HDAC9: Difference between revisions
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Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.<ref name="entrez"/> |
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.<ref name="entrez"/> |
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| ⚫ | |||
| ⚫ | Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined. |
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| ⚫ | HDAC9 and BCL2L11 were upregulated while miR-92a was downregulated in IA clinical samples and rat models. HDAC9 inhibition or miR-92a elevation improved pathological changes and repressed apoptosis and expression of MMP-2, MMP-9, VEGF and inflammatory factors in vascular tissues from IA rats. Oppositely, HDAC9 overexpression or miR-92a reduction had contrary effects. miR-92a downregulation reversed the effect of silenced HDAC9 on IA rats. |
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| ⚫ | Conclusion: HDAC9 inhibition upregulates miR-92a to repress the progression of IA via silencing BCL2L11.* {{cite journal | vauthors = Cai Y, Huang D, Ma W, Wang M, Qin Q, Jiang Z, Liu M | title = Histone deacetylase 9 inhibition upregulates microRNA-92a to repress the progression of intracranial aneurysm via silencing Bcl-2-like protein 11 | journal = Journal of Drug Targeting | volume = 29 | issue = 7 | pages = 761–770 | date = August 2021 | pmid = 33480300 | doi = 10.1080/1061186X.2021.1878365 }} |
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Data partially confirmed earlier results and showed that variants in CDKN2B-AS1, RP1, and HDAC9 could be genetic susceptibility factors for IA in a Chinese population.<ref>{{cite journal | vauthors = Li B, Hu C, Liu J, Liao X, Xun J, Xiao M, Yan J | title = Associations among Genetic Variants and Intracranial Aneurysm in a Chinese Population | journal = Yonsei Medical Journal | volume = 60 | issue = 7 | pages = 651–658 | date = July 2019 | pmid = 31250579 | doi = 10.3349/ymj.2019.60.7.651 }}</ref> |
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| ⚫ | Yang et al.<ref name="pmid25760078">{{cite journal | vauthors = Yang R, Wu Y, Wang M, Sun Z, Zou J, Zhang Y, Cui H | title = HDAC9 promotes glioblastoma growth via TAZ-mediated EGFR pathway activation | journal = Oncotarget | volume = 6 | issue = 10 | pages = 7644–56 | date = April 2015 | pmid = 25760078 | pmc = 4480706 | doi = 10.18632/oncotarget.3223 | url = }}</ref> found that HDAC9 is over-expressed in prognostically poor glioblastoma patients. Knockdown HDAC9 decreased proliferation in vitro and tumor formation in vivo. HDAC9 accelerated cell cycle in part by potentiating the EGFR signaling pathway. Also, HDAC9 interacted with TAZ, a key downstream effector of Hippo pathway. Knockdown of HDAC9 decreased the expression of TAZ. We found that overexpressed TAZ in HDAC9-knockdown cells abrogated the effects induced by HDAC9 silencing both in vitro and in vivo. We demonstrated that HDAC9 promotes tumor formation of glioblastoma via TAZ-mediated EGFR pathway activation, and provide the evidence for promising target for the treatment of glioblastoma 3). |
||
| ⚫ | HDAC9 was suggested to contribute to developmental delay in Saethre-Chotzen syndrome (SCS) patients with 7p21 mirodeletions 4).<ref>{{cite journal | vauthors = Shimbo H, Oyoshi T, Kurosawa K | title = Contiguous gene deletion neighboring TWIST1 identified in a patient with Saethre-Chotzen syndrome associated with neurodevelopmental delay: Possible contribution of HDAC9 | journal = Congenital Anomalies | volume = 58 | issue = 1 | pages = 33–35 | date = January 2018 | pmid = 28220539 | doi = 10.1111/cga.12216 }}</ref> |
