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.
Wegrowski
Y
Y
Laboratoire de Biochimie, Faculté de Médecine, UPRESA CNRS 6021, Reims, France. yanusz@infobiogen.fr
Perreau
C
C
Bontemps
Y
Y
Maquart
F X
FX
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics* / Q000302:isolation & purification; D005786:Gene Expression Regulation; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011509:Proteoglycans / Q000096:biosynthesis* / Q000235:genetics; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D015398:Signal Transduction / Q000235:genetics*; D014533:Uridine Diphosphate Glucose Dehydrogenase / Q000235:genetics* / Q000378:metabolism
D018076:DNA, Complementary; D011509:Proteoglycans; D012333:RNA, Messenger; D014533:Uridine Diphosphate Glucose Dehydrogenase