Document Detail


Transcriptional activation of prion protein gene in growth-arrested and differentiated mouse erythroleukemia and human neoplastic cells.
MedLine Citation:
PMID:  11262197     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The prion protein (PrP) is a GPI-anchored sialoglycoprotein that has attracted worldwide attention over the years due to its involvement in the pathogenesis of transmissible spongiform encephalopathies in sheep (scrapie), cattle (BSE), and humans (CJD). To understand the precise role of the Prn-p gene in cell growth and differentiation we investigated the expression pattern of the Prn-p gene in proliferating cells and in cells arrested in growth either by confluency or by induction of terminal differentiation. Viral-transformed mouse spleen hematopoietic cells named murine erythroleukemia (MEL) and other types of inducible cells (human neuroectodermal RD/TE-671, myoid RD cells) were employed. Cells grown exponentially, at confluency, or irreversibly arrested in growth at terminal differentiation state were analyzed by fluorescence cell sorting and Northern blot hybridization to estimate the steady-state level of PrP mRNA at different phases of the cell cycle. MEL cells that failed to differentiate from treatment with N(6)-methyladenosine (N(6)mAdo), an inhibitor of differentiation, were also analyzed for PrP mRNA level. Our results indicate the following: (a) growth arrest of cells at G(1) phase by confluency or by induction of terminal differentiation led to increased accumulation of PrP mRNA transcripts, an event observed also in differentiated MEL, RD/TE-671, and RD cells independent of the inducer used; (b) treatment of MEL cells with N(6)mAdo prevented early activation of the Prn-p gene in cells treated with the inducer; and (c) cell-free nuclear run-off studies showed enhanced expression of the Prn-p gene due to transcriptional activation. These findings indicate, for the first time, that the Prn-p gene, which is thought to be a housekeeping gene, is transcriptionally activated in G(1) phase in confluent and terminally differentiated cells. This information may be valuable in understanding the overaccumulation of PrP in some differentiated tissues and may let us repress Prn-p gene activation by novel agents.
Authors:
D D Gougoumas; I S Vizirianakis; A S Tsiftsoglou
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Experimental cell research     Volume:  264     ISSN:  0014-4827     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2001 Apr 
Date Detail:
Created Date:  2001-03-23     Completed Date:  2001-06-07     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  408-17     Citation Subset:  IM    
Copyright Information:
Copyright 2001 Academic Press.
Affiliation:
Laboratory of Pharmacology, Aristotle University of Thessaloniki, Thessaloniki, GR-54006, Greece.
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MeSH Terms
Descriptor/Qualifier:
Adenosine / analogs & derivatives,  pharmacology
Animals
Cell Differentiation / drug effects
Cell Division
Dimethyl Sulfoxide / pharmacology
Gene Expression Profiling
Humans
Leukemia, Erythroblastic, Acute
Mice
PrPC Proteins / genetics*
Pyridines / pharmacology
RNA, Messenger / metabolism
Sialoglycoproteins / genetics*
Transcriptional Activation*
Tumor Cells, Cultured
Urea / analogs & derivatives,  pharmacology
Chemical
Reg. No./Substance:
0/PrPC Proteins; 0/Pyridines; 0/RNA, Messenger; 0/Sialoglycoproteins; 141766-10-1/2-(3-ethylureido)-6-methylpyridine; 1867-73-8/N(6)-methyladenosine; 57-13-6/Urea; 58-61-7/Adenosine; 67-68-5/Dimethyl Sulfoxide

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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