Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2010-9-27
pubmed:abstractText
The transcription factor C/EBP? is more potent than C/EBP? in inducing granulocitic differentiation and inhibiting BCR/ABL-expressing cells. We took a "domain swapping" approach to assess biological effects, modulation of gene expression, and binding to C/EBP?-regulated promoters by wild-type and chimeric C/EBP?/C/EBP? proteins. Wild-type and N-C/EBP?+ C/EBP?-DBD induced transcription of the granulocyte-colony stimulating factor receptor (G-CSFR) gene, promoted differentiation, and suppressed proliferation of K562 cells vigorously; instead, wild-type C/EBP? and N-C/EBP?+C/EBP?-DBD had modest effects, although they bound the G-CSFR promoter like wild-type C/EBP? and N-C/EBP?+C/EBP?-DBD. Chimeric proteins consisting of the TAD of VP16 and the DBD of C/EBP? or C/EBP? inhibited proliferation and induced differentiation of K562 cells as effectively as wild-type C/EBP?. Gene expression profiles induced by C/EBP? resembled those modulated by N-C/EBP?+C/EBP?-DBD, whereas C/EBP? induced a pattern similar to that of N-C/EBP?+C/EBP?-DBD. C/EBP? activation induced changes in the expression of more cell cycle- and apoptosis-related genes than the other proteins and enhanced Imatinib-induced apoptosis of K562 cells. Expression of FOXO3a, a novel C/EBP?-regulated gene, was required for apoptosis but not for differentiation induction or proliferation inhibition of K562 cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
285
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30837-50
pubmed:dateRevised
2011-10-3
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The biological effects of C/EBPalpha in K562 cells depend on the potency of the N-terminal regulatory region, not on specificity of the DNA binding domain.
pubmed:affiliation
Department of Biological Sciences, University of Modena and Reggio Emilia, 41100 Modena, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural