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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study. Wegrowski, Y., Perreau, C., Bontemps, Y., Maquart, F.X. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
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