Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.1.53 (sialidase)
2,694 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

By selection for plastic adhesiveness we have previously established a variant tumor line (ESb-MP) from the metastatic murine lymphoma ESb. In contrast to the parental line, the adhesion variant is significantly decreased in malignancy and is altered in the capacity to bind soybean agglutinin (SBA) lectin. Here we show biochemically that the major SBA-binding cell-surface component of ESb-MP cells is the T200 glycoprotein. In ESb cells, T200 antigens bind SBA only after sialidase treatment. Enzymatic studies suggested that glycans detected by the lectin with or without sialidase treatment are different. Inhibition of N-glycosylation by tunicamycin and biosynthetic labeling revealed two T200 chains for ESb-MP cells that were larger in size than the single chain detected in ESb cells. Studies on the biosynthesis revealed that ESb-MP cells expressed two precursor chains for T200 whereas ESb cells displayed only one. There was no size difference detectable in the mature T200 molecules of ESb and ESb-MP cells. Our data suggest that the molecules differ in expression of O-linked glycans that can be recognized by SBA. Additional O-linked sugars on ESb-MP T200 molecules seem to be expressed in particular after trimming of the second T200 precursor chain.
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PMID:Structural basis for altered soybean agglutinin lectin binding between a murine metastatic lymphoma and an adhesive low malignant variant. 244 94

Glycolipids of murine lymphoma cell lines with low metastatic (Eb) and high metastatic (ESb) potentials have been investigated. The Eb cell line was characterized by a high quantity of gangliotriaosylceramide (Gg3), gangliotetraosylceramide (Gg4), GM1b, and a new type of disialoganglioside, termed GD1 alpha. In contrast, the high metastatic ESb cell line was characterized by the absence of these glycolipids and instead by the presence of GM3, GM2, GM1a, GD1a, and GD1b gangliosides. A clear cell surface reactivity with monoclonal antibody anti-Gg3 (2D4) was observed only in Eb cells. Thus, Eb cells are distinct from ESb cells in their ability to add the GalNAc residue to LacCer, supplying Gg3 for synthesis of a series of glycolipids via an asialogangliotetraosyl pathway, while ESb cells are capable of synthesizing GM3, which initiates synthesis of ganglio-series gangliosides GM2, GM1a, GD1a, and GD1b. While disialogangliosides of ESb cells were identified as GD1a and GD1b, a disialoganglioside isolated from Eb cells was characterized as having a novel structure (referred to as GD1 alpha) as follows: (formula; see text) Thus, Eb and ESb cells are clearly different in their qualitative sialylation patterns, i.e., the position of sialic acid residues. Cell surface labeling with galactose-oxidase/NaB[3H]4 revealed a high exposure of Gg3 and Gg4 at the Eb cell surface, while both labels were absent in ESb cells. In contrast, ESb cells showed a substantial label at GM1a, which was greatly enhanced after sialidase treatment.
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PMID:Qualitative differences in position of sialylation and surface expression of glycolipids between murine lymphomas with low metastatic (Eb) and high metastatic (ESb) potentials and isolation of a novel disialoganglioside (GD1 alpha) from Eb cells. 348 80

We have generated and characterized three new monoclonal antibodies (mAbs), termed SN3, SN3a, and SN3b, which are directed to sialic acid of a glycoprotein(s) on human non-T leukemia cells. These mAbs were generated by immunizing mice with an antigen preparation isolated from cell-membrane glycoconjugates of NALM-1, a pre-B leukemia cell line. The initial characterization of the mAbs consisted of a sensitive cellular radioimmunoassay against various cultured human leukemia-lymphoma (HLL) and nonmalignant cell lines. They strongly reacted with all four (all three in the case of SN3a) non-T/non-B HLL cell lines tested and both pre-B HLL cell lines tested. However, they reacted with only one of three B HLL cell lines tested. In addition, these mAbs did not react with other cell lines, which include T- and myelomonocytic HLL cell lines and nonmalignant B-cell lines. Normal peripheral blood cells were also tested; the mAbs reacted with B cells and granulocytes but not with T cells, monocytes, erythrocytes, or platelets. In a test using SN3 and SN3b with uncultured cell specimens derived from various cancer patients, the mAbs primarily reacted with non-T/non-B and B HLL specimens, as well as with chronic myelocytic leukemia specimens. The biochemical nature of antigenic determinants defined by the three mAbs was studied by treating the non-T leukemia cells with sialidase and proteases. The results show that the antigenic determinants defined by these mAbs all contain a sialic acid residue(s) that is attached to the cells via a protein backbone(s). Competitive binding experiments show that binding of SN3 to the leukemia cells was blocked almost completely by SN3a and SN3b, as well as by BA-1. Both SN3 and SN3a are IgG1 antibodies, whereas SN3b is an IgM antibody; SN3b showed a strong complement-mediated cytotoxic activity against non-T leukemia cells.
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PMID:New monoclonal antibodies SN3, SN3a, and SN3b directed to sialic acid of glycoprotein on human non-T leukemia cells. 348 35

