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C Setoyama

Publications and source records attributed to C Setoyama.

23 records · Page 2Linked to original sources

Isolation and characterization of the cDNAs corresponding to mRNAs abundant in undifferentiated mouse embryonal teratocarcinoma stem cells, but not in differentiated mouse parietal endoderm cells.

As retinoic acid (RA) and dibutyryl cAMP (cAMP) treatment induces differentiation of mouse teratocarcinoma F9 cells into parietal endoderm cells in vitro, we initiated studies on the molecular mechanisms underlying early mammalian cell differentiation in this system. We constructed cDNA libraries on the poly(A)+RNAs extracted from the undifferentiated F9 cells, and screened for cDNA sequences expressed abundantly in F9 cells, but not in terminally differentiated mouse parietal endoderm PYS-2 cells. Six different cDNA clones were isolated and characterized. The levels of RNAs hybridizable to these clones were at most 5 to 24% in the PYS-2 cells when compared with those in the undifferentiated F9 cells. The six clones were classified into two groups on the basis of their responses to the RA and cAMP treatment. In F9 cells, the levels of RNAs hybridizable to the first group, which contained four clones, were decreased within 72 h after the addition of RA and cAMP, while those of the second group, which contained the remaining two clones, did not decrease significantly. One of the first group clones, named pF9-1, corresponded to the mouse "early transposon-like elements" and another, named pF9-4, hybridized to multi-size RNAs extracted from the undifferentiated F9 cells. The mouse genomic DNA sequences hybridizable to pF9-4 were repeated approximately 5,000 times, and comprise a new gene family, the expression of which is developmentally regulated in mouse F9 cells.

Animals

Structural and functional studies on the interstitial collagen genes.

An understanding of the molecular mechanisms which control expression of the type I and III collagen genes may provide a rational basis for the design of more effective therapeutic approaches to fibrotic diseases. The structure of the interstitial collagen genes is reviewed and potential sites which could control their expression are examined. One approach to the study of the regulation of these genes consists in DNA-mediated gene transfection experiments and is discussed in this paper.

Animals

Pleiotropic mutants of NIH 3T3 cells with altered regulation in the expression of both type I collagen and fibronectin.

Transformation of NIH 3T3 fibroblasts by v-mos causes a decrease in the levels of type I collagen RNA. In NIH 3T3 cells that have been made resistant to G418 by transfection with a plasmid in which the mouse alpha 2(I) collagen promoter is linked to the neo gene, subsequent v-mos transformation causes a loss of G418 resistance. After mutagenesis of these v-mos-transformed cells, G418-resistant colonies were selected. Two of these G418-resistant mutants showed an increased expression of the neo gene and of the endogenous type I collagen and fibronectin genes, without changes in their levels of v-mos RNA or in their ability to induce tumors. The mutations might alter cellular trans-acting factors that either directly or indirectly control the expression of the type I collagen and fibronectin genes in transformed cells.

Animals

Regulation of a collagen gene promoter by the product of viral mos oncogene.

Oncogenic transformation of cells produces important changes in the biosynthetic pattern of certain cellular proteins. For example, the synthesis of type I collagen in transformed fibroblasts is severely reduced as a result of changes in transcription. Here we report the results of DNA-mediated transfection experiments using recombinant plasmids in which the promoter region of the alpha 2(I) collagen gene is fused to an easily recognizable marker gene, and cell lines expressing the marker gene are isolated. Our data show that the expression of the marker gene fused to the cloned alpha 2(I) collagen promoter is strongly inhibited by v-mos transformation, suggesting that a common mechanism inhibits both the transfected and endogeneous alpha 2(I) collagen promoters.

Animals