PubMed Health⌕ Search

Biomedical subjects

A Hirose-Kumagai

Publications and source records attributed to A Hirose-Kumagai.

9 recordsLinked to original sources
PubMed1995

The interaction between nucleoproteins and thyroid response element (TRE) during regenerating rat liver.

We examined the interaction of nucleoproteins with thyroid response element (TRE) by south-western method. The proteins that bound specifically to TRE were detected at apparent molecular weight about 30,000 and 15,000 - 10,000. After digestion of nucleoproteins blotted on PVDF membrane with Endoglycosidase H, the amounts of TRE that bound to the nucleoproteins were increased. These results show that carbohydrate moieties of nucleoproteins have an important role on the interaction of the nucleoproteins with TRE. T3 stimulated the binding of TRE to nucleoproteins. The amount of T3 binding to nucleoproteins was changed during liver regeneration. These results indicate that T3 changes the interaction of the nucleoproteins with TRE, so T3 serves as a transducing signal to modulate the gene regulating activity of TRE-binding nucleoproteins. Liver regeneration may be controlled by these modification of interaction of nucleoproteins with DNA.

Animals↗
PubMed1993

Alteration of glycoproteins in nuclei during regeneration of rat liver.

Hepatocyte nuclei from partially hepatectomized and sham operated rats were isolated. Total and 0.35 M NaCl soluble proteins were prepared from the nuclei. The proteins were separated by gel electrophoresis and examined by lectin staining methods. Within the limits of sensitivity of these techniques, the following features emerged. 1) A majority of proteins visualized were common to and present in similar relative quantities in the nuclei during rat liver regeneration. 2) The nuclear glycoproteins were detected by several lectins. The fluctuations at the stages of the regeneration were evident. The complicated patterns of changes were observed. 3) The DNA binding activities of the nuclear proteins were observed by the south-western methods. The DNA binding activities of nuclear proteins were changed after enzyme digestion of sugar moieties of nuclear glycoproteins. From these of our results, it is suggested that the sugar chains of nuclear glycoproteins play important roles of DNA binding activities of the nuclear proteins.

Animals↗
PubMed1989

Change in transferrin receptor distribution in regenerating rat liver.

Partial hepatectomy results in an increase in the ability of the liver cells to bind 125I-labeled transferrin to surface receptors. Scatchard analysis of the binding of transferrin in regenerating rat liver indicates that this increase was due to an increase in the number of transferrin receptors on the cell surface. When we measured total cellular transferrin receptor number, we found that control and regenerating livers had identical amounts of receptor number. The increase in the surface receptor number is apparently due to the translocation of intracellular transferrin receptor to the cell surface.

Animals↗
PubMed1982

UDP-N-methyl-D-glucosamine-phosphate--a possible intermediate of N-methyl-L-glucosamine moiety of streptomycin.

The formation of N-methyl-L-glucosamine moiety of streptomycin from D-glucosamine by Streptomyces griseus was studied. The addition of thymine to the culture medium stimulated the formation of streptomycin and the incorporation of D-glucosamine into N-methyl-L-glucosamine moiety. During a study of sugar nucleotides in the mycelia, a novel UDP-amino sugar was isolated. The compound was formed before the maximum production of streptomycin. It was UDP-N-methyl-D-glucosamine-phosphate.

Biotransformation↗