 JW Bullen (76340_CR17) 2014; 289 K Julenius (76340_CR11) 2005; 15 EH Heiss (76340_CR7) 2014; 20 K Kuboki (76340_CR28) 2000; 101 T Issad (76340_CR24) 2010; 36 SA Amiel (76340_CR15) 2017; 60 H Moore (76340_CR14) 2010; 24 MW Radomski (76340_CR4) 1993; 27 B Xiao (76340_CR8) 2011; 472 SF Ali (76340_CR30) 2019; 10 C Cabou (76340_CR5) 2007; 56 MO Aquinogil (76340_CR16) 2017; 45 R Erkens (76340_CR1) 2017; 26
References_xml	– volume: 17 start-page: 273 year: 2017 end-page: 281 ident: CR29 article-title: The positive regulation of eNOS signaling by PPAR agonists in cardiovascular diseases publication-title: Am. J. Cardiovasc. Drugs doi: 10.1007/s40256-017-0220-9 – volume: 60 start-page: 3 year: 2017 end-page: 6 ident: CR15 article-title: Glucose concentrations of less than 3.0 mmol/l (54 mg/dl) should be reported in clinical trials: a joint position statement of the American Diabetes Association and the Europian Association for the Study of Diabetes publication-title: Diabetologia – volume: 472 start-page: 230 year: 2011 end-page: 233 ident: CR8 article-title: Structure of mammalian AMPK and its regulation by ADP publication-title: Nature – volume: 102 start-page: 11870 year: 2005 end-page: 11875 ident: CR12 article-title: Inactivation of phosphorylated endothelial nitric oxide synthase (Ser-1177) by O-GlcNAc in diabetes-associated erectile dysfunction publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 6 start-page: 241 year: 2000 end-page: 251 ident: CR3 article-title: eNOS-overexpressing endothelial cells inhibit platelet aggregation and smooth muscle cell proliferation in vitro publication-title: Tissue Eng. – volume: 10 start-page: 186 year: 2019 ident: CR30 article-title: Tocomin restores endothelium-dependent relaxation in the diabetic rat aorta by increasing NO bioavailability and improving the expression of eNOS publication-title: Front. Physiol. doi: 10.3389/fphys.2019.00186 – volume: 9 start-page: 434 year: 2017 end-page: 449 ident: CR23 article-title: Macro- and microvascular endothelial dysfunction in diabetes publication-title: J. Diabetes – volume: 106 start-page: 466 year: 2002 end-page: 472 ident: CR27 article-title: Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells publication-title: Circulation doi: 10.1161/01.cir.0000023043.02648.51 – volume: 284 start-page: 34777 year: 2009 end-page: 34784 ident: CR18 article-title: O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation publication-title: J. Biol. Chem. – volume: 283 start-page: 13009 year: 2008 end-page: 13020 ident: CR9 article-title: AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation publication-title: J. Biol. Chem. – volume: 2005 start-page: 13 year: 2005 ident: CR22 article-title: The hexosamine signaling pathway: deciphering the "O-GlcNAc code" publication-title: Sci. STKE doi: 10.1126/stke.3122005re13 – volume: 407 start-page: 233 year: 2000 end-page: 241 ident: CR26 article-title: Atherosclerosis publication-title: Nature doi: 10.1038/35025203 – volume: 61 start-page: 2993 year: 2012 end-page: 2997 ident: CR6 article-title: Evidence that hyperglycemia after recovery from hypoglycemia worsens endothelial function and increases oxidative stress and inflammation in healthy control subjects and subjects with type 1 diabetes publication-title: Diabetes doi: 10.2337/db12-0224 – volume: 26 start-page: 917 year: 2017 end-page: 935 ident: CR1 article-title: Modulation of local and systemic heterocellular communication by mechanical forces: a role of endothelial nitric oxide synthase publication-title: Antioxid. Redox Signal doi: 10.1089/ars.2016.6904 – volume: 289 start-page: 10592 year: 2014 end-page: 10606 ident: CR17 article-title: Cross-talk between two essential nutrient-sensitive enzymes O-GlcNAc transferase (OGT) and amp-activated protein kinase (AMPK) publication-title: J. Biol. Chem. – volume: 274 start-page: 32015 year: 