Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1997-4-3
pubmed:databankReference
pubmed:abstractText
omega-Conotoxin-sensitive N-type Ca2+ channels, unlike dihydropyridine-sensitive L-type channels, are exclusively expressed in nervous tissues. To understand the molecular basis for neuron-specific expression of the N-type channel, we have isolated genomic clones encoding the human alpha1B subunit gene, localized to the long arm of chromosome 9 (9q34) by fluorescence in situ hybridization, and characterized its 5'-upstream region. The proximal promoter of the alpha1B subunit gene lacks a typical TATA box, is highly GC-rich, and contains several sequences for transcription factor binding. Primer extension experiments revealed the presence of two transcription start sites. In vitro transfection study of the alpha1B subunit-luciferase fusion gene showed that the 4.0-kb 5'-flanking region of the alpha1B gene functions as an efficient promoter in neuronal cells but not in glioma or nonneuronal cells, consistent with the patterns of the endogenous alpha1B gene expression in these cells. Deletion analysis of alpha1B subunit-luciferase fusion gene constructs further revealed the presence of several cis-acting regulatory elements, including a potential repressor located in the distal upstream region (-3992 to -1788) that may be important for the neuron-specific expression of the N-type Ca2+ channel alpha1B subunit gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5098-104
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Isolation and characterization of the 5'-upstream region of the human N-type calcium channel alpha1B subunit gene. Chromosomal localization and promoter analysis.
pubmed:affiliation
Laboratory of Neurochemistry, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article