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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology. 2015;35:2366-2373, originally published September 17, 2015
https://doi.org/10.1161/ATVBAHA.115.305796

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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song, Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology November 2015, 35 (11) 2366-2373; DOI: https://doi.org/10.1161/ATVBAHA.115.305796

Figure 1.
By Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

Endothelial nitric oxide (NO) synthase (eNOS)–derived NO prevents dihydrofolate reductase (DHFR) protein red...
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Endothelial nitric oxide (NO) synthase (eNOS)–derived NO prevents dihydrofolate reductase (DHFR) protein reduction in human umbilical vein endothelial cells (HUVECs). A, eNOS silencing reduced DHFR but not GTP cyclohydrolase I (GTPCH) protein expression. B, eNOS silencing did not alter DHFR mRNA expression. C, NO scavenger 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) treatment reduced DHFR expression in a dose- (0, 75, 150, and 300 μmol/L) and a time- (0, 6, 12, 24, and 48 hours) dependent manner but had no effect on GTPCH expression. D, PTIO (150 μmol/L) had no significant effect on DHFR mRNA expression. E, NO donor S-nitroso-l-glutathione (GSNO; 100 μmol/L) reversed PTIO- (150 μmol/L) induced DHFR reduction. F, GSNO (100 μmol/L) prevents DHFR reduction induced by eNOS silencing (n=3 for each group; *P<0.05 vs scramble [Scr] siRNA in A and F or P<0.05 vs control in E; #P<0.05 vs PTIO in E or P<0.05 vs eNOS siRNA in F).
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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song, Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology November 2015, 35 (11) 2366-2373; DOI: https://doi.org/10.1161/ATVBAHA.115.305796

Figure 2.
By Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

Nitric oxide (NO) depletion promotes dihydrofolate reductase (DHFR) degradation via ubiquitin–proteasome deg...
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Nitric oxide (NO) depletion promotes dihydrofolate reductase (DHFR) degradation via ubiquitin–proteasome degradation in human umbilical vein endothelial cells. A, S-Nitroso-l-glutathione (GSNO; 100 μmol/L) supplementation prevented DHFR reduction induced by cycloheximide (CHX; 30 μg/mL) treatment. DHFR degradation induced by endothelial NO synthase (eNOS) silencing (B) or 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO; 150 μmol/L; C) could be inhibited by proteasome inhibitor, MG132 (1 μmol/L). D, PTIO- (150 μmol/L) induced DHFR polyubiquitination, which could be suppressed by GSNO (100 μmol/L; n=3; *P<0.05 vs control in A, C, and D or P<0.05 vs scramble [Scr] siRNA in B; #P<0.05 vs eNOS siRNA in B or P<0.05 vs PTIO in C and D).
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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song, Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology November 2015, 35 (11) 2366-2373; DOI: https://doi.org/10.1161/ATVBAHA.115.305796

Figure 3.
By Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

Cystein 7 is the site of S-nitrosylation of dihydrofolate reductase (DHFR). A, S-Nitroso-l-...
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Cystein 7 is the site of S-nitrosylation of dihydrofolate reductase (DHFR). A, S-Nitroso-l-glutathione (GSNO; 100 μmol/L) restored DHFR S-nitrosylation in the presence of 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO; 150 μmol/L) as determined by biotin switch assay. B, Amino acid sequence comparison of DHFR among species. C, C7S mutation blocked GSNO- (100 μmol/L) induced DHFR S-nitrosylation (n=3; *P<0.05 vs control in A or P<0.05 vs wild-type [WT] in C; #P<0.05 vs PTIO in A).
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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song, Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology November 2015, 35 (11) 2366-2373; DOI: https://doi.org/10.1161/ATVBAHA.115.305796

Figure 4.
By Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

Dihydrofolate reductase (DHFR) S-nitrosylation prevents ubiquitination and degradation. A,...
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Dihydrofolate reductase (DHFR) S-nitrosylation prevents ubiquitination and degradation. A, C7S mutation in DHFR destabilized the protein compared with the wild-type (WT) DHFR treated with cycloheximide (CHX; 30 μg/mL). S-Nitroso-l-glutathione (GSNO; 100 μmol/L) stabilized DHFR, whereas the C7S mutation abolished the effect. B, GSNO (100 μmol/L) restored DHFR S-nitrosylation, which was suppressed by 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO; 150 μmol/L). Dithiothreitol (DTT; 10 mmol/L) inhibited the effect of GSNO (100 μmol/L). C and D, GSNO (100 μmol/L) prevented DHFR ubiquitination and degradation induced by PTIO (150 μmol/L); this effect could be blocked by DTT (10 mmol/L) supplementation. E, PTIO (150 μmol/L) promoted 26S proteasome activity, which could be reversed by GSNO (100 μmol/L). The addition of DTT (10 mmol/L) did not affect 26S proteasome activity compared with the PTIO+GSNO group (n=3; *P<0.05 vs WT in A or P<0.05 vs control in B–E; #P<0.05 vs C7S in A or P<0.05 vs PTIO in B–E; $P<0.05 vs PTIO+GSNO in B–D).
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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song, Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology November 2015, 35 (11) 2366-2373; DOI: https://doi.org/10.1161/ATVBAHA.115.305796

