Chk1 and Hsp90 cooperatively regulate phosphorylation of endothelial nitric oxide synthase at serine 1179
The effects of DNA damage on NO production have not been completely elucidated. Using ultraviolet (UV) irradiation as a DNA-damaging agent, we studied its effect on NO production in bovine aortic endothelial cells (BAEC). UV irradiation acutely increased NO production, the phosphorylation of endothe...
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Published in | Free radical biology & medicine Vol. 51; no. 12; pp. 2217 - 2226 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
15.12.2011
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Abstract | The effects of DNA damage on NO production have not been completely elucidated. Using ultraviolet (UV) irradiation as a DNA-damaging agent, we studied its effect on NO production in bovine aortic endothelial cells (BAEC). UV irradiation acutely increased NO production, the phosphorylation of endothelial NO synthase (eNOS) at serine 1179, and eNOS activity. No alterations in eNOS expression nor phosphorylation at eNOS Thr497 or eNOS Ser116 were found. SB218078, a checkpoint kinase 1 (Chk1) inhibitor, inhibited UV-irradiation-stimulated eNOS-Ser1179 phosphorylation and NO production. Similarly, ectopic expression of small interference RNA for Chk1 or a dominant-negative Chk1 repressed the UV-irradiation stimulatory effect, whereas wild-type Chk1 increased basal eNOS-Ser1179 phosphorylation. Purified Chk1 directly phosphorylated eNOS Ser1179 in vitro. Confocal microscopy and coimmunoprecipitation studies revealed a colocalization of eNOS and Chk1. In basal BAEC, heat shock protein 90 (Hsp90) predominantly interacted with Chk1. This interaction, which decreased significantly in response to UV irradiation, was accompanied by increased interaction of Hsp90 with eNOS. The Hsp90 inhibitor geldanamycin attenuated UV-irradiation-stimulated eNOS-Ser1179 phosphorylation by dissociating Hsp90 from eNOS. UV irradiation and geldanamycin did not alter the interaction between eNOS and Chk1. Overall, this is the first study demonstrating that Chk1 directly phosphorylates eNOS Ser1179 in response to UV irradiation, which is dependent on Hsp90 interaction.
► UV irradiation increases NO production and eNOS activity by p-eNOS-Ser1179 in EC. ► Chk1 mediates p-eNOS-Ser1179 in response to UV irradiation. ► UV irradiation increases Hsp90/eNOS binding, but decreases its binding to Chk1. ► Increased NO by UV irradiation induces apoptosis of EC. |
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AbstractList | The effects of DNA damage on NO production have not been completely elucidated. Using ultraviolet (UV) irradiation as a DNA-damaging agent, we studied its effect on NO production in bovine aortic endothelial cells (BAEC). UV irradiation acutely increased NO production, the phosphorylation of endothelial NO synthase (eNOS) at serine 1179, and eNOS activity. No alterations in eNOS expression nor phosphorylation at eNOS Thr497 or eNOS Ser116 were found. SB218078, a checkpoint kinase 1 (Chk1) inhibitor, inhibited UV-irradiation-stimulated eNOS-Ser1179 phosphorylation and NO production. Similarly, ectopic expression of small interference RNA for Chk1 or a dominant-negative Chk1 repressed the UV-irradiation stimulatory effect, whereas wild-type Chk1 increased basal eNOS-Ser1179 phosphorylation. Purified Chk1 directly phosphorylated eNOS Ser1179 in vitro. Confocal microscopy and coimmunoprecipitation studies revealed a colocalization of eNOS and Chk1. In basal BAEC, heat shock protein 90 (Hsp90) predominantly interacted with Chk1. This interaction, which decreased significantly in response to UV irradiation, was accompanied by increased interaction of Hsp90 with eNOS. The Hsp90 inhibitor geldanamycin attenuated UV-irradiation-stimulated eNOS-Ser1179 phosphorylation by dissociating Hsp90 from eNOS. UV irradiation and geldanamycin did not alter the interaction between eNOS and Chk1. Overall, this is the first study demonstrating that Chk1 directly phosphorylates eNOS Ser1179 in response to UV irradiation, which is dependent on Hsp90 interaction.