It is reported that concanavalin A (conA) and wheat germ agglutinin (WGA) have a differential binding pattern on normal mouse spleen lymphocytes and the surface of Dalton's lymphoma cells. It is suggested that sialic acid on the cell surface controls the expression of lectin binding sites. Further, it has been observed that the increased release of sialic acid from cell surfaces after cis-dichlorodiammine platinum (II) (cis-Platin) treatment is due to the increased activity of sialidase.
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PMID:Differential binding of conA and WGA on the cell surface, the role of sialic acid in their expression and the increased activity of sialidase after cis-Platin treatment. 391 32

The effects of the sequential application of specific glycosidases on surfaces of living mammalian cells were studied with respect to their ability to bind the beta-galactoside-specific lectin, Ricinus communis agglutinin (RCA). Sialidase and beta-galactosidases from different sources were tested for their actions on two strains of mouse lymphoma cells differing markedly in their metastatic potential. Binding studies were performed by quantitative flow cytometry with fluorescent RCA, and numbers of specific binding sites and equilibrium association constants for the lectin on living cells were determined before and after the various enzyme treatments. Although the number of binding sites for native and sialidase-treated cells were almost identical for both cell strains, differences in the apparent affinity constants could be detected. Differences between the two strains became even more pronounced, also with respect to the number of binding sites, after treatment with beta-galactosidases from S. pneumoniae and from bovine testis. It is suggested that such combined strategies provide valuable tools for the differentiation of surface carbohydrate moieties on intact living cells, especially for comparative purposes.
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PMID:The effect of specific glycosidases on Ricinus communis agglutinin binding to cell surfaces of two tumor sublines. A comparative flow-cytometric study. 621 Jan 45

In our previous study, a Burkitt lymphoma-associated antigen defined by a monoclonal antibody, designated 38.13, was characterized as globotriaosylceramide (Gb3, Gal alpha 1----4 Gal beta 1----4 Glc beta 1----1 Cer) (Nudelman, E., Kannagi, R., Hakomori, S., Parsons, M., Lipinski, M., Wiels, J., Fellous, M., and Tursz, T. (1983) Science (Wash. D.C.) 220, 509-511). Consequently, we have studied the enzymatic basis and organization of Gb3 expression in Burkitt as compared with non-Burkitt lymphoblastoid cell lines. Burkitt lymphoma cell lines (Ramos, Daudi, Put) were characterized by a high chemical quantity of Gb3, high enzyme activity for synthesis of Gb3 (UDP-Gal:LacCer alpha-galactosyltransferase), and a high degree of surface exposure of Gb3, as determined by galactose oxidase/NaB[3H]4 and by cytofluorometry with the monoclonal antibody to Gb3 (38.13). Non-Burkitt lymphoblastoid cell lines (Priess, Remb1, and ARH77) were characterized by the absence of Gb3 at the cell surface detected by cytofluorometry or cell-surface labeling. The cell lines Priess and Remb1 did not contain Gb3 and showed a low alpha-galactosyltransferase activity for Gb3 synthesis. However, the cell line ARH77, though it did not express Gb3 at the cell surface, was found to contain a large chemical quantity of Gb3 and a high level of alpha-galactosyltransferase activity for Gb3 synthesis. However, Gb3 of ARH77 cells was exposed by sialidase treatment, but not by protease treatment, although Gb3 itself was not sialylated. The crypticity of Gb3 in ARH77 cells could be associated with an adjacent sialosyl residue of a second glycoconjugate at the cell surface, in the same way as Gg3 in mouse lymphoma L5178 (Urdal, D. L., and Hakomori, S. (1983) J. Biol. Chem. 258, 6869-6874). Thus, the expression in Burkitt and non-Burkitt lymphoma is dependent on (i) Gb3 synthesis due to alpha-galactosyltransferase activity and (ii) membrane organization of Gb3, which may be controlled through interaction with the sialosyl residue of a second glycoconjugate.
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PMID:Enzymatic and organizational difference in expression of a Burkitt lymphoma-associated antigen (globotriaosylceramide) in Burkitt lymphoma and lymphoblastoid cell lines. 643 3

The sialic acid content of erythrocytes from healthy individuals of different blood types and of patients with known hematological disorders has been determined. The sialic acid was completely released enzymatically with sialidase and quantitated by the thiobarbituric acid method. The sialic acid content of erythrocytes was constant irrespective of ABO blood type, or anticoagulant used; viz, 0.85-0.92 mumoles/ml of packed erythrocytes or 46-53 X 10(6) sialyl residues per cell. Deviations from these normal values were obtained with erythrocytes from patients with a variety of hematological disorders. Patients with the following disorders have significantly (P less than 0.01) lower sialic acid values compared to erythrocytes from healthy individuals (given in the order of decreasing sialic acid content): sickle cell anemia, acute lymphocytic leukemia, chronic lymphocytic leukemia, acute myelomonocytic leukemia, non-Hodgkin lymphocytic lymphoma, chronic granulocytic leukemia, acute myelocytic leukemia, leukemia, and Hodgkin disease.
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PMID:Sialic acid content of erythrocytes in normal individuals and patients with certain hematologic disorders. 721 33

Roles of surface sialic acid residues in cell adhesion to substratum were investigated in model systems to clarify their contribution to intercellular interactions. Treatment of cells of a fibroblastic cell line, Swiss 3T3, an epithelial cell line, TES-1, and a T lymphoma cell line, BW5147, with a sialylated oligosaccharide binding lectin enhanced adhesion to plastic plates irrespective of the cell lineage. This enhancement was inhibited by the addition of sialyl lactose. Digestion of the cells with sialidase or endoglycoceramidase also augmented adhesion. On the other hand, adhesion was reduced by pre-coating plastic plates with gangliosides but not with desialylated gangliosides. These findings suggest that sialic acid residues exposed to cell surfaces negatively regulate cell adhesiveness.
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PMID:Repulsive contribution of surface sialic acid residues to cell adhesion to substratum. 798 55

Chronic myelogenous leukemia (CML) granulocytes exhibit a number of characteristics attributable to immature granulocytes, including marked increases in cell surface sialylation of glycoproteins which may be due, at least in part, to an increased activity of cytidine 5'-monophosphate-N-acetylneuraminic acid:Ga1 beta 1-3Ga1NAc alpha(2-3)-sialyltransferase (EC 2.4.99.4), and perhaps to altered activity of other glycosyltransferases and sialidases. This aberrant sialylation of CML granulocytes contributes to the decreased binding of the synthetic chemotactic peptide, formyl Met Leu Phe (fMLP), to the surface of CML granulocytes which leads to a rapid, transient increase in cytosolic free calcium ([Ca2+]i), an integral step in the biochemical cascade leading to cell activation. To determine if the decrease in binding of fMLP to CML granulocytes translates into a functional deficit, we measured fMLP-induced increases in [Ca2+]i. Compared to normal granulocytes, fMLP-induced increases in [Ca2+]i were markedly decreased in CML granulocytes. After sialidase treatment, a significant augmentation in fMLP-induced increases in [Ca2+]i was noted in CML granulocytes, indicating that the decreased signalling may be a consequence of aberrant sialylation. To determine if the effects of aberrant sialylation also alters the binding of endogenous polypeptide mediators, we determined the effect of desialylation of CML and normal granulocytes on binding of the colony stimulating factor for granulocytes and monocytes (GM-CSF), which plays a role in differentiation and proliferation of myeloid-lineage cells. As with fMLP binding, we also showed that the binding of GM-CSF to CML granulocytes, but not normal granulocytes, was markedly increased after sialidase treatment. Similarly, binding of GM-CSF to undifferentiated HL-60 cells was markedly increased after sialidase treatment. Therefore, we have demonstrated that aberrant sialylation of CML granulocytes not only alters the binding of fMLP and GM-CSF to their receptor(s), but may also alter signal transduction. Thus, aberrant glycosylation of CML granulocytes may reduce the binding of hematopoietic growth factors, which in turn may be responsible for the immature phenotype of CML granulocytes.
Leuk Lymphoma 1993 Sep
PMID:Role of aberrant sialylation of chronic myeloid leukemia granulocytes on binding and signal transduction by chemotactic peptides and colony stimulating factors. 822 Jan 57

The B-lymphotropic papovavirus (LPV) productively infects only a subset of human B-lymphoma-derived cell lines while transfection of the viral genome yields infectious viral particles in a much wider variety of human hematopoietic cell lines. We have analyzed the contribution of a putative LPV receptor on the cell surface of B-cell lines in restricting the virus host range. In order to establish a quantitative virus binding assay for LPV, infectious virus particles were highly purified by metrizamide equilibrium density centrifugation and used as immunogens to raise seven mouse monoclonal antibodies specific for LPV VP1. Virus particle binding was quantitated in an indirect, nonradioactive assay with an LPV VP1-specific enzyme-linked immunosorbent assay. Binding of LPV particles to permissive human B-lymphoma cell line BJA-B occurred within minutes. Kinetics and capacity of binding were similar at 4 and 37 degrees C. A BJA-B cell was estimated to bind approximately 600 virus particles at conditions under which 50% of the administered virus was bound. The sialidase and trypsin sensitivities of the cellular virus binding moiety show that sialylated and proteinaceous components are necessary components of the LPV receptor on BJA-B cells. Despite a high binding capacity of BJA-B cells for simian virus 40, LPV binding was not significantly affected by a 20-fold excess of simian virus 40 particles, indicating that these related polyomaviruses do not bind to the same receptor on BJA-B cells. Reduction of LPV binding to sialidase-pretreated BJA-B cells was accompanied by a similar reduction of infection, indicating that virus binding may be a limiting factor in the LPV replicative cycle. The two highly LPV-permissive human B-lymphoma cell lines BJA-B and Namalwa displayed high virus binding whereas low and nonpermissive hematopoietic cell lines showed reduced or undetectable virus binding. We conclude that the inability of LPV particles to productively infect the nonpermissive human hematopoietic cell lines analyzed is probably due to the absence or insufficient expression of a functional cell surface receptor.
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PMID:The cell surface receptor is a major determinant restricting the host range of the B-lymphotropic papovavirus. 823 Apr 69


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