Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.4.99.7 (sialyltransferase)
 1,534 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To establish the basis for the reduced expression of the X determinant on leukemic blasts and the changes in antigenic expression that occur during myeloid maturation, the presence on myeloid cells of X and related structures was examined in conjunction with studies on the activities of the glycosyltransferases involved in their biosynthesis. Expression of X and sialyl-X was weak on blasts in comparison with neutrophils despite the presence of the requisite precursor structures. Much higher levels of 3-fucosyltransferase activity were found in blasts than in neutrophils when nonsialylated substrates were used, but, whereas the enzyme in neutrophils reacted equally well with 3'-sialylated and nonsialylated acceptors, the enzyme in blasts showed a marked preference for nonsialylated substrates. 6'-Sialyltransferase activity was strong in blasts but was not detectable in neutrophils, whereas a much lower level of 3'-sialyltransferase activity was present in both blasts and neutrophils. Dimethyl sulfoxide-induced maturation of HL60 cells was associated with (1) a decrease in both 6'-sialyltransferase and 3-fucosyltransferase activities, (2) a change in the substrate specificity of 3-fucosyltransferase towards that found in mature cells, and (3) increased cell surface expression of sialyl-X. These results suggest that the reduced expression of X in myeloblasts is related to the presence of the strong 6'-sialyltransferase, which uses the precursor substrate at the expense of the 3-fucosyltransferase and prevents the synthesis of X and sialyl-X. The developmental regulation of the levels of 3'- and 6'-sialyltransferases, and the level and specificity of the 3-fucosyltransferases, therefore controls the expression of X and its degree of sialylation.
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PMID:Enzymic control of the expression of the X determinant (CD15) in human myeloid cells during maturation: the regulatory role of 6-sialytransferase. 167 56

We have assayed glycosyltransferase activities during the granulocytic and macrophage-like differentiation of human promyelocytic leukemia (HL-60) cells. Functional granulocytic differentiation was assayed by the decarboxylation of 2-deoxyglucose in addition to nitroblue tetrazolium reduction. Dimethylsulfoxide (DMSO) treated HL-60 cells, induced to granulocytic differentiation, had higher 2-deoxy-glucose decarboxylation activity, and contained less sialyltransferase (ST), more fucosyltransferase (FT), and more N-acetylglucosaminyltransferase (NGT) activities than untreated cells. HL-60 cells treated with another granulocytic differentiator, retinoic acid, also had higher 2-deoxyglucose decarboxylation activity, and contained less ST, more FT, and more NGT activities than untreated cells. In contrast, cells treated with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) reported to differentiate HL-60 to macrophage-like cells, but did not show an increased level of 2-deoxyglucose decarboxylation activity, but contained more galactosyltransferase (GT) and FT activities as compared to untreated cells. These findings suggest that the alterations of glycosyltransferase levels during the differentiation of precursor cells may not depend upon different inducers, but are characteristic of the phenotypic expression of the mature cell type.
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PMID:Glycosyltransferase alterations are cell type related when human promyelocytic leukemia (HL-60) cells are treated with various inducers of differentiation. 641 38

Sodium butyrate and dimethylsulfoxide (DMSO) have marked effects on the growth, morphology, and biochemistry of two human colonic adenocarcinoma cell lines in culture. Doubling times were increased between 18% and 660% while cell viability was unaffected. Both cell lines formed colonies in soft agar in the absence of butyrate of DMSO, but no colonies were observed in the presence of these agents. However, no differences in in vivo tumorigenicities, when cells were implanted in athymic mice, were seen following treatment. Gross morphological alterations including cell enlargement, process formation, and cellular flattening occurred during culture in butyrate or DMSO. Acrylamide gel electrophoresis in sodium dodecyl sulfate revealed no change in membrane protein constituents, but autoradiographic analysis of membrane glycoproteins demonstrated differences between treated and untreated cells. Ganglioside compositions were altered, and a sialyltransferase required for the synthesis of GM3 ganglioside was elevated by butyrate. Although cytoplasmic aminooligopeptidase remained unaffected by butyrate or DMSO, brush border-associated activity was enhanced by butyrate. Alkaline phosphatase also rose dramiatically during culture in butyrate but was not enhanced by DMSO.
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PMID:Effects of sodium butyrate and dimethylsulfoxide on biochemical properties of human colon cancer cells. 735 11

Castrated male rats were subcutaneously injected testosterone (5 and 10 mg) or a mixture of beta-estradiol and progesterone (1 microg + 2 mg), to determine whether sex steroid hormones (testosterone, beta-estradiol, progesterone) might affect the content of sialoglycoproteins, the content and pattern of lipid-bound sialic acid, and the activities of sialyltransferase (SAT) I and SAT II in the Golgi-rich membrane fraction isolated from rat kidney. During four days testosterone did not affect significantly the content of proteins, sialoglycoproteins and total gangliosides, but increased the content of b-series gangliosides from 0.05 +/- 0.006 (untreated animals injected subcutaneously with 0.1 ml DMSO for four days) to 0.16 +/- 0.02 nmol sialic acid (SA) per mg protein (castrated animals injected subcutaneously with 10 mg testosterone/0.1 ml DMSO for four days). This increase was due to the increase in GD3 ganglioside from 0.03 to 0.12 nmol SA/mg protein, and to the decrease of GM3 ganglioside from 0.06 to 0.03 nmol SA/mg protein by testosterone administration. The major ganglioside in the rat kidney was GM3, constituting 63% (control group) and 51% (castrated animals injected daily with 10 mg testosterone) of all gangliosides. Castration itself induced an increase in the rat kidney SAT I and SAT II activities from 712 +/- 130 to 1723 +/- 412 pmol/h x mg protein and from 208 +/- 48 to 751 +/- 176 pmol/h x mg protein, respectively. However, subsequent administration of testosterone, at the highest concentration tested, reversed this effect. In the kidneys of castrated rats, a mixture of beta-estradiol and progesterone decreased SAT II activity from 208 +/- 48 to 87 +/- 33 pmol/h x mg protein.
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PMID:The influence of sex steroid hormones on ganglioside biosynthesis in rat kidney. 968 18