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| ⚫ | Motor innervation controls chromatin acetylation in skeletal muscle and that histone deacetylase 9 (HDAC9) is a signal-responsive transcriptional repressor which is downregulated upon denervation, with consequent upregulation of chromatin acetylation and AChR expression. Forced expression of Hdac9 in denervated muscle prevents upregulation of activity-dependent genes and chromatin acetylation by linking myocyte enhancer factor 2 (MEF2) and class I HDACs. By contrast, Hdac9-null mice are supersensitive to denervation-induced changes in gene expression and show chromatin hyperacetylation and delayed perinatal downregulation of myogenin, an activator of AChR genes. These findings show a molecular mechanism to account for the control of chromatin acetylation by presynaptic neurons and the activity-dependent regulation of skeletal muscle genes by motor innervation 5).<ref>{{cite journal | vauthors = Méjat A, Ramond F, Bassel-Duby R, Khochbin S, Olson EN, Schaeffer L | title = Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression | journal = Nature Neuroscience | volume = 8 | issue = 3 | pages = 313–321 | date = March 2005 | pmid = 15711539 | doi = 10.1038/nn1408 }}</ref> |
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| ⚫ | Histone deacetylase 9 (HDAC9) has been reported to be elevated in ischemic brain injury, but its mechanism in stroke is still enigmatic. Shen et al.<ref>{{cite journal | vauthors = Shen J, Han Q, Li W, Chen X, Lu J, Zheng J, Xue S | title = miR-383-5p Regulated by the Transcription Factor CTCF Affects Neuronal Impairment in Cerebral Ischemia by Mediating Deacetylase HDAC9 Activity. | journal = Mol Neurobiol | date = 2022 | doi = 10.1007/s12035-022-02840-4 | pmid = 35927544 }}</ref> aimed to unveil the manner of regulation of HDAC9 expression and the effect of HDAC9 activation on neuronal function in cerebral ischemia. MicroRNAs (miRNAs) targeting HDAC9 were predicted utilizing bioinformatics analysis. They then constructed the oxygen glucose deprivation cell model and the middle cerebral artery occlusion rat model, and elucidated the expression of CCCTC binding factor (CTCF)/miR-383-5p/HDAC9. Targeting between miR-383-5p and HDAC9 was verified by Dual-Luciferase Reporter Assay and RNAi. After conducting an overexpression/knockdown assay, they assessed neuronal impairment and brain injury. They found that CTCF inhibited miR-383-5p expression via its enrichment in the promoter region of miR-383-5p, whereas the miR-383-5p targeted and inhibited HDAC9 expression. In the oxygen glucose deprivation cell model and the middle cerebral artery occlusion rat model , they confirmed that elevation of HDAC9 regulated by the CTCF/miR-383-5p/HDAC9 pathway mediated apoptosis induced by endoplasmic reticulum stress, while reduction of HDAC9 alleviated apoptosis and the symptoms of cerebral infarction in MCAO rats. Thus, the CTCF/miR-383-5p/HDAC9 pathway may present a target for drug development against ischemic brain injury 6).<ref name="pmid33584204" /> |
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| ⚫ | Zhong et al.<ref name="pmid33584204">{{cite journal | vauthors = Zhong L, Yan J, Li H, Meng L | title = HDAC9 Silencing Exerts Neuroprotection Against Ischemic Brain Injury via miR-20a-Dependent Downregulation of NeuroD1 | journal = Frontiers in Cellular Neuroscience | volume = 14 | issue = | pages = 544285 | date = 2020 | pmid = 33584204 | pmc = 7873949 | doi = 10.3389/fncel.2020.544285 | url = }}</ref> investigated the possible effect of HDAC9 on ischemic brain injury, with the underlying mechanism related to microRNA-20a (miR-20a)/neurogenic differentiation 1 (NeuroD1) explored. The expression of HDAC9 was first detected in the constructed middle cerebral artery occlusion (MCAO)-provoked mouse model and oxygen-glucose deprivation (OGD)-induced cell model. Next, primary neuronal apoptosis, expression of apoptosis-related factors (Bax, cleaved caspase3 and bcl-2), LDH leakage rate, as well as the release of inflammatory factors (TNF-α, IL-1β, and IL-6) were evaluated by assays of TUNEL, Western blot, and ELISA. The relationships among HDAC9, miR-20a, and NeuroD1 were validated by in silico analysis and ChIP assay. HDAC9 was highly-expressed in MCAO mice and OGD-stimulated cells. Silencing of HDAC9 inhibited neuronal apoptosis and inflammatory factor release in vitro. HDAC9 downregulated miR-20a by enriching in its promoter region, while silencing of HDCA9 promoted miR-20a expression. miR-20a targeted Neurod1 and down-regulated its expression. Silencing of HDAC9 diminished OGD-induced neuronal apoptosis and inflammatory factor release in vitro as well as ischemic brain injury in vivo by regulating the miR-20a/NeuroD1 signaling. Overall, our study revealed that HDAC9 silencing could retard ischemic brain injury through the miR-20a/Neurod1 signaling 7) |
