Abnormal Activity Of The Enzymes Responsible For Gag Sulfation In Diabetes

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To date three different forms of N-deacetylase/N-sulfotransferase have been cloned [37,38]. The activity of N-deacetylase/N-sulfotransferase is approximately 40% lower in hepatocytes from streptozotocin diabetic rats as compared with control cells [39]. Furthermore, Kofoed-Enevoldsen et al [4042] found a reduction in N-deacetylase/N-sulfotransferase activity in streptozotocin diabetic rats. In humans, the activity or gene expression of N-deacetylase/N-sulfotransferase has been evaluated in cell cultures of skin fibroblasts obtained from diabetic patients with/without diabetic nephropathy. Neither the activity of N-deacetylase/N-sulfotransferase in type 1 diabetics [43] nor mRNA levels of N-deacetylase/N-sulfotransferase 1 and 2, in type 2 diabetic patients [44] levels were altered. Interestingly, only the N-deacetylase/N-sulfotransferase 2 gene expression was down-regulated by diabetes, but this was only in skin fibroblasts, not in mesangial cells [44].

It should be recognized that N-deacetylase/N-sulfotransferase 1 and 2 enzymes are not the only enzymes involved in HS-PG sulfation. Indeed, N-deacetylase/N-sulfotransferase 3, epimerase and the 3-O-sulfotransferases may also substantially contribute to HS-PG sulfation. Interestingly, while there is no data in the literature on the effect of the diabetic milieu on the activity of the two former, quite recently Edge and Spiro [45] have obtained findings suggesting an abnormal activity of isoforms of 3-O-sulfotransferase. Indeed, a highly specific reduction in the disaccharide unit IdUA(2S)a1^4GlcN(3S) was observed in the GBM from kidneys of patients (not reported whether type 1 or 2 diabetics) with diabetic nephropathy. This disaccharide unit has so far been found only in the HS from GBM in substantial quantities representing approximately 20% of all HS disaccharide units.

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