Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1991-7-10
pubmed:abstractText
Based on competition analysis of gel shift assays utilizing nuclear extracts from the mouse adrenal Y1 cell line, the cAMP-responsive element of the human CYP21B gene (-129/-96 base pairs (bp] is found to contain two overlapping nuclear protein binding elements. One, -126/-113 bp, interacts specifically with an adrenal-specific protein factor (ASP) while the other, -119/-110 bp, contains a GC boxlike sequence and binds Sp1. The nucleotide replacements (GG----CC at -113 and -112 bp) introduced within the sequence -129/-96 bp greatly decreased the binding affinities of both Sp1 and ASP to the fragment and resulted in a loss of cAMP-enhanced transcription of a reporter gene in transient transfection experiments. When the 14-bp ASP-binding sequence was inserted in front of the reporter gene, induced transcription by cAMP was observed that could be increased by multimerization of this -126/-113-bp sequence. The -126/-113-bp fragment revealed specific binding only with nuclear extracts from adrenal Y1 cells among various types of cells tested, indicating that the protein factor ASP is specifically expressed in adrenal cells. The nucleotide replacement (G----C at -117 bp) of the -126 -113-bp sequence not only abolishes the binding to ASP but also the cAMP-dependent transcription, strongly supporting the hypothesis that ASP is a tissue-specific transacting protein that directly functions as a transcription factor essential to the cAMP-dependent transcription. Furthermore, the -129/-115-bp sequence of the bovine cytochrome P450C21 gene corresponding to the human -126/-113-bp sequence is demonstrated to be functionally conserved with respect to both cAMP-dependent enhancement of transcription and ASP binding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11199-204
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1645728-Adrenal Glands, pubmed-meshheading:1645728-Animals, pubmed-meshheading:1645728-Base Composition, pubmed-meshheading:1645728-Base Sequence, pubmed-meshheading:1645728-Binding, Competitive, pubmed-meshheading:1645728-Binding Sites, pubmed-meshheading:1645728-Cattle, pubmed-meshheading:1645728-Cell Line, pubmed-meshheading:1645728-Cyclic AMP, pubmed-meshheading:1645728-Forskolin, pubmed-meshheading:1645728-Gene Expression Regulation, Enzymologic, pubmed-meshheading:1645728-Humans, pubmed-meshheading:1645728-Mice, pubmed-meshheading:1645728-Molecular Sequence Data, pubmed-meshheading:1645728-Nuclear Proteins, pubmed-meshheading:1645728-Nucleotide Mapping, pubmed-meshheading:1645728-Oligonucleotide Probes, pubmed-meshheading:1645728-Plasmids, pubmed-meshheading:1645728-Steroid 21-Hydroxylase, pubmed-meshheading:1645728-Transcription, Genetic, pubmed-meshheading:1645728-Transfection
pubmed:year
1991
pubmed:articleTitle
Evidence that an adrenal-specific nuclear protein regulates the cAMP responsiveness of the human CYP21B (P450C21) gene.
pubmed:affiliation
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't