Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이영식 | - |
dc.date.accessioned | 2019-08-05T05:23:41Z | - |
dc.date.available | 2019-08-05T05:23:41Z | - |
dc.date.issued | 2006-06 | - |
dc.identifier.citation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v. 346, No. 2, Page. 426-435 | en_US |
dc.identifier.issn | 0006-291X | - |
dc.identifier.issn | 1090-2104 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0006291X06011661 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/108216 | - |
dc.description.abstract | Tyrosine hydroxylase (TH), the biosynthetic enzyme of catecholamine, is synthesized specifically in catecholaminergic neurons. Thus, it is possible that neuronal cell type-specific expression of this gene is coordinately regulated. One of the neuron- specific transcription regulators, neuron-restrictive silencer factor (NRSF)/ repressor element 1 (RE1) silencing transcription factor (REST), represses the expression of neuronal genes in non-neuronal cells. To elucidate the molecular mechanisms that control catecholaminergic neuronal expression of human TH, we initially characterized the 50 regulatory region. Previous studies have shown that a 3174 bp fragment of the human TH promoter confers specific expression to the reporter gene in dopaminergic neuron-like cell lines. Within this 50 regulatory region, three putative neuron-restrictive silencer elements (NRSE)/RE1 were identified, which bound NRSF/REST in a sequence-specific manner, as confirmed using EMSA and ChIP assays. In transient transfection assays, deletion or mutation of NRSE/RE1 elements led to a 7-fold increase in activity of the 3.2 kb TH promoter in human neural stem cells (NSCs), but had no major effects on differentiated neuron- like cells. Suppression of NRSF/REST functions with either the histone deacetylase inhibitor, trichostatin, or DN-NRSFinduced TH promoter activity. Our data strongly suggest that NRSF/REST functions as a repressor of TH transcription in NSCs via a mechanism dependent on the TH NRSE/RE1 sites. | en_US |
dc.description.sponsorship | We thank Dr. D.J. Anderson for providing the mouse NRSF monoclonal antibody, and Dr. G. Mendel for the dominant-negative REST expression plasmids. The research was supported by Grants (the BK21 Program of the Ministry of Education and Human Resource Development) from the KOSEF/BDRC Ajou University, a Neurobiology Research Program grant from the Korea Ministry of Science and Technology, and a grant (SC3090) from Stem Cell Research Center of the 21st Century Frontier Research Program, funded by the Ministry of Science and Technology, Republic of Korea. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | ACADEMIC PRESS INC | en_US |
dc.subject | tyrosine hydroxylase | en_US |
dc.subject | promoter | en_US |
dc.subject | repression | en_US |
dc.subject | NRSF/REST | en_US |
dc.subject | NRSE/RE1 | en_US |
dc.subject | catecholaminergic | en_US |
dc.subject | neural stem cells | en_US |
dc.title | Regulation of human tyrosine hydroxylase gene by neuron-restrictive silencer factor | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1016/j.bbrc.2006.05.142 | - |
dc.relation.journal | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.contributor.googleauthor | Kim, Soo Min | - |
dc.contributor.googleauthor | Yang, Jae Won | - |
dc.contributor.googleauthor | Park, Mi Jung | - |
dc.contributor.googleauthor | Lee, Joon-Kyu | - |
dc.contributor.googleauthor | Kim, Seung U | - |
dc.contributor.googleauthor | Lee, Young Seek | - |
dc.contributor.googleauthor | Lee, Myung Ae | - |
dc.relation.code | 2008201235 | - |
dc.sector.campus | E | - |
dc.sector.daehak | COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E] | - |
dc.sector.department | DEPARTMENT OF MOLECULAR AND LIFE SCIENCE | - |
dc.identifier.pid | yslee | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.