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      Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase.

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          Abstract

          Regulation of proteoglycan and glycosaminoglycan synthesis is critical throughout development, and to maintain normal adult functions in wound healing and the immune system, among others. It has become increasingly clear that these processes are also under tight metabolic control and that availability of carbohydrate and amino acid metabolite precursors has a role in the control of proteoglycan and glycosaminoglycan turnover. The enzyme uridine diphosphate (UDP)-glucose dehydrogenase (UGDH) produces UDP-glucuronate, an essential precursor for new glycosaminoglycan synthesis that is tightly controlled at multiple levels. Here, we review the cellular mechanisms that regulate UGDH expression, discuss the structural features of the enzyme, and use the structures to provide a context for recent studies that link post-translational modifications and allosteric modulators of UGDH to its function in downstream pathways.

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          Author and article information

          Journal
          J Histochem Cytochem
          The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
          SAGE Publications
          1551-5044
          0022-1554
          January 2021
          : 69
          : 1
          Affiliations
          [1 ] Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina.
          Article
          10.1369/0022155420947500
          7780191
          32749901
          08346727-0d1a-4d4d-a5cf-bc1bda9c85aa
          History

          developmental disorders,extracellular matrix,proteoglycan,post-translational modifications,nucleotide sugars,hyaluronan,glycosaminoglycan,glucuronidation,UDP-glucuronate

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