Figure 5.
By Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

2-(4-Carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) reduces aortic endothelial dihydrof...
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2-(4-Carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) reduces aortic endothelial dihydrofolate reductase (DHFR) expression and BH₄ content via proteasomal degradation ex vivo. A, Western blot analysis showed reduced DHFR expression in PTIO- (150 μmol/L) treated aortas, which could be blocked by MG132 (1 μmol/L, 6 hours) supplementation. B, Representative immunofluorescence staining of DHFR (red) and endothelium marker CD31 (green) of ex vivo cultured aortas. C, PTIO (150 μmol/L) reduced endothelial DHFR expression, whereas MG132 (1 μmol/L, 6 hours) reversed the effect. D, Representative immunofluorescence staining of GTP cyclohydrolase I (GTPCH; red) and endothelium marker CD31 (green) of ex vivo cultured aortas. E, PTIO (150 μmol/L) had no significant effect on endothelial GTPCH expression. F, PTIO (150 μmol/L) reduced BH₄ content, which could be reversed by addition of MG132 (1 μmol/L, 6 hours) in aortas ex vivo (n=4 for each group; *P<0.05 vs control; #P<0.05 vs PTIO).
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Endothelial Nitric Oxide Synthase–Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-NitrosylationSignificance
Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song, Ming-Hui Zou

Arteriosclerosis, Thrombosis, and Vascular Biology November 2015, 35 (11) 2366-2373; DOI: https://doi.org/10.1161/ATVBAHA.115.305796

Figure 6.
By Zhejun Cai, Qiulun Lu, Ye Ding, Qilong Wang, Lei Xiao, Ping Song and Ming-Hui Zou

MG132 prevents aortic endothelial dihydrofolate reductase (DHFR) expression and BH₄ content in en...
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MG132 prevents aortic endothelial dihydrofolate reductase (DHFR) expression and BH₄ content in endothelial nitric oxide synthase (eNOS^−/−) mice. A, Representative immunofluorescence staining of DHFR (red) and endothelium marker CD31 (green) of aortas from mice received indicated treatment. B, MG132 (5 mg/kg per day, 3 days) suppressed endothelial DHFR reduction in eNOS^−/− mice. C, Representative immunofluorescence staining of GTP cyclohydrolase I (GTPCH; red) and endothelium marker CD31 (green) of aortas from indicated treated mice. D, eNOS deficiency had no significant effect on endothelial GTPCH expression. E, Supplementation of MG132 (5 mg/kg per day, 3 days) suppressed aortic BH₄ content reduction in eNOS^−/− mice (n=5 for each group; *P<0.05 vs wild-type [WT]; #P<0.05 vs eNOS^−/−).
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Fractalkine Upregulates Intercellular Adhesion Molecule-1 in Endothelial Cells Through CX3CR1 and the Jak–Stat5 Pathway
Xiao Ping Yang, Subhendra Mattagajasingh, Shaobo Su, Guibin Chen, Zheqing Cai, Karen Fox-Talbot, Kaikobad Irani, Lewis C. Becker

Circulation Research November 2007, 101 (10) 1001-1008; DOI: https://doi.org/10.1161/CIRCRESAHA.107.160812

By Xiao Ping Yang, Subhendra Mattagajasingh, Shaobo Su, Guibin Chen, Zheqing Cai, Karen Fox-Talbot, Kaikobad Irani and Lewis C. Becker

Figure 1. a, Hypoxia/reoxygenation increases the expression of FKN protein in ECs. Cultured HCAECs and HUVECs were exposed to hypoxia for 2 hours and...Show More

