Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study.

Abstract

Using a reverse-transcriptase-polymerase chain reaction approach human and murine UDPG-dehydrogenase (GDH) was cloned from fibroblast mRNAs. Human enzyme is 97% and 27% identical with its murine and E. coli orthologs. Murine mRNA of 3.1 kb size is expressed in all the tissue studied at a level independent of glyceraldehyde-3-phosphate dehydrogenase (GADPH) mRNA. In human fibroblast in vitro, 2 GDH transcripts were observed. They were expressed proportionally to GAPDH. The simple pattern of human GDH Southern blotting suggests a single copy gene. An antisense oligonucleotide directed to the ATG region of the human enzyme inhibited 35S-sulphate incorporation into extracellular macromolecules, especially proteoglycans. These data indicate that GDH expression may regulate proteoglycan synthesis in the cells.

Cite this paper

@article{Wegrowski1998UridineDD, title={Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study.}, author={Yanusz Wegrowski and Corinne Perreau and Yannick Bontemps and F. X. Maquart}, journal={Biochemical and biophysical research communications}, year={1998}, volume={250 2}, pages={206-11} }