1999 end-page: 32022 ident: CR20 article-title: Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.45.32015 – volume: 56 start-page: 2872 year: 2007 end-page: 2877 ident: CR5 article-title: Central insulin regulates heart rate and arterial blood flow: an endothelial nitric oxide synthase-dependent mechanism altered during diabetes publication-title: Diabetes doi: 10.2337/db07-0115 – volume: 108 start-page: 1341 year: 2001 end-page: 1348 ident: CR13 article-title: Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site publication-title: J. Clin. Invest. – volume: 45 start-page: 365 year: 2017 end-page: 370 ident: CR16 article-title: OGT: a short overview of an enzyme standing out from usual glycosyltransferases publication-title: Biochem. Soc. Trans. – volume: 15 start-page: 153 year: 2005 end-page: 164 ident: CR11 article-title: Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites publication-title: Glycobiology – volume: 27 start-page: 1380 year: 1993 end-page: 1382 ident: CR4 article-title: Platelet adhesion to human vascular endothelium is modulated by constitutive and cytokine induced nitric oxide publication-title: Cardiovasc. Res. – volume: 56 start-page: 115 year: 2012 end-page: 121 ident: CR25 article-title: Activation of hexosamine pathway impairs nitric oxide (NO)-dependent arteriolar dilations by increased protein O-GlcNAcylation publication-title: Vascul. Pharmacol. doi: 10.1016/j.vph.2011.11.003 – volume: 283 start-page: 6050 year: 2008 end-page: 6057 ident: CR10 article-title: Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-Linked N-acetylglucosaminyltransferase publication-title: J. Biol. Chem. – volume: 20 start-page: 3503 year: 2014 end-page: 3513 ident: CR7 article-title: Regulation of eNOS enzyme activity by posttranslational modification publication-title: Curr. Pharm. Des. – volume: 36 start-page: 423 year: 2010 end-page: 435 ident: CR24 article-title: O-GlcNAc modification, insulin signaling and diabetic complications publication-title: Diabetes Metab. – volume: 284 start-page: 3425 year: 2009 end-page: 3432 ident: CR19 article-title: Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux publication-title: J. Biol. Chem. – volume: 537 start-page: 8 year: 2017 end-page: 12 ident: CR21 article-title: Measurement of O-GlcNAcylated endothelial nitric oxide synthase by using 2',5'-ADP-Sepharose pull-down assay publication-title: Anal. Biochem. doi: 10.1016/j.ab.2017.08.017 – volume: 99 start-page: 278 year: 1997 end-page: 287 ident: CR2 article-title: Important role of tissue angiotensin-converting enzyme activity in the pathogenesis of coronary vascular and myocardial structural changes induced by long-term blockade of nitric oxide synthesis in rats publication-title: J. Clin. Invest. – volume: 101 start-page: 676 year: 2000 end-page: 681 ident: CR28 article-title: Regulation of endothelial constitutive nitric oxide synthase gene expression in endothelial cells and in vivo a specific vascular action of insulin publication-title: Circulation – volume: 24 start-page: 839 year: 2010 end-page: 849 ident: CR14 article-title: Moderate recurrent hypoglycemia during early development leads to persistent changes in affective behavior in the rat publication-title: Brain Behav. Immun. – volume: 15 start-page: 153 year: 2005 ident: 76340_CR11 publication-title: Glycobiology doi: 10.1093/glycob/cwh151 – volume: 9 start-page: 434 year: 2017 ident: 76340_CR23 publication-title: J. Diabetes doi: 10.1111/1753-0407.12521 – volume: 17 start-page: 273 year: 2017 ident: 76340_CR29 publication-title: Am. J. Cardiovasc. Drugs doi: 10.1007/s40256-017-0220-9 – volume: 283 start-page: 13009 year: 2008 ident: 76340_CR9 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M801222200 – volume: 99 start-page: 278 year: 1997 ident: 76340_CR2 publication-title: J. Clin. Invest. doi: 10.1172/JCI119156 – volume: 60 