UDP-glucuronate decarboxylase (UGD; EC 4.1.1.35) catalyzes the formation of UDP-xylose from UDP-glucuronate. UDP-xylose is then used to initiate glycosaminoglycan biosynthesis on the core protein of proteoglycans.
The topology of the deduced 420-amino acid protein was consistent with a type II transmembrane protein. Northern blot analysis of rat tissues detected a single UGD transcript with highest levels in heart, brain, and testes. Substantial levels were also detected in kidney, liver and lung, and lower levels in spleen and skeletal muscle. Western blot analysis demonstrated highest levels of the protein in kidney, liver, and brain, with negligible staining in heart, spleen, skeletal muscle, lung, and testes. Subcellular studies and histochemistry localized the protein to the perinuclear Golgi.
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