Regulatory mechanisms of UDP-glucuronic acid biosynthesis in cultured human skin fibroblasts.
Article Details
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Castellani AA, De Luca G, Rindi S, Salvini R, Tira ME
Regulatory mechanisms of UDP-glucuronic acid biosynthesis in cultured human skin fibroblasts.
Ital J Biochem. 1986 Sep-Oct;35(5):296-303.
- PubMed ID
- 3804697 [ View in PubMed]
- Abstract
Kinetic parameters and regulatory properties of UDPGDH extracted from cultured human skin fibroblasts were determined and compared with those of UDPGDH from cornea and epiphysial-plate cartilage. Fibroblast enzyme showed an affinity for UDPG 7 times higher than cartilage enzyme and 42 times higher than cornea enzyme. UDP-xylose acted as a co-operative allosteric inhibitor, but under the same experimental conditions fibroblast enzyme was significantly less inhibited. These results were in agreement with the different GAG production of the cells we studied. Fibroblast UDPGDH activity was regulated by the NAD/NADH ratio and it was also affected by modifications of extracellular matrix composition. A significant increase of UDPGDH affinity for UDPG was observed after the treatment of the monolayers with Chase ABC.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions NADH UDP-glucose 6-dehydrogenase Protein Humans UnknownNot Available Details