Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-4-13
pubmed:abstractText
Transcriptional activity of the human apolipoprotein (apo) A-II promoter has been reported in transiently transfected Caco-2 cells, but not in the intestine in vivo. In the present study we established that the transcription of a stably transfected reporter gene under the control of the -911/+29 human apo A-II, decreases with the onset of the differentiation process. This decrease paralleled that of the expression of the endogenous apo A-II gene. The decrease in apo A-II expression is also followed by a marked increase in the expression of the intestine-specific apo A-IV gene, analyzed here as a marker of enterocytic differentiation. Using clonal glucose metabolic variants of Caco-2 cells we have also observed that the lowest levels of apo A-II mRNA are associated with the lowest rates of glucose consumption. The illegitimate apo A-II transcriptional activity observed in Caco-2 cells is linked to the presence of DNase-I hypersensitive sites within the enhancer. This reflects a chromatin organization which allows, in Caco-2 cells as in the liver, the communication between the apo A-II enhancer and the proximal promoter, unlike what is observed in intestinal epithelial cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
247
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
373-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Illegitimate expression of apolipoprotein A-II in Caco-2 cells is due to chromatin organization.
pubmed:affiliation
INSERM U505, Université Pierre et Marie Curie, 15 rue de l'Ecole de Médecine, Paris, 75006, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't