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. coil ort hologs. Murine mRNA of 3.1 kb size is expressed in all the tissues stu died at a level independent of glyceraldehyde-3-phosphate dehydrogenas e (GADPH) mRNA. In human fibroblast in vitro, 2 GDH transcripts were o bserved. They were expressed proportionally to GAPDH. The simple patte rn of human GDH Southern blotting suggests a single copy gene. An anti sense oligonucleotide directed to the ATG region of the human enzyme i nhibited S-35-sulphate incorporation into extracellular macromolecules , especially proteoglycans. These data indicate that GDH expression ma y regulate proteoglycan synthesis in the cells. (C) 1998 Academic Pres s.