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== Interactions == |
== Interactions == |
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[[Category:EC 3.5.1]] |
[[Category:EC 3.5.1]] |
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| ⚫ | |||
| ⚫ | Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined. |
||
| ⚫ | HDAC9 and BCL2L11 were upregulated while miR-92a was downregulated in IA clinical samples and rat models. HDAC9 inhibition or miR-92a elevation improved pathological changes and repressed apoptosis and expression of MMP-2, MMP-9, VEGF and inflammatory factors in vascular tissues from IA rats. Oppositely, HDAC9 overexpression or miR-92a reduction had contrary effects. miR-92a downregulation reversed the effect of silenced HDAC9 on IA rats. |
||
Conclusion: HDAC9 inhibition upregulates miR-92a to repress the progression of IA via silencing BCL2L11 1). |
|||
Data partially confirmed earlier results and showed that variants in CDKN2B-AS1, RP1, and HDAC9 could be genetic susceptibility factors for IA in a Chinese population 2). |
|||
| ⚫ | Yang et al. found that HDAC9 is over-expressed in prognostically poor glioblastoma patients. Knockdown HDAC9 decreased proliferation in vitro and tumor formation in vivo. HDAC9 accelerated cell cycle in part by potentiating the EGFR signaling pathway. Also, HDAC9 interacted with TAZ, a key downstream effector of Hippo pathway. Knockdown of HDAC9 decreased the expression of TAZ. We found that overexpressed TAZ in HDAC9-knockdown cells abrogated the effects induced by HDAC9 silencing both in vitro and in vivo. We demonstrated that HDAC9 promotes tumor formation of glioblastoma via TAZ-mediated EGFR pathway activation, and provide the evidence for promising target for the treatment of glioblastoma 3). |
||
HDAC9 was suggested to contribute to developmental delay in Saethre-Chotzen syndrome (SCS) patients with 7p21 mirodeletions 4). |
|||
| ⚫ | Motor innervation controls chromatin acetylation in skeletal muscle and that histone deacetylase 9 (HDAC9) is a signal-responsive transcriptional repressor which is downregulated upon denervation, with consequent upregulation of chromatin acetylation and AChR expression. Forced expression of Hdac9 in denervated muscle prevents upregulation of activity-dependent genes and chromatin acetylation by linking myocyte enhancer factor 2 (MEF2) and class I HDACs. By contrast, Hdac9-null mice are supersensitive to denervation-induced changes in gene expression and show chromatin hyperacetylation and delayed perinatal downregulation of myogenin, an activator of AChR genes. These findings show a molecular mechanism to account for the control of chromatin acetylation by presynaptic neurons and the activity-dependent regulation of skeletal muscle genes by motor innervation 5). |
||
| ⚫ | |||
| ⚫ | Histone deacetylase 9 (HDAC9) has been reported to be elevated in ischemic brain injury, but its mechanism in stroke is still enigmatic. Shen et al. aimed to unveil the manner of regulation of HDAC9 expression and the effect of HDAC9 activation on neuronal function in cerebral ischemia. MicroRNAs (miRNAs) targeting HDAC9 were predicted utilizing bioinformatics analysis. They then constructed the oxygen glucose deprivation cell model and the middle cerebral artery occlusion rat model, and elucidated the expression of CCCTC binding factor (CTCF)/miR-383-5p/HDAC9. Targeting between miR-383-5p and HDAC9 was verified by Dual-Luciferase Reporter Assay and RNAi. After conducting