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Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study
Y Wegrowski1, C Perreau, Y Bontemps
1Laboratoire de Biochimie, Faculté de Médecine, UPRESA CNRS 6021, Reims, France. yanusz@infobiogen.fr
Biochemical and Biophysical Research Communications
|October 1, 1998
Summary
This study cloned UDP-glucose dehydrogenase (GDH) and found its expression regulates proteoglycan synthesis. Inhibiting human GDH reduced sulfate incorporation into extracellular macromolecules, highlighting GDH
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- UDP-glucose dehydrogenase (GDH) is crucial for synthesizing UDP-glucuronic acid, a precursor for glycosaminoglycans.
- The role of GDH in proteoglycan synthesis requires further elucidation at the molecular level.
Purpose of the Study:
- To clone and characterize human and murine UDP-glucose dehydrogenase (GDH) genes.
- To investigate the role of GDH in proteoglycan synthesis in human fibroblasts.
Main Methods:
- Reverse-transcriptase polymerase chain reaction (RT-PCR) for gene cloning.
- Southern blotting for gene copy number analysis.
- Antisense oligonucleotide inhibition assay to study gene function.
Main Results:
- Human and murine GDH were successfully cloned, showing high sequence identity between species.
- GDH mRNA expression was detected in various tissues, independent of GAPDH mRNA levels.
- Inhibition of human GDH with antisense oligonucleotides significantly reduced proteoglycan synthesis.
Conclusions:
- GDH is expressed as a single-copy gene in humans.
- GDH expression plays a regulatory role in cellular proteoglycan synthesis.