Linked Life Data

8912641

Source:http://linkedlifedata.com/resource/pubmed/id/8912641

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-12-13
pubmed:abstractText
Fibroblasts cultivated in a collagen matrix exhibit a large decrease in the synthesis of most proteins, depending on transcriptional and posttranscriptional controls. We have previously shown that ribosomal RNA content and half-life were decreased in collagen lattice cultures. Here, we cultivated human dermal fibroblasts in monolayers and in lattices and studied by competitive RT-PCR analysis the expression of the nucleolar proteins nucleolin and fibrillarin, two key factors in ribosome processing and association. Nucleolin expression was found increased, and fibrillarin expression decreased, in collagen-lattice vs monolayer-cultured fibroblasts, with some variability according to the strains (+25 to +250% and -40 to -60%, respectively). These data suggest that a possible trouble of the association between neosynthesized rRNA and nucleolar proteins is, at least partly, responsible for the inhibition of protein synthesis induced by the extracellular matrix.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
228
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
94-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Modulation of protein synthesis by extracellular matrix: potential involvement of two nucleolar proteins, nucleolin and fibrillarin.
pubmed:affiliation
Laboratory of Biochemistry and Molecular Biology, CNRS EP 89, IFR 53-Biomolecules, Faculty of Medicine, University of Reims Champagne-Ardenne, France.
pubmed:publicationType
Journal Article, Comparative Study