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Conference Paper: Plant natural product puerarin suppressed 6-hydroxydopamine (6-OHDA)-induced neurotoxicity via inducing mitochondrial enzyme arginase-2
Title | Plant natural product puerarin suppressed 6-hydroxydopamine (6-OHDA)-induced neurotoxicity via inducing mitochondrial enzyme arginase-2 |
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Authors | |
Issue Date | 2015 |
Citation | The 27th International Symposium on Cerebral Blood Flow, Metabolism and Function & 12th International Conference on Quantification of Brain Function with PET, Vancouver, Canada, 27-30 June 2015. How to Cite? |
Abstract | Aberrant production of nitric oxide (NO) is implicated in the progression of neurodegenerative diseases. The aim of the present study was to explore whether plant natural product puerarin could attenuate nitric oxide (NO)-mediated neurotoxicity via modulating the enzymes in the L-arginine-NO pathway. Neurotoxin 6-hydroxydopamine (6-OHDA) is well known to induce neurodegeneration via a NO-dependent mechanism. We first validated that puerarin protected rat dopamingeric PC12 cells against 6-OHDA-induced neurotoxicity in a concentration-dependent manner. We subsequently profiled the cellular responses to puerarin by a proteomic response fingerprinting approach. A total of sixteen protein spots with > 1.5-fold change of intensity were selected and identified by mass spectrometry. As one of puerarin-upregulated proteins, mitochondrial arginase-2 hydrolyzes L-arginine to L-ornithine, thereby competing with neuronal NOS for substrate L-arginine in mitochondria. Thus, we hypothesize that puerain may attenuate nitric oxide (NO)-mediated mitochondrial injury via increasing arginase-2 expression. Western blot and RT-PCR analyses confirmed that puerarin increased arginase-2 expression in a concentration- and time-dependent manner. Accordingly, puerarin suppressed 6-OHDA-induced NO production and neurotoxicity in PC12 cells and primary rat midbrain neurons. Arginase inhibitor BEC diminished the effect of puerarin on 6-OHDA-induced NO production and neurotoxicity. The activation of arginase-2 by puerarin represents an endogenous mechanism for specific control of NO-mediated mitochondrial damage. Thus, puerarin is useful lead for suppressing NO-mediated neurotoxicity in neurodegenerative diseases. |
Description | Poster - Late Breaking Abstracts: no. 905 |
Persistent Identifier | http://hdl.handle.net/10722/215716 |
DC Field | Value | Language |
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dc.contributor.author | Zhao, J | - |
dc.contributor.author | Lao, L | - |
dc.contributor.author | Rong, J | - |
dc.date.accessioned | 2015-08-21T13:36:21Z | - |
dc.date.available | 2015-08-21T13:36:21Z | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | The 27th International Symposium on Cerebral Blood Flow, Metabolism and Function & 12th International Conference on Quantification of Brain Function with PET, Vancouver, Canada, 27-30 June 2015. | - |
dc.identifier.uri | http://hdl.handle.net/10722/215716 | - |
dc.description | Poster - Late Breaking Abstracts: no. 905 | - |
dc.description.abstract | Aberrant production of nitric oxide (NO) is implicated in the progression of neurodegenerative diseases. The aim of the present study was to explore whether plant natural product puerarin could attenuate nitric oxide (NO)-mediated neurotoxicity via modulating the enzymes in the L-arginine-NO pathway. Neurotoxin 6-hydroxydopamine (6-OHDA) is well known to induce neurodegeneration via a NO-dependent mechanism. We first validated that puerarin protected rat dopamingeric PC12 cells against 6-OHDA-induced neurotoxicity in a concentration-dependent manner. We subsequently profiled the cellular responses to puerarin by a proteomic response fingerprinting approach. A total of sixteen protein spots with > 1.5-fold change of intensity were selected and identified by mass spectrometry. As one of puerarin-upregulated proteins, mitochondrial arginase-2 hydrolyzes L-arginine to L-ornithine, thereby competing with neuronal NOS for substrate L-arginine in mitochondria. Thus, we hypothesize that puerain may attenuate nitric oxide (NO)-mediated mitochondrial injury via increasing arginase-2 expression. Western blot and RT-PCR analyses confirmed that puerarin increased arginase-2 expression in a concentration- and time-dependent manner. Accordingly, puerarin suppressed 6-OHDA-induced NO production and neurotoxicity in PC12 cells and primary rat midbrain neurons. Arginase inhibitor BEC diminished the effect of puerarin on 6-OHDA-induced NO production and neurotoxicity. The activation of arginase-2 by puerarin represents an endogenous mechanism for specific control of NO-mediated mitochondrial damage. Thus, puerarin is useful lead for suppressing NO-mediated neurotoxicity in neurodegenerative diseases. | - |
dc.language | eng | - |
dc.relation.ispartof | Brain & Brain Pet 2015 | - |
dc.title | Plant natural product puerarin suppressed 6-hydroxydopamine (6-OHDA)-induced neurotoxicity via inducing mitochondrial enzyme arginase-2 | - |
dc.type | Conference_Paper | - |
dc.identifier.email | Lao, L: lxlao1@hku.hk | - |
dc.identifier.email | Rong, J: jrong@hku.hk | - |
dc.identifier.authority | Lao, L=rp01784 | - |
dc.identifier.authority | Rong, J=rp00515 | - |
dc.identifier.hkuros | 247201 | - |