an overexpression/knockdown assay, they assessed neuronal impairment and brain injury. They found that CTCF inhibited miR-383-5p expression via its enrichment in the promoter region of miR-383-5p, whereas the miR-383-5p targeted and inhibited HDAC9 expression. In the oxygen glucose deprivation cell model and the middle cerebral artery occlusion rat model , they confirmed that elevation of HDAC9 regulated by the CTCF/miR-383-5p/HDAC9 pathway mediated apoptosis induced by endoplasmic reticulum stress, while reduction of HDAC9 alleviated apoptosis and the symptoms of cerebral infarction in MCAO rats. Thus, the CTCF/miR-383-5p/HDAC9 pathway may present a target for drug development against ischemic brain injury 6). |
||
| ⚫ | Zhong et al. investigated the possible effect of HDAC9 on ischemic brain injury, with the underlying mechanism related to microRNA-20a (miR-20a)/neurogenic differentiation 1 (NeuroD1) explored. The expression of HDAC9 was first detected in the constructed middle cerebral artery occlusion (MCAO)-provoked mouse model and oxygen-glucose deprivation (OGD)-induced cell model. Next, primary neuronal apoptosis, expression of apoptosis-related factors (Bax, cleaved caspase3 and bcl-2), LDH leakage rate, as well as the release of inflammatory factors (TNF-α, IL-1β, and IL-6) were evaluated by assays of TUNEL, Western blot, and ELISA. The relationships among HDAC9, miR-20a, and NeuroD1 were validated by in silico analysis and ChIP assay. HDAC9 was highly-expressed in MCAO mice and OGD-stimulated cells. Silencing of HDAC9 inhibited neuronal apoptosis and inflammatory factor release in vitro. HDAC9 downregulated miR-20a by enriching in its promoter region, while silencing of HDCA9 promoted miR-20a expression. miR-20a targeted Neurod1 and down-regulated its expression. Silencing of HDAC9 diminished OGD-induced neuronal apoptosis and inflammatory factor release in vitro as well as ischemic brain injury in vivo by regulating the miR-20a/NeuroD1 signaling. Overall, our study revealed that HDAC9 silencing could retard ischemic brain injury through the miR-20a/Neurod1 signaling 7) |
||
| ⚫ | |||
2) Li B, Hu C, Liu J, Liao X, Xun J, Xiao M, Yan J. Associations among Genetic Variants and Intracranial Aneurysm in a Chinese Population. Yonsei Med J. 2019 Jul;60(7):651-658. doi: 10.3349/ymj.2019.60.7.651. PMID: 31250579; PMCID: PMC6597466. |
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3) Yang R, Wu Y, Wang M, Sun Z, Zou J, Zhang Y, Cui H. HDAC9 promotes glioblastoma growth via TAZ-mediated EGFR pathway activation. Oncotarget. 2015 Apr 10;6(10):7644-56. PubMed PMID: 25760078; PubMed Central PMCID: PMC4480706. |
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| ⚫ | 4) Shimbo H, Oyoshi T, Kurosawa K |
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5) Méjat A, Ramond F, Bassel-Duby R, Khochbin S, Olson EN, Schaeffer L. Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression. Nat Neurosci. 2005 Mar;8(3):313-21. doi: 10.1038/nn1408. Epub 2005 Feb 13. PMID: 15711539. |
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6) Shen J, Han Q, Li W, Chen X, Lu J, Zheng J, Xue S. miR-383-5p Regulated by the Transcription Factor CTCF Affects Neuronal Impairment in Cerebral Ischemia by Mediating Deacetylase HDAC9 Activity. Mol Neurobiol. 2022 Aug 4. doi: 10.1007/s12035-022-02840-4. Epub ahead of print. PMID: 35927544. |
|||
7) Zhong L, Yan J, Li H, Meng L. HDAC9 Silencing Exerts Neuroprotection Against Ischemic Brain Injury via miR-20a-Dependent Downregulation of NeuroD1. Front Cell Neurosci. 2021 Jan 11;14:544285. doi: 10.3389/fncel.2020.544285. PMID: 33584204; PMCID: PMC7873949. |
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Revision as of 09:07, 5 August 2022
Histone deacetylase 9 is an enzyme that in humans is encoded by the HDAC9 gene.[5][6][7]
Function
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.[7]
Histone deacetylase 9 (HDAC9), a member of class II HDACs, regulates a wide variety of normal and abnormal physiological functions.
