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

Sialyltransferase was measured in serum of normal and hepatoma Mc-29 bearing chickens. By preparative isoelectric focusing the multiple forms of sialyltransferase from both kind of serums was studied as well. By using influenza virus neuraminidase an attempt was made for partial structural characterization of the sialylation sites in asialofetuin applied as exogenous acceptor for sialyltransferase determination. It was established an elevated serum sialyltransferase activity in tumor bearing chickens with tumor an enzyme form was detected with pI-4.99 identical with an enzyme form described previously in solubilized plasma membrane preparations from hepatoma Mc-29. Monitoring of multiple forms of serum glycosyltransferases may be of value in answering the problem concerning the tissue origin of serum enzymes.
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PMID:Characterization of sialyltransferases from serum of normal and hepatoma Mc-29 bearing chickens. 395 42

Sialyltransferase (CMP-sialic acid:asialofetuin sialyltransferase) and human mammary epithelial antigens (HME-Ags, cell surface antigens specific to human mammary epithelial cells) were determined in plasma of nude mice grafted with breast and non-breast human tumors to assess their possible usefulness as breast cancer markers. The plasma transferase activity was significantly higher (p less than 0.01) in tumor groups relative to the control. However, no significant difference (p less than 0.05) could be found in the transferase level between breast and non-breast tumor groups, showing the enzyme's lack of specificity for breast cancer. Furthermore, the surgical procedure performed on the control normal healthy group (no tumor), resulted in an important increase of the enzyme level, while HME-Ags remained unchanged. HME-Ags were essentially negative in control as well as non-breast tumor groups. After surgical removal of breast tumors, HME-Ags level dropped drastically to the background level (from 122 to less than 30 ng/ml plasma). These data indicate that HME-Ags are more sensitive and specific than sialyltransferase as markers for human breast tumor, and suggest that HME-Ags may be clinically useful in the early detection of breast cancer as well as in the followup of patients with metastatic breast tumor.
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PMID:Breast cancer markers: comparison between sialyltransferase and human mammary epithelial antigens (HME-Ags) for the detection of human breast tumors grafted in nude mice. 397 47

Serum samples from progesterone-oestrogen-treated ovariectomized Holstein cows (N = 4) were compared with samples from control ovariectomized Holstein cows (N = 4) to determine the effects of physiological levels (0-6 ng/ml) of circulating progesterone. The average progesterone level in treated animals rose from 1 ng/ml (Day 0) to plateau at 5 ng/ml (Days 12 to 36). Sera from progesterone-oestrogen-treated cows during Days 4 to 10 significantly suppressed stimulation of lymphocytes by phytohaemagglutinin as compared with sera from control cows (P = 0.02), whereas no differences were detected in serum samples from Days 12 to 36. Serum samples from progesterone-oestrogen-treated or control cows did not affect the stimulation of lymphocytes by pokeweed mitogen. Sialyltransferase activity (P = 0.0002) and sialic acid content (P = 0.006) were both significantly elevated in serum from progesterone-oestrogen-treated animals compared with controls during Days 8 to 16, whereas no significant differences were observed at later times. The results suggest that suppression of phytohaemagglutinin-induced stimulation, sialic acid content, and sialyltransferase activity are sensitive not to the circulating level of progesterone but rather to increases in progesterone concentration, with maximal effects observed at Days 8, 12 and 12, respectively, after the start of progesterone treatment. The work provides a preliminary basis for further studies on the mechanism of immunosuppression by steroids and during pregnancy.
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PMID:Immunosuppression, sialic acid, and sialyltransferase of bovine serum as a function of progesterone concentration. 404 19

Sialyltransferase and 5'-nucleotidase were measured in the sera of 135 women with breast cancer: 53 undergoing mastectomy for primary cancer and 83 receiving different modalities of palliative therapy for metastatic disease. The objective of this study was to determine whether these enzyme levels were associated with the extent of the disease and whether changes in these enzyme levels could be correlated with success or failure of treatment. Mastectomy caused a rapid fall of elevated enzyme levels to within the normal range in all patients with stage I breast cancer but not in those with stage II or III disease. In women with metastatic disease, elevated enzyme levels fell only in patients responding to treatment. Thus serum sialyltransferase and 5'-nucleotidase activities are reliable biomarkers of breast cancer activity, and serial measurement of these enzyme activities provides a useful tool for the monitoring of disease activity and success or failure of the treatment.
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PMID:Serum sialyltransferase and 5'-nucleotidase as reliable biomarkers in women with breast cancer. 625 2

The MAT-B1 and MAT-C1 ascites sublines of the 13762 rat mammary adenocarcinoma differ in morphology, agglutinability with concanavalin A, and xenotransplantability. Both cell lines contain a major mucin-type glycoprotein, but the MAT-C1 (xenotransplantable) subline contains a 3-fold-greater content of sialic acid on the glycoprotein than does the MAT-B1 (nonxenotransplantable) subline. The present work indicates that whole cells of both lines incorporate radioactivity from labeled CMP-sialic acid into a component which comigrates with the major glycoprotein by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and that label incorporated by MAT-B1 cells is released by alkaline-borohydride treatment. Sialyltransferase can be purified from 250- to 400-fold by chromatography of a Triton X-100 extract of microsomes on CDP-agarose. The purified fraction of both cell lines has a Km for CMP-sialic acid of 0.40 +/- 0.10 mM with asialofetuin as the acceptor, and gives 35 to 40% of the activity with the acceptor asialotransferrin as with asialofetuin. When assayed with a variety of acceptors, the MAT-C1 extract showed higher sialyltransferase activity at a pH below 6.5 than did the MAT-B1 extract. Analysis of the products following incubation with lactose yields only 3'-sialyllactose for both cell lines. The results indicate that the differences in MAT-B1 and MAT-C1 sialyltransferase when assayed with glycoprotein acceptors are not large enough to account for the differences in sialic acid content of the two cell lines.
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PMID:Sialyltransferase of the 13762 rat mammary ascites tumor cells. 669 99

Two highly purified plasma membrane fractions have been obtained from mouse parotid glands by a combination of differential centrifugation and isopycnic centrifugation in discontinuous sucrose gradients. The membranes were characterized by enzymic, chemical and morphological criteria. The effect of isoproterenol, which induces parotid acinar cells to proliferate, upon sialic acid and five different enzyme activities located in the plasma membrane phosphodiesterase (EC 3.1.4.1), Mg2+-ATPase (EC 3.6.1.4), leucine aminopeptidase (EC 3.4.1.1), protein kinase (EC 2.7.1.37) and sialyltransferase (EC 2.4.99.1), were quantified along the cell cycle. Plasma membrane sialic acid content falls 30% within 30 min and remains depressed for at least 6 h with the major restoration towards normal levels occurring between 12 and 16 h later. In contrast multiple daily isoproterenol injections lead to a more than 2-fold elevation of sialic acid content. Sialyltransferase activity rises 2-fold by 12 h after isoproterenol treatment and then rapidly falls. This enzyme has a pH optimum of 6.5, requires a divalent cation for activity and is inhibited by Triton X-100. Other enzyme activities showed markedly different changes after isoproterenol stimulation, either increasing, decreasing or remaining unaltered. These continuous functional modifications suggest an active role of the plasma membrane in the control of the proliferative cycle.
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PMID:Purification of plasma membranes from mouse parotid gland and membrane reorganization in response to isoproterenol. 683 Jul 90

The level of sialyltransferase activity in leukaemic blasts from acute lymphoblastic leukaemia (ALL) cases was significantly lower (3.29 +/- 2.09 pmoles/5 X 10(7) cells or 1.77 +/- 1.16 pmoles/mg protein) than those (18.80 +/- 4.91 pmoles/5 X 10(7) cells or 7.72 +/- 1.75 pmoles/mg protein) of mature lymphocytes from normal volunteers (T less than 0.001). An inverse relationship between the level of sialyltransferase activity and the level of terminal transferase (TdT)activity was seen in blasts from eight TdT-positive ALL cases. No significant difference was observed in the level of sialyltransferase activity between ALL and cells of chronic myelogenous leukemia (CML) in blast crisis. Short Term culture of ALL blast cells with 12-0-tetradecanoylphorbol-13-acetate (TPA) at the concentration of 10-(6)M to 10-(9)M caused a marked increase in sialyltransferase activity. In one of these three ALL cases the population of TdT-positive cells and the TdT activity of the blasts decreased significantly after culture with TPA. These results suggest that biochemical differentiation of leukaemic lymphoblasts has been induced by the addition of TPA, although morphological changes were not observed. Sialyltransferase activity may be a useful indicator for the analysis of differentiation of lymphocytes.
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PMID:Sialyltransferase activity as a marker for the differentiation of lymphocytes. Increase in sialyltransferase activity of blasts from acute lymphoblastic leukaemia cases by 12-o-tetradecanoylphorbol-13-acetate (TPA). 695 64

Sialyltransferase activity of the intima-media of arterial walls is located in microsomes. The solubilization of enzyme by Triton X-100, purification by chromatography and isoelectric focusing lead to two isoenzymes (pHi 4.5 and 6.4), the second is widely predominant. Aortic sialyltransferase is sensitive to nucleotides, Mn++ dependent, and the affinity for substrate N-acetyl-neuraminic acid is 300 microM.
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PMID:[Glycoconjugate biosynthesis in the arterial wall. VIII. Separation of molecular types in microsomal sialyltransferase]. 733 43

Sialyltransferase activities and sialic acid concentrations were measured in sera form patients with malignant melanoma (n = 49), healthy control persons (n = 20), and patients with non-malignant skin disorders (n = 30). Both parameters were found to be higher in malignant melanoma patients than in healthy control persons, but they were not significantly higher in primary melanoma patients than in patients with benign skin orders, unless widespread dissemination of metastases had occurred. The highest values were found in patients with liver and lung metastases. In early stages of the disease, shedding from tumor cells seems not to be the major source of elevated serum levels of sialyltransferase and sialic acid, respectively. There is no general correlation between sialyltransferase activities and sialic acid concentrations. However, a correlation was found between serum concentrations of sialic acid and orosomucoid in patients with melanomas stage III, indicating that humoral defense mechanisms contribute to the higher values in advanced stages of the disease.
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PMID:[Clinical significant of sialic acid concentrations in the serum of melanoma patients]. 739 10

The observation that the activity of sialyltransferase (EC 2.4.99.1; serum glycoprotein:N-acetylneuraminic acid transferase) is often elevated in the serum of cancer patients necessitates an elucidation of the interrelationships of this serum enzyme with host tissues. Accordingly, the activity of this enzyme in serum, tumor, and liver was determined at various times after implantation of the R3230AC mammary carcinoma into Fischer rats. Results from samples obtained at numerous, sequential time points demonstrated that significant elevations in serum sialyltransferase enzyme activity occurred only in animals bearing large tumor burdens, i.e., greater than 20 g, or in animals with tumors present for longer than 21 days. In these tumor-bearing rats, the activity of sialyltransferase increased in liver tissue at 21 to 25 days concurrently with the increase in serum enzyme activity, suggesting that the liver may be a potential source of the serum enzyme. Sialyltransferase activity in tumor tissue was quite variable; the activity increased one week after tumor implantation and remained at the same level thereafter. When tumors were excised, the activity of the serum enzyme returned to control values within four days after surgery, suggesting that the half-life of serum sialyltransferase was two days. Serum enzyme levels were again elevated upon regrowth of the tumor. These results show that the serum sialyltransferase alters its activity in conjunction with changes in tumor burden.
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PMID:Correlation of serum, tumor, and liver serum glycoprotein: N-acetylneuraminic acid transferase activity with growth of the R3230AC mammary tumor in rats and relationship of the serum activity to tumor burden. 742 28


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