|Reference : Rat Chromosome 5 (Q22-23) Contains Elements That Control Cell Morphology and Interaction...|
|Scientific journals : Article|
|Life sciences : Anatomy (cytology, histology, embryology...) & physiology|
|Rat Chromosome 5 (Q22-23) Contains Elements That Control Cell Morphology and Interactions with the Extracellular Matrix: A Study of Normal Fibroblast X Malignant Hepatoma Cell Hybrids|
|Lewalle, J. M. [> > > >]|
|Szpirer, C. [> > > >]|
|Szpirer, J. [> > > >]|
|Munaut, Carine [Université de Liège - ULg > Département des sciences cliniques > Labo de biologie des tumeurs et du développement >]|
|Foidart, Jean-Michel [Université de Liège - ULg > Département des sciences cliniques > Gynécologie - Obstétrique >]|
|Experimental Cell Research|
|Yes (verified by ORBi)|
|[en] Cell interactions with the extracellular matrix are consistently modified in neoplasia. Malignant transformation has been correlated with modifications in the synthesis and distribution of matrix components and with alterations of cell adhesive properties to these components. A particular class of genes, able to suppress the transformed phenotype in normal cells, may be involved in those phenotypic changes. By studying somatic cell hybrids between mouse hepatoma (BWTG3) cells and normal rat skin fibroblasts (RSF), Islam and co-workers were able to localize a gene or a group of genes controlling anchorage dependence and cell growth in vitro. This (or these) gene(s) was (were) assigned to the q22-23 fragment of rat chromosome 5. In the present study, we compare the morphology and the interactions with the extracellular matrix proteins (laminin, fibronectin, and collagen IV) and the synthesis of these proteins by RSF X BWTG3 hybrid cells that had either retained (BS181p10) or lost (BS181a5) the q22-23 region of rat chromosome 5. Our results suggest that the rat 5q22-23 fragment controls a part of the cell differentiation program including morphology, attachment to extracellular matrix, and synthesis of some matrix proteins, particularly alpha 1 and alpha 2 chains of collagen IV.|
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