► UV irradiation increases NO production and eNOS activity by p-eNOS-Ser1179 in EC. ► Chk1 mediates p-eNOS-Ser1179 in response to UV irradiation. ► UV irradiation increases Hsp90/eNOS binding, but decreases its binding to Chk1. ► Increased NO by UV irradiation induces apoptosis of EC. The effects of DNA damage on NO production have not been completely elucidated. Using ultraviolet (UV) irradiation as a DNA-damaging agent, we studied its effect on NO production in bovine aortic endothelial cells (BAEC). UV irradiation acutely increased NO production, the phosphorylation of endothelial NO synthase (eNOS) at serine 1179, and eNOS activity. No alterations in eNOS expression nor phosphorylation at eNOS Thr(497) or eNOS Ser(116) were found. SB218078, a checkpoint kinase 1 (Chk1) inhibitor, inhibited UV-irradiation-stimulated eNOS-Ser(1179) phosphorylation and NO production. Similarly, ectopic expression of small interference RNA for Chk1 or a dominant-negative Chk1 repressed the UV-irradiation stimulatory effect, whereas wild-type Chk1 increased basal eNOS-Ser(1179) phosphorylation. Purified Chk1 directly phosphorylated eNOS Ser(1179) in vitro. Confocal microscopy and coimmunoprecipitation studies revealed a colocalization of eNOS and Chk1. In basal BAEC, heat shock protein 90 (Hsp90) predominantly interacted with Chk1. This interaction, which decreased significantly in response to UV irradiation, was accompanied by increased interaction of Hsp90 with eNOS. The Hsp90 inhibitor geldanamycin attenuated UV-irradiation-stimulated eNOS-Ser(1179) phosphorylation by dissociating Hsp90 from eNOS. UV irradiation and geldanamycin did not alter the interaction between eNOS and Chk1. Overall, this is the first study demonstrating that Chk1 directly phosphorylates eNOS Ser(1179) in response to UV irradiation, which is dependent on Hsp90 interaction. |
Author | Kwon, Young-Guen Jo, Inho Park, Min-Ha Kim, Wuon-Shik Yun, Cheol-Won Park, Jung-Hyun Kim, Jin Yi Nam, Jae-Hwan |
Author_xml | – sequence: 1 givenname: Jung-Hyun surname: Park fullname: Park, Jung-Hyun organization: Department of Molecular Medicine and Ewha Medical Research Institute, Ewha Womans University Medical School, Seoul 158–710, Korea – sequence: 2 givenname: Wuon-Shik surname: Kim fullname: Kim, Wuon-Shik organization: Center for Medical Measurements, Division of Convergence Technology, Korea Research Institute of Standards and Science, Daejeon 305–340, Korea – sequence: 3 givenname: Jin Yi surname: Kim fullname: Kim, Jin Yi organization: Department of Biochemistry, College of Life Sciences and Biotechnology, Yonsei University, Seoul 120–749, Korea – sequence: 4 givenname: Min-Ha surname: Park fullname: Park, Min-Ha organization: Department of Molecular Medicine and Ewha Medical Research Institute, Ewha Womans University Medical School, Seoul 158–710, Korea – sequence: 5 givenname: Jae-Hwan surname: Nam fullname: Nam, Jae-Hwan organization: Department of Biotechnology, The Catholic University of Korea, Bucheon 420–743, Korea – sequence: 6 givenname: Cheol-Won surname: Yun fullname: Yun, Cheol-Won organization: Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136–701, Korea – sequence: 7 givenname: Young-Guen surname: Kwon fullname: Kwon, Young-Guen organization: Department of Biochemistry, College of Life Sciences and Biotechnology, Yonsei University, Seoul 120–749, Korea – sequence: 8 givenname: Inho surname: Jo fullname: Jo, Inho email: inhojo@ewha.ac.kr organization: Department of Molecular Medicine and Ewha Medical Research Institute, Ewha Womans University Medical School, Seoul 158–710, Korea |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22001744$$D View this record in MEDLINE/PubMed |
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Keywords | Checkpoint kinase UV eNOS L-NAME Phosphorylation Free radicals VEGF PKA DN UV irradiation Chk1 Hsp90 Endothelial nitric oxide synthase CaMKII CPD Heat shock protein AMPK WT EC |
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Snippet | The effects of DNA damage on NO production have not been completely elucidated. Using ultraviolet (UV) irradiation as a DNA-damaging agent, we studied its... |
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SubjectTerms | Alkaloids - pharmacology Animals Cattle Cells, Cultured Checkpoint kinase Checkpoint Kinase 1 Endothelial nitric oxide synthase Free radicals Heat shock protein HSP90 Heat-Shock Proteins - metabolism Nitric Oxide - biosynthesis Nitric Oxide Synthase Type III - metabolism Phosphorylation Phosphorylation - drug effects Protein Kinases - metabolism Serine - metabolism Ultraviolet Rays UV irradiation |
Title | Chk1 and Hsp90 cooperatively regulate phosphorylation of endothelial nitric oxide synthase at serine 1179 |
URI | https://dx.doi.org/10.1016/j.freeradbiomed.2011.09.021 https://www.ncbi.nlm.nih.gov/pubmed/22001744 https://search.proquest.com/docview/906155100 |
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