Uridine diphosphoglucose dehydrogenase activity in normal and osteoarthritic human chondrocytes.
The activity of uridine diphosphoglucose dehydrogenase (UDPGD), a key enzyme in the synthesis of proteoglycans was measured by a quantitative cytochemical method in normal and in osteoarthritic (OA) human cartilage. Normal adult chondrocytes showed low UDPGD activity, which was about half the activity of glucose-6-phosphate dehydrogenase of the same specimens. No significant increase in UDPGD activity was noted in OA chondrocytes. The lack of significantly enhanced UDPGD activity in OA indirectly agrees with studies showing normal 35S uptake in this disease and might explain in part the inability of chondrocytes to cope with continuous proteoglycan loss.
H. Schussheim Rheumatology Research Laboratory, Faculty of Medicine, Technion-Israel Institute of Technology, Haifa.
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Zemel
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Nahir
D000818:Animals; D002237:Carbohydrate Dehydrogenases / Q000032:analysis*; D002358:Cartilage, Articular / Q000201:enzymology* / Q000473:pathology; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D010003:Osteoarthritis / Q000201:enzymology* / Q000473:pathology; D011509:Proteoglycans / Q000096:biosynthesis; D011817:Rabbits; D014533:Uridine Diphosphate Glucose Dehydrogenase / Q000032:analysis*
D011509:Proteoglycans; D002237:Carbohydrate Dehydrogenases; D014533:Uridine Diphosphate Glucose Dehydrogenase; D005954:Glucosephosphate Dehydrogenase