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.
HDAC9 and BCL2L11 were upregulated while miR-92a was downregulated in IA clinical samples and rat models. HDAC9 inhibition or miR-92a elevation improved pathological changes and repressed apoptosis and expression of MMP-2, MMP-9, VEGF and inflammatory factors in vascular tissues from IA rats. Oppositely, HDAC9 overexpression or miR-92a reduction had contrary effects. miR-92a downregulation reversed the effect of silenced HDAC9 on IA rats.
Conclusion: HDAC9 inhibition upregulates miR-92a to repress the progression of IA via silencing BCL2L11.* Cai Y, Huang D, Ma W, Wang M, Qin Q, Jiang Z, Liu M (August 2021). "Histone deacetylase 9 inhibition upregulates microRNA-92a to repress the progression of intracranial aneurysm via silencing Bcl-2-like protein 11". Journal of Drug Targeting. 29 (7): 761–770. doi:10.1080/1061186X.2021.1878365. PMID 33480300.
Data partially confirmed earlier results and showed that variants in CDKN2B-AS1, RP1, and HDAC9 could be genetic susceptibility factors for IA in a Chinese population.[8]
Yang et al.[9] found that HDAC9 is over-expressed in prognostically poor glioblastoma patients. Knockdown HDAC9 decreased proliferation in vitro and tumor formation in vivo. HDAC9 accelerated cell cycle in part by potentiating the EGFR signaling pathway. Also, HDAC9 interacted with TAZ, a key downstream effector of Hippo pathway. Knockdown of HDAC9 decreased the expression of TAZ. We found that overexpressed TAZ in HDAC9-knockdown cells abrogated the effects induced by HDAC9 silencing both in vitro and in vivo. We demonstrated that HDAC9 promotes tumor formation of glioblastoma via TAZ-mediated EGFR pathway activation, and provide the evidence for promising target for the treatment of glioblastoma 3).
