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

First Author  Wegrowski Y Year  1998
Journal  Biochem Biophys Res Commun Volume  250
Issue  2 Pages  206-11
PubMed ID  9753608 Mgi Jnum  J:50102
Mgi Id  MGI:1289867 Doi  10.1006/bbrc.1998.9262
Citation  Wegrowski Y, et al. (1998) Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study. Biochem Biophys Res Commun 250(2):206-11
abstractText  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.
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