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Uridine diphosphoglucose dehydrogenase activity in normal and osteoarthritic human chondrocytes.

作者信息

Zemel E, Nahir A M

机构信息

H. Schussheim Rheumatology Research Laboratory, Faculty of Medicine, Technion-Israel Institute of Technology, Haifa.

出版信息

J Rheumatol. 1989 Jun;16(6):825-7.

PMID:2778766
Abstract

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.

摘要

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引用本文的文献

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UDP-glucose dehydrogenase modulates proteoglycan synthesis in articular chondrocytes: its possible involvement and regulation in osteoarthritis.UDP-葡萄糖脱氢酶调节关节软骨细胞中蛋白聚糖的合成:其在骨关节炎中的可能作用及调控
Arthritis Res Ther. 2014 Dec 3;16(6):484. doi: 10.1186/s13075-014-0484-2.
2
Structural basis of cooperativity in human UDP-glucose dehydrogenase.人源 UDP-葡萄糖脱氢酶协同作用的结构基础。
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3
Study of the effect of a glycosaminoglycan-peptide complex on the degradative enzyme activities in human osteoarthritic cartilage.
糖胺聚糖-肽复合物对人骨关节炎软骨中降解酶活性影响的研究。
Clin Rheumatol. 1990 Sep;9(3):383-8. doi: 10.1007/BF02114400.