Involvement of NDPK-B in glucose metabolism-mediated endothelial damage via activation of the hexosamine biosynthesis pathway and suppression of O-GlcNAcase activity
Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP). Herein, we investigated how NDPK-B is invol...
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| Hauptverfasser: | , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
19 October 2020
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| In: |
Cells
Year: 2020, Jahrgang: 9, Heft: 10 |
| ISSN: | 2073-4409 |
| DOI: | 10.3390/cells9102324 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3390/cells9102324 Verlag, lizenzpflichtig, Volltext: https://www.mdpi.com/2073-4409/9/10/2324 
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| Verfasserangaben: | Anupriya Chatterjee, Rachana Eshwaran, Gernot Poschet, Santosh Lomada, Mahmoud Halawa, Kerstin Wilhelm, Martina Schmidt, Hans-Peter Hammes, Thomas Wieland and Yuxi Feng |
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| 245 | 1 | 0 | |a Involvement of NDPK-B in glucose metabolism-mediated endothelial damage via activation of the hexosamine biosynthesis pathway and suppression of O-GlcNAcase activity |c Anupriya Chatterjee, Rachana Eshwaran, Gernot Poschet, Santosh Lomada, Mahmoud Halawa, Kerstin Wilhelm, Martina Schmidt, Hans-Peter Hammes, Thomas Wieland and Yuxi Feng |
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| 520 | |a Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP). Herein, we investigated how NDPK-B is involved in the HBP in endothelial cells (ECs). The activities of NDPK-B and O-GlcNAcase (OGA) were measured by in vitro assays. Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively. Re-expression of NDPK-B was achieved with recombinant adenoviruses. Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment. Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed. Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs. Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels. However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation. NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2. The data indicate a critical role of NDPK-B in endothelial damage via the modulation of the HBP. | ||
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