Herr 2007 Cell Mol Life Sci: Difference between revisions
No edit summary |
Bader Helga (talk | contribs) No edit summary Β |
||
| (7 intermediate revisions by 5 users not shown) | |||
| Line 1: | Line 1: | ||
{{Publication | {{Publication | ||
|title=Herr B, Zhou J, DrΓΆse S, BrΓΌne B (2007) The interaction of superoxide with nitric oxide destabilizes hypoxia-inducible factor-1alpha. Cell Mol Life Sci | |title=Herr B, Zhou J, DrΓΆse S, BrΓΌne B (2007) The interaction of superoxide with nitric oxide destabilizes hypoxia-inducible factor-1alpha. Cell Mol Life Sci 64:3295-305. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17989922 PMID: 17989922 ] | |||
|authors=Herr B, Zhou J, Droese S, Bruene B | |authors=Herr B, Zhou J, Droese S, Bruene B | ||
|year=2007 | |year=2007 | ||
|journal=Cell Mol Life Sci | |journal=Cell Mol Life Sci | ||
|abstract=In renal carcinoma cells (RCC4) hypoxia inducible factor-1 (HIF-1) is constitutively expressed due to a von Hippel Lindau protein deficiency, but can be degraded by calpain, independently of the 26S proteasome, when exposed to hypoxia/nitric oxide (NO). In this study we examined molecular mechanisms to explain calpain activation. The inability of hypoxia/NO to degrade HIF-1Ξ± in respiratory-deficient RCC4-Ο0 cells pointed to the requirement for mitochondria-derived reactive oxygen species. A prerequisite for O<sub>2</sub>Β βΒ in combination with NO to destabilize HIF-1Ξ± was corroborated in RCC4-p0 cells, when the redox cycler 2,3-dimethoxy-1,4-naphthoquinone was used as a source of superoxide. Degradation of HIF-1Ξ± required intracellular calcium transients and calpain activation. Using uric acid to interfere with signal transmission elicited by NO/O<sub>2</sub>Β βΒ blocked HIF-1Ξ± degradation and attenuated a calcium increase. We conclude that an oxidative signal as a result of NO/O<sub>2</sub>Β βΒ coformation triggers a calcium increase that activates calpain to degrade HIF-1Ξ±, independently of the proteasome. | |abstract=In renal carcinoma cells (RCC4) hypoxia inducible factor-1 (HIF-1) is constitutively expressed due to a von Hippel Lindau protein deficiency, but can be degraded by calpain, independently of the 26S proteasome, when exposed to hypoxia/nitric oxide (NO). In this study we examined molecular mechanisms to explain calpain activation. The inability of hypoxia/NO to degrade HIF-1Ξ± in respiratory-deficient RCC4-Ο0 cells pointed to the requirement for mitochondria-derived reactive oxygen species. A prerequisite for O<sub>2</sub>Β βΒ in combination with NO to destabilize HIF-1Ξ± was corroborated in RCC4-p0 cells, when the redox cycler 2,3-dimethoxy-1,4-naphthoquinone was used as a source of superoxide. Degradation of HIF-1Ξ± required intracellular calcium transients and calpain activation. Using uric acid to interfere with signal transmission elicited by NO/O<sub>2</sub>Β βΒ blocked HIF-1Ξ± degradation and attenuated a calcium increase. We conclude that an oxidative signal as a result of NO/O<sub>2</sub>Β βΒ coformation triggers a calcium increase that activates calpain to degrade HIF-1Ξ±, independently of the proteasome. | ||
|keywords=HIF-1Ξ±, Nitric oxide, Oxygen radicals, Calcium, Calpain, Mitochondria | |keywords=HIF-1Ξ±, Nitric oxide, Oxygen radicals, Calcium, Calpain, Mitochondria | ||
| | |mipnetlab=DE Frankfurt Droese S | ||
|discipline=Mitochondrial Physiology, Biomedicine | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|injuries=Oxidative stress;RONS | |||
|couplingstates=OXPHOS | |||
|instruments=Oxygraph-2k | |||
|discipline=Mitochondrial Physiology, Biomedicine | |discipline=Mitochondrial Physiology, Biomedicine | ||
}} | }} | ||
Latest revision as of 16:32, 23 February 2015
| Herr B, Zhou J, DrΓΆse S, BrΓΌne B (2007) The interaction of superoxide with nitric oxide destabilizes hypoxia-inducible factor-1alpha. Cell Mol Life Sci 64:3295-305. |
Herr B, Zhou J, Droese S, Bruene B (2007) Cell Mol Life Sci
Abstract: In renal carcinoma cells (RCC4) hypoxia inducible factor-1 (HIF-1) is constitutively expressed due to a von Hippel Lindau protein deficiency, but can be degraded by calpain, independently of the 26S proteasome, when exposed to hypoxia/nitric oxide (NO). In this study we examined molecular mechanisms to explain calpain activation. The inability of hypoxia/NO to degrade HIF-1Ξ± in respiratory-deficient RCC4-Ο0 cells pointed to the requirement for mitochondria-derived reactive oxygen species. A prerequisite for O2 β in combination with NO to destabilize HIF-1Ξ± was corroborated in RCC4-p0 cells, when the redox cycler 2,3-dimethoxy-1,4-naphthoquinone was used as a source of superoxide. Degradation of HIF-1Ξ± required intracellular calcium transients and calpain activation. Using uric acid to interfere with signal transmission elicited by NO/O2 β blocked HIF-1Ξ± degradation and attenuated a calcium increase. We conclude that an oxidative signal as a result of NO/O2 β coformation triggers a calcium increase that activates calpain to degrade HIF-1Ξ±, independently of the proteasome. β’ Keywords: HIF-1Ξ±, Nitric oxide, Oxygen radicals, Calcium, Calpain, Mitochondria
β’ O2k-Network Lab: DE Frankfurt Droese S
Labels:
Stress:Oxidative stress;RONS
Coupling state: OXPHOS
HRR: Oxygraph-2k
