Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lactosylceramide sulfate and galactosylceramide sulfate were found to be increased markedly in human renal cell carcinoma (adenocarcinoma) as compared to uninvolved tissue, while neither of them were found in human nephroblastoma tissues. Activities of two sulfotransferases toward galactosyl ceramide and lactosylceramide as substrates were significantly elevated in the renal cell carcinoma compared to the uninvolved, endorsing enhanced synthesis of the two sulfatides in the renal cell carcinoma. The levels of elevated activities of two sulfotransferases were parallel in most renal cell carcinomas. In nephroblastoma tissues, the activity of sulfotransferase was not detected or only in trace, if any. No consistent change in the activity of arylsulfatase A which disulfate two sulfatides was observed in nephroblastoma and renal cell carcinoma as compared to that in the uninvolved tissue. In the nephroblastoma and the renal cell carcinoma, neolactosylceramide was detected but not in the uninvolved tissue. The present results show that the increased sulfatide (s) in the renal cell carcinoma and the disappearance of the sulfatides in the nephroblastoma are biochemical characteristics of histologically different carcinoma.
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PMID:[Glycolipid alterations in human kidney carcinoma]. 254 45

Paracrine signaling between podocytes and glomerular endothelial cells through vascular endothelial growth factor A (VEGFA) maintains a functional glomerular filtration barrier. Heparan sulfate proteoglycans (HSPGs), located on the cell surface or in the extracellular matrix, bind signaling molecules such as VEGFA and affect their local concentrations, but whether modulation of these moieties promotes normal crosstalk between podocytes and endothelial cells is unknown. Here, we found that the transcription factor Wilms' Tumor 1 (WT1) modulates VEGFA and FGF2 signaling by increasing the expression of the 6-O-endosulfatases Sulf1 and Sulf2, which remodel the heparan sulfate 6-O-sulfation pattern in the extracellular matrix. Mice deficient in both Sulf1 and Sulf2 developed age-dependent proteinuria as a result of ultrastructural abnormalities in podocytes and endothelial cells, a phenotype similar to that observed in children with WT1 mutations and in Wt1(+/-) mice. These kidney defects associated with a decreased distribution of VEGFA in the glomerular basement membrane and on endothelial cells. Collectively, these data suggest that WT1-dependent sulfatase expression plays a critical role in maintaining the glomerular filtration barrier by modulating the bioavailability of growth factors, thereby promoting normal crosstalk between podocytes and endothelial cells.
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PMID:WT1-dependent sulfatase expression maintains the normal glomerular filtration barrier. 2171 93