Figure 1. a, Hypoxia/reoxygenation increases the expression of FKN protein in ECs. Cultured HCAECs and HUVECs were exposed to hypoxia for 2 hours and reoxygenation for up to 120 minutes. Western blots showed an increase in FKN protein in EC lysates beginning within 10 minutes of reoxygenation and continuing for at least 120 minutes. HUVECs were seeded into 12-well plates and grown to 100% confluence (lower left). For each time point of normoxia or hypoxia/reoxygenation, medium was harvested from 2 wells, pooled (600 μL), concentrated to ≈30 μL, and completely loaded on the gel in the appropriate lane. FKN in the media, representing the lower-molecular-weight s-FKN, increased within 15 minutes of reoxygenation and peaked at 30 minutes. b, s-FKN increases ICAM-1 mRNA in ECs. HUVECs were exposed to s-FKN for the indicated doses and times. Cells were harvested, total RNA was isolated, and real-time RT-PCR was performed for quantitation of ICAM-1 mRNA. ICAM-1 mRNA increased in a dose-dependent (top) and time-dependent (bottom) fashion.Show Less
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Fractalkine Upregulates Intercellular Adhesion Molecule-1 in Endothelial Cells Through CX3CR1 and the Jak–Stat5 Pathway
Xiao Ping Yang, Subhendra Mattagajasingh, Shaobo Su, Guibin Chen, Zheqing Cai, Karen Fox-Talbot, Kaikobad Irani, Lewis C. Becker

Circulation Research November 2007, 101 (10) 1001-1008; DOI: https://doi.org/10.1161/CIRCRESAHA.107.160812

By Xiao Ping Yang, Subhendra Mattagajasingh, Shaobo Su, Guibin Chen, Zheqing Cai, Karen Fox-Talbot, Kaikobad Irani and Lewis C. Becker

Figure 2. s-FKN upregulates ICAM-1 protein in the intact mouse heart. Hearts were perfused with or without 50 ng/mL mouse s-FKN for 3 hours. a, Wester...Show More

Figure 2. s-FKN upregulates ICAM-1 protein in the intact mouse heart. Hearts were perfused with or without 50 ng/mL mouse s-FKN for 3 hours. a, Western blots were done with goat anti-mouse ICAM-1 antibody. b and c, Immunohistology shows that ICAM-1 is upregulated in capillary endothelium (brown stain) following perfusion with s-FKN compared with perfusion with control buffer. Image magnification for b and c, ×160. IB indicates immunoblotting.Show Less
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Fractalkine Upregulates Intercellular Adhesion Molecule-1 in Endothelial Cells Through CX3CR1 and the Jak–Stat5 Pathway
Xiao Ping Yang, Subhendra Mattagajasingh, Shaobo Su, Guibin Chen, Zheqing Cai, Karen Fox-Talbot, Kaikobad Irani, Lewis C. Becker

Circulation Research November 2007, 101 (10) 1001-1008; DOI: https://doi.org/10.1161/CIRCRESAHA.107.160812

By Xiao Ping Yang, Subhendra Mattagajasingh, Shaobo Su, Guibin Chen, Zheqing Cai, Karen Fox-Talbot, Kaikobad Irani and Lewis C. Becker

Figure 3. Vascular ECs express the FKN receptor CX3CR1. a, The cellular lysates from cultured HCAECs and HUVECs and fresh human leukocytes were used f...Show More

Figure 3. Vascular ECs express the FKN receptor CX3CR1. a, The cellular lysates from cultured HCAECs and HUVECs and fresh human leukocytes were used for Western blots, using anti-human FKN and CX3CR1 antibodies. Both types of ECs (left 2 lanes) express both FKN and CX3CR1. Macrophages and neutrophils express CX3CR1 but not FKN itself. CX3CR1 in ECs has two 50-kDa bands as well as a 40-kDa band. Macrophages (MΦ) (fourth lane) express only a 40-kDa CX3CR1 protein, and neutrophils (PMNs) (right lane) also express it but in lesser amounts. b, RT-PCR assay for CX3CR1 mRNA. A pair of primers from the V28 cDNA sequence–spanning exons 2 and 4 was used to amplify reverse transcript products from total RNA from ECs and leukocytes. The RT-PCR products were run on 5% polyacrylamide gel and stained with ethidium bromide. ECs and leukocytes both express CX3CR1 mRNA. However, PMNs express less than ECs and MΦ. c, Confocal microscopic images of an HUVEC. Cultured HUVECs were fixed with methanol, blocked with goat serum, and incubated with anti-human CX3CR1 antibody. After washing, cells were incubated with secondary antibody labeled with green fluorescence. Top, Confocal scan sections of a single HUVEC. Bottom, Image of a single-scan section (2.24 μm) through the cell. The green staining, representing CX3CR1, is located primarily on the cell membrane and partially extends to the cytoplasm. The nucleus is stained blue with DAPI (2′,6′-diamidino-2-phenylindole).Show Less