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Biochem Biophys Res Commun. 1996 Nov 1;228(1):94-9.

Modulation of protein synthesis by extracellular matrix: potential involvement of two nucleolar proteins, nucleolin and fibrillarin.

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Laboratory of Biochemistry and Molecular Biology, CNRS EP 89, IFR 53-Biomolecules, Faculty of Medicine, University of Reims Champagne-Ardenne, France.


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.

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