HDAC9 was suggested to contribute to developmental delay in Saethre-Chotzen syndrome (SCS) patients with 7p21 mirodeletions 4).[10]
Motor innervation controls chromatin acetylation in skeletal muscle and that histone deacetylase 9 (HDAC9) is a signal-responsive transcriptional repressor which is downregulated upon denervation, with consequent upregulation of chromatin acetylation and AChR expression. Forced expression of Hdac9 in denervated muscle prevents upregulation of activity-dependent genes and chromatin acetylation by linking myocyte enhancer factor 2 (MEF2) and class I HDACs. By contrast, Hdac9-null mice are supersensitive to denervation-induced changes in gene expression and show chromatin hyperacetylation and delayed perinatal downregulation of myogenin, an activator of AChR genes. These findings show a molecular mechanism to account for the control of chromatin acetylation by presynaptic neurons and the activity-dependent regulation of skeletal muscle genes by motor innervation 5).[11]
Histone deacetylase 9 in Ischemic stroke Histone deacetylase 9 (HDAC9) has been reported to be elevated in ischemic brain injury, but its mechanism in stroke is still enigmatic. Shen et al.[12] aimed to unveil the manner of regulation of HDAC9 expression and the effect of HDAC9 activation on neuronal function in cerebral ischemia. MicroRNAs (miRNAs) targeting HDAC9 were predicted utilizing bioinformatics analysis. They then constructed the oxygen glucose deprivation cell model and the middle cerebral artery occlusion rat model, and elucidated the expression of CCCTC binding factor (CTCF)/miR-383-5p/HDAC9. Targeting between miR-383-5p and HDAC9 was verified by Dual-Luciferase Reporter Assay and RNAi. After conducting an overexpression/knockdown assay, they assessed neuronal impairment and brain injury. They found that CTCF inhibited miR-383-5p expression via its enrichment in the promoter region of miR-383-5p, whereas the miR-383-5p targeted and inhibited HDAC9 expression. In the oxygen glucose deprivation cell model and the middle cerebral artery occlusion rat model , they confirmed that elevation of HDAC9 regulated by the CTCF/miR-383-5p/HDAC9 pathway mediated apoptosis induced by endoplasmic reticulum stress, while reduction of HDAC9 alleviated apoptosis and the symptoms of cerebral infarction in MCAO rats. Thus, the CTCF/miR-383-5p/HDAC9 pathway may present a target for drug development against ischemic brain injury 6).[13]
Zhong et al.[13] investigated the possible effect of HDAC9 on ischemic brain injury, with the underlying mechanism related to microRNA-20a (miR-20a)/neurogenic differentiation 1 (NeuroD1) explored. The expression of HDAC9 was first detected in the constructed middle cerebral artery occlusion (MCAO)-provoked mouse model and oxygen-glucose deprivation (OGD)-induced cell model. Next, primary neuronal apoptosis, expression of apoptosis-related factors (Bax, cleaved caspase3 and bcl-2), LDH leakage rate, as well as the release of inflammatory factors (TNF-α, IL-1β, and IL-6) were evaluated by assays of TUNEL, Western blot, and ELISA. The relationships among HDAC9, miR-20a, and NeuroD1 were validated by in silico analysis and ChIP assay. HDAC9 was highly-expressed in MCAO mice and OGD-stimulated cells. Silencing of HDAC9 inhibited neuronal apoptosis and inflammatory factor release in vitro. HDAC9 downregulated miR-20a by enriching in its promoter region, while silencing of HDCA9 promoted miR-20a expression. miR-20a targeted Neurod1 and down-regulated its expression. Silencing of HDAC9 diminished OGD-induced neuronal apoptosis and inflammatory factor release in vitro as well as ischemic brain injury in vivo by regulating the miR-20a/NeuroD1 signaling. Overall, our study revealed that HDAC9 silencing could retard ischemic brain injury through the miR-20a/Neurod1 signaling 7)
Interactions
HDAC9 has been shown to interact with:
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000048052 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004698 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (November 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Molecular and Cellular Biology. 19 (11): 7816–27. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.
- ^ Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ (September 1999). "MEF-2 function is modified by a novel co-repressor, MITR". The EMBO Journal. 18 (18): 5085–98. doi:10.1093/emboj/18.18.5085. PMC 1171579. PMID 10487760.
- ^ a b "Entrez Gene: HDAC9 histone deacetylase 9".
- ^ Li B, Hu C, Liu J, Liao X, Xun J, Xiao M, Yan J (July 2019). "Associations among Genetic Variants and Intracranial Aneurysm in a Chinese Population". Yonsei Medical Journal. 60 (7): 651–658. doi:10.3349/ymj.2019.60.7.651. PMID 31250579.
- ^ Yang R, Wu Y, Wang M, Sun Z, Zou J, Zhang Y, Cui H (April 2015). "HDAC9 promotes glioblastoma growth via TAZ-mediated EGFR pathway activation". Oncotarget. 6 (10): 7644–56. doi:10.18632/oncotarget.3223. PMC 4480706. PMID 25760078.
- ^ Shimbo H, Oyoshi T, Kurosawa K (January 2018). "Contiguous gene deletion neighboring TWIST1 identified in a patient with Saethre-Chotzen syndrome associated with neurodevelopmental delay: Possible contribution of HDAC9". Congenital Anomalies. 58 (1): 33–35. doi:10.1111/cga.12216. PMID 28220539.
- ^ Méjat A, Ramond F, Bassel-Duby R, Khochbin S, Olson EN, Schaeffer L (March 2005). "Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression". Nature Neuroscience. 8 (3): 313–321. doi:10.1038/nn1408. PMID 15711539.
- ^ Shen J, Han Q, Li W, Chen X, Lu J, Zheng J, Xue S (2022). "miR-383-5p Regulated by the Transcription Factor CTCF Affects Neuronal Impairment in Cerebral Ischemia by Mediating Deacetylase HDAC9 Activity". Mol Neurobiol. doi:10.1007/s12035-022-02840-4. PMID 35927544.
- ^ a b Zhong L, Yan J, Li H, Meng L (2020). "HDAC9 Silencing Exerts Neuroprotection Against Ischemic Brain Injury via miR-20a-Dependent Downregulation of NeuroD1". Frontiers in Cellular Neuroscience. 14: 544285. doi:10.3389/fncel.2020.544285. PMC 7873949. PMID 33584204.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ a b Asare Y, Campbell-James TA, Bokov Y, Yu LL, Prestel M, El Bounkari O, Roth S, Megens RT, Straub T, Thomas K, Yan G, Schneider M, Ziesch N, Tiedt S, Silvestre-Roig C, Braster Q, Huang Y, Schneider M, Malik R, Haffner C, Liesz A, Soehnlein O, Bernhagen J, Dichgans M (June 2020). "Histone Deacetylase 9 Activates IKK to Regulate Atherosclerotic Plaque Vulnerability". Circulation Research. 127 (6): 811–823. doi:10.1161/CIRCRESAHA.120.316743. PMID 32546048. S2CID 219726725.
- ^ a b Zhang CL, McKinsey TA, Olson EN (October 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Molecular and Cellular Biology. 22 (20): 7302–12. doi:10.1128/mcb.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
- ^ a b c Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (May 2003). "The histone deacetylase 9 gene encodes multiple protein isoforms". The Journal of Biological Chemistry. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
- ^ Zhou X, Richon VM, Rifkind RA, Marks PA (February 2000). "Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5". Proceedings of the National Academy of Sciences of the United States of America. 97 (3): 1056–61. Bibcode:2000PNAS...97.1056Z. doi:10.1073/pnas.97.3.1056. PMC 15519. PMID 10655483.
- ^ Micheli L, D'Andrea G, Leonardi L, Tirone F (July 2017). "HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression" (PDF). Journal of Cellular Physiology. 232 (7): 1696–1707. doi:10.1002/jcp.25467. PMID 27333946. S2CID 4070837.
- ^ Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (September 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". The EMBO Journal. 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. PMC 1171580. PMID 10487761.
- ^ Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S (May 2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity" (PDF). The Journal of Biological Chemistry. 275 (20): 15594–9. doi:10.1074/jbc.M908437199. PMID 10748098. S2CID 39220205.
- ^ Koipally J, Georgopoulos K (June 2002). "Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression". The Journal of Biological Chemistry. 277 (26): 23143–9. doi:10.1074/jbc.M202079200. PMID 11959865.
Further reading
- Marks PA, Richon VM, Rifkind RA (August 2000). "Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells". Journal of the National Cancer Institute. 92 (15): 1210–6. doi:10.1093/jnci/92.15.1210. PMID 10922406.
- Verdin E, Dequiedt F, Kasler HG (May 2003). "Class II histone deacetylases: versatile regulators". Trends in Genetics. 19 (5): 286–93. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
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External links
- HDAC9+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
