NDLI: Regulation of ERα Signaling Pathway in Neuronal HN10 Cells: Role of Protein Acetylation and Hsp90

Content Provider	Springer Nature Link
Author	Suuronen, Tiina Ojala, Johanna Hyttinen, Juha M. T. Kaarniranta, Kai Thornell, Anders Kyrylenko, Sergiy Salminen, Antero
Copyright Year	2008
Abstract	Estrogen has a variety of neuroprotective effects but the molecular basis of its function is still mainly unclear. Estrogen receptor (ER) signaling is highly dependent on posttranslational modifications and the assembly of coactivator and corepressor complexes. Several proteins involved in ERα signaling have recently been found to be acetylated, including ERα itself and Hsp90, a key chaperone in the functional regulation of ERα. ERα complexes also contain histone deacetylases (HDAC) which repress transactivation. Our purpose was to clarify the role of protein acetylation and Hsp90 function in the ERE-mediated ERα signaling in neuronal HN10 cells. We observed that increasing protein/histone acetylation status with trichostatin A, a potent HDAC inhibitor, increased the 17β-estradiol (E2)-induced transactivation of ERE-driven luciferase in non-transfected cells, and even more extensively in pERα-transfected cells. E2-induced ERE-driven transactivation was blocked by ICI 182.780. Several ER antagonists, such as raloxifene and tamoxifen, were unresponsive. Valproate, an antiepileptic drug which is recently characterized as a HDAC inhibitor, was also able to potentiate the E2-induced ERE-transactivation. Inhibition of the function of Hsp90 chaperone with geldanamycin strongly inhibited the E2-induced ERE-transactivation. Overexpression of SIRT2 protein deacetylase did not inhibit the acetylation-potentiated ERE-driven transactivation indicating that SIRT2 deacetylase is not involved in ERα signaling. Our results reveal that ERα signaling is dependent on protein acetylation and epigenetic regulation.
Starting Page	1768
Ending Page	1775
Page Count	8
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	33
Issue Number	9
e-ISSN	15736903
Language	English
Publisher	Springer US
Publisher Date	2008-02-29
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Estrogen Epigenetics HDAC Neuroprotection SERM Valproate Neurology Biochemistry Neurosciences
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Estrogen-like neuroprotection of isopsoralen against spinal cord injury through estrogen receptor ERα

Neuronal Peroxisome Proliferator-Activated Receptor γ Signaling: Regulation by Mood-Stabilizer Valproate

Inducible mutant huntingtin expression in HN10 cells reproduces Huntington's disease-like neuronal dysfunction

Hypoinsulinemia Alleviates the Grf1/Ras/Akt Anti-Apoptotic Pathway and Induces Alterations of Mitochondrial Ras Trafficking in Neuronal Cells

Effects of HDAC inhibitors on neuroblastoma SH-SY5Y cell differentiation into mature neurons via the Wnt signaling pathway

Lithium and Valproate Protect Hippocampal Slices Against ATP-induced Cell Death

Immune cell-mediated neuroprotection is independent of estrogen action through estrogen receptor-alpha

Regulation of ERα Protein Expression by 17β-Estradiol in Cultured Neurons of Hypothalamic Ventromedial Nucleus

Neuroprotection of Atractylenolide III from Atractylodis macrocephalae Against Glutamate-Induced Neuronal Apoptosis Via Inhibiting Caspase Signaling Pathway

Regulation of ERα Signaling Pathway in Neuronal HN10 Cells: Role of Protein Acetylation and Hsp90

Similar Documents

Estrogen-like neuroprotection of isopsoralen against spinal cord injury through estrogen receptor ERα

Neuronal Peroxisome Proliferator-Activated Receptor γ Signaling: Regulation by Mood-Stabilizer Valproate

Inducible mutant huntingtin expression in HN10 cells reproduces Huntington's disease-like neuronal dysfunction

Hypoinsulinemia Alleviates the Grf1/Ras/Akt Anti-Apoptotic Pathway and Induces Alterations of Mitochondrial Ras Trafficking in Neuronal Cells

Effects of HDAC inhibitors on neuroblastoma SH-SY5Y cell differentiation into mature neurons via the Wnt signaling pathway

Lithium and Valproate Protect Hippocampal Slices Against ATP-induced Cell Death

Immune cell-mediated neuroprotection is independent of estrogen action through estrogen receptor-alpha

Regulation of ERα Protein Expression by 17β-Estradiol in Cultured Neurons of Hypothalamic Ventromedial Nucleus

Neuroprotection of Atractylenolide III from Atractylodis macrocephalae Against Glutamate-Induced Neuronal Apoptosis Via Inhibiting Caspase Signaling Pathway

Regulation of ERα Signaling Pathway in Neuronal HN10 Cells: Role of Protein Acetylation and Hsp90