start-page: 3 year: 2017 ident: 76340_CR15 publication-title: Diabetologia doi: 10.1007/s00125-016-4146-6 – volume: 284 start-page: 3425 year: 2009 ident: 76340_CR19 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M803198200 – volume: 289 start-page: 10592 year: 2014 ident: 76340_CR17 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.523068 – volume: 102 start-page: 11870 year: 2005 ident: 76340_CR12 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0502488102 – volume: 61 start-page: 2993 year: 2012 ident: 76340_CR6 publication-title: Diabetes doi: 10.2337/db12-0224 – volume: 56 start-page: 2872 year: 2007 ident: 76340_CR5 publication-title: Diabetes doi: 10.2337/db07-0115 – volume: 2005 start-page: 13 year: 2005 ident: 76340_CR22 publication-title: Sci. STKE doi: 10.1126/stke.3122005re13 – volume: 36 start-page: 423 year: 2010 ident: 76340_CR24 publication-title: Diabetes Metab. doi: 10.1016/j.diabet.2010.09.001 – volume: 283 start-page: 6050 year: 2008 ident: 76340_CR10 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M707328200 – volume: 24 start-page: 839 year: 2010 ident: 76340_CR14 publication-title: Brain Behav. Immun. doi: 10.1016/j.bbi.2009.11.013 – volume: 106 start-page: 466 year: 2002 ident: 76340_CR27 publication-title: Circulation doi: 10.1161/01.cir.0000023043.02648.51 – volume: 537 start-page: 8 year: 2017 ident: 76340_CR21 publication-title: Anal. Biochem. doi: 10.1016/j.ab.2017.08.017 – volume: 27 start-page: 1380 year: 1993 ident: 76340_CR4 publication-title: Cardiovasc. Res. doi: 10.1093/cvr/27.7.1380 – volume: 10 start-page: 186 year: 2019 ident: 76340_CR30 publication-title: Front. Physiol. doi: 10.3389/fphys.2019.00186 – volume: 108 start-page: 1341 year: 2001 ident: 76340_CR13 publication-title: J. Clin. Invest. doi: 10.1172/JCI11235 – volume: 45 start-page: 365 year: 2017 ident: 76340_CR16 publication-title: Biochem. Soc. Trans. doi: 10.1042/BST20160404 – volume: 101 start-page: 676 year: 2000 ident: 76340_CR28 publication-title: Circulation doi: 10.1161/01.CIR.101.6.676 – volume: 284 start-page: 34777 year: 2009 ident: 76340_CR18 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.026351 – volume: 26 start-page: 917 year: 2017 ident: 76340_CR1 publication-title: Antioxid. Redox Signal doi: 10.1089/ars.2016.6904 – volume: 6 start-page: 241 year: 2000 ident: 76340_CR3 publication-title: Tissue Eng. doi: 10.1089/10763270050044425 – volume: 274 start-page: 32015 year: 1999 ident: 76340_CR20 publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.45.32015 – volume: 407 start-page: 233 year: 2000 ident: 76340_CR26 publication-title: Nature doi: 10.1038/35025203 – volume: 472 start-page: 230 year: 2011 ident: 76340_CR8 publication-title: Nature doi: 10.1038/nature09932 – volume: 56 start-page: 115 year: 2012 ident: 76340_CR25 publication-title: Vascul. Pharmacol. doi: 10.1016/j.vph.2011.11.003 – volume: 20 start-page: 3503 year: 2014 ident: 76340_CR7 publication-title: Curr. Pharm. Des. doi: 10.2174/13816128113196660745
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SubjectTerms	631/45 631/45/320 692/4019 692/4019/592 Acylation Animals Aorta Cattle Cell culture Endothelial cells Endothelial Cells - enzymology Glucose Glucose - metabolism Glucose - pharmacology HEK293 Cells High-performance liquid chromatography Humanities and Social Sciences Humans Immunoblotting Immunoprecipitation Liquid chromatography multidisciplinary Mutation Nitric oxide Nitric Oxide Synthase Type III - metabolism Nitric-oxide synthase O-GlcNAcylation Phosphorylation Post-translation Protein Processing, Post-Translational Rats Science Science (multidisciplinary) Serine Thorax Translation Variance analysis
Title	Regulation of O-GlcNAcylation on endothelial nitric oxide synthase by glucose deprivation and identification of its O-GlcNAcylation sites
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