Linked Life Data

17229153

Source:http://linkedlifedata.com/resource/pubmed/id/17229153

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-1-18
pubmed:abstractText
Neurons are highly polarized cells composed of two structurally and functionally distinct parts, the axon and the dendrite. The establishment of this asymmetric structure is a tightly regulated process. In fact, alterations in the proteins involved in the configuration of the microtubule lattice are frequent in neuro-oncologic diseases. One of these cytoplasmic mediators is the protein known as collapsin response mediator protein-2, which interacts with and promotes tubulin polymerization. In this study, we investigated collapsin response mediator protein-2 transcriptional regulation during all-trans-retinoic acid-induced differentiation of SH-SY5Y neuroblastoma cells. All-trans-retinoic acid is considered to be a potential preventive and therapeutic agent, and has been extensively used to differentiate neuroblastoma cells in vitro. Therefore, we first demonstrated that collapsin response mediator protein-2 mRNA levels are downregulated during the differentiation process. After completion of deletion construct analysis and mutagenesis and mobility shift assays, we concluded that collapsin response mediator protein-2 basal promoter activity is regulated by the transcription factors AP-2 and Pax-3, whereas E2F, Sp1 and NeuroD1 seem not to participate in its regulation. Furthermore, we finally established that reduced expression of collapsin response mediator protein-2 after all-trans-retinoic acid exposure is associated with impaired Pax-3 and AP-2 binding to their consensus sequences in the collapsin response mediator protein-2 promoter. Decreased attachment of AP-2 is a consequence of its accumulation in the cytoplasm. On the other hand, Pax-3 shows lower binding due to all-trans-retinoic acid-mediated transcriptional repression. Unraveling the molecular mechanisms behind the action of all-trans-retinoic acid on neuroblastoma cells may well offer new perspectives for its clinical application.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1742-464X
pubmed:author
pubmed:issnType
Print
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
498-511
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17229153-Antineoplastic Agents, pubmed-meshheading:17229153-Base Sequence, pubmed-meshheading:17229153-Cell Differentiation, pubmed-meshheading:17229153-Cell Line, Tumor, pubmed-meshheading:17229153-Humans, pubmed-meshheading:17229153-Intercellular Signaling Peptides and Proteins, pubmed-meshheading:17229153-Molecular Sequence Data, pubmed-meshheading:17229153-Nerve Tissue Proteins, pubmed-meshheading:17229153-Neuroblastoma, pubmed-meshheading:17229153-Paired Box Transcription Factors, pubmed-meshheading:17229153-Promoter Regions, Genetic, pubmed-meshheading:17229153-RNA Processing, Post-Transcriptional, pubmed-meshheading:17229153-Sequence Homology, Nucleic Acid, pubmed-meshheading:17229153-Transcription, Genetic, pubmed-meshheading:17229153-Transcription Factor AP-2, pubmed-meshheading:17229153-Tretinoin
pubmed:year
2007
pubmed:articleTitle
All-trans-retinoic acid inhibits collapsin response mediator protein-2 transcriptional activity during SH-SY5Y neuroblastoma cell differentiation.
pubmed:affiliation
Department of Biochemistry, University of Navarra, Pamplona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't