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)

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

The relationship between the mitogenic activity of influenza type A viruses for murine B lymphocytes and the receptor-binding specificity of their hemagglutinin was examined. Receptor-binding specificity was determined by the ability of the virus to agglutinate erythrocytes that had been sialidase treated and then enzymatically resialylated to contain sialyloligosaccharides with defined sequences. Distinct differences in receptor-binding specificity were observed between strongly and weakly mitogenic viruses of the H3 subtype, with strong mitogenic activity correlating with the ability of the virus to recognize the sequence N-glycolylneuraminic acid alpha 2,6 galactose (NeuGc alpha 2,6Gal). Viruses isolated early in the evolution of the H3 subtype (from 1968 to 1971) are relatively weak mitogens and recognize the sequence N-acetylneuraminic acid alpha 2,6 galactose (NeuAc alpha 2,6Gal) but not NeuGc alpha 2,6Gal. H3 viruses isolated since 1972 are strongly mitogenic, and these viruses recognize both NeuGc alpha 2,6Gal and NeuAc alpha 2,6Gal. The amino acid substitution of Tyr for Thr at residue 155 of HA1 may be critical to this change in receptor-binding specificity and mitogenic activity of the later H3 viruses. Horse serum-resistant variants of H3 viruses, which bind preferentially to the sequence NeuAc alpha 2,3Gal, are poorly mitogenic. Differences were also observed between the receptor-binding specificity of the strongly mitogenic H3 viruses and viruses of the H2 and H6 subtypes, the mitogenic activity of which is limited to strains of mice that express the class II major histocompatibility complex glycoprotein I-E. The results indicate that the receptor-binding specificity of the hemagglutinin plays a critical role in determining the mitogenic activity of influenza viruses.
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PMID:Relationship between mitogenic activity of influenza viruses and the receptor-binding specificity of their hemagglutinin molecules. 349 May 81

A lectin isolated from Rana catesbeiana eggs preferentially agglutinates a large variety of human and animal tumor cells but not normal red blood cells, lymphocytes, or fibroblasts. The phenomenon correlates with a higher binding activity of the lectin with tumor cells. Chemical and physical analysis of the purified lectin indicates that the lectin is a low molecular weight basic polypeptide with five intrachain disulfide bonds. Its agglutination of tumor cells was abolished by blocking the amino group. The lectin strongly binds with a large variety of tumor cells but binds only minimally with fibroblasts, lymphocytes, and erythrocytes. Tumor cell agglutination induced by this lectin was strongly inhibited by submaxillary mucin, to a lesser degree by fetuin and keratan sulfate, and not at all by less-sialylated glycoproteins, such as transferrin. Inhibition by mucin or fetuin was greatly reduced by desialylation of glycoprotein with sialidase. Treatment of tumor cells with sialidase greatly reduced the lectin-dependent agglutination, and the sialidase-dependent reduction of tumor cell agglutination was inhibited by the sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid. However, tumor cell agglutination was not inhibited by chondroitin sulfates or hyaluronic acid. Thus, the lectin-dependent tumor cell agglutination is due to a high density of sialic acid at the cell surface. The receptor glycoprotein that interacts with this lectin was demonstrated in the detergent-insoluble fraction of a variety of tumor cells by sodium dodecyl sulfate:polyacrylamide gel electrophoresis, followed by Western blotting with lectin and anti-lectin antibodies. The presence of a common high molecular weight lectin-binding glycoprotein in various tumor cells was demonstrated.
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PMID:Isolation and characterization of Rana catesbeiana lectin and demonstration of the lectin-binding glycoprotein of rodent and human tumor cell membranes. 349 12

Plasma of normal human individuals was shown to contain an inhibitor of Trypanosoma cruzi neuraminidase (NAase; acylneuraminyl hydrolase, sialidase, EC 3.2.1.18). The inhibitor has been purified to homogeneity by PEG precipitation, CM Affi-Gel Blue Sepharose chromatography, and gel filtration. The purified preparation inhibits T. cruzi NAase at a concentration as low as 10(-9) M and has no effect at concentrations at least 100 times higher on any of the other NAases tested, including those from influenza virus, the closely related trypanosome Trypanosoma rangeli, and mammalian NAases. The inhibitor is unique in that it prevents T. cruzi desialylation of intact mammalian cells but does not prevent desialylation of soluble glycoconjugates. In addition, the isolated material is effective in inhibiting the T. cruzi NAase whether the enzyme is on the parasite outer membrane or in solution. Molecular characterization indicates that the inhibitor is a glycoprotein with a Mr of 246,000 +/- 20,000 composed of subunits of Mr 28,000 +/- 2000. Its plasma concentration is at least 60 micrograms/ml. The mechanism of action has not been fully elucidated, but it appears to be noncompetitive. Attempts to match the isolated NAase inhibitor with known plasma glycoproteins have not been successful. In view of this and of the specificity of the inhibitor for T. cruzi, we have named the inhibitor "cruzin." This finding suggests a different approach in investigating the role that NAase plays in host-parasite interaction.
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PMID:Specific inhibition of Trypanosoma cruzi neuraminidase by the human plasma glycoprotein "cruzin". 355 30

With methylumbelliferyl-N-acetyl-neuraminic acid (MU-NANA) as substrate, acid sialidase was determined in intestinal biopsies of children. The enzyme has an acid pH optimum, a Km value of 4 mmol/l and a pronounced thermal lability which can be partially prevented by the addition of albumin. N-acetyl-neuraminic acid (NANA) and derivatives as well as other glycoprotein and oligosaccharide sialidase substrates inhibit sialidase whereas gangliosides have no effect. This could be an indication that intestinal MU-NANA sialidase is different from ganglioside sialidase as has been reported for many other tissues.
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PMID:Characteristics of human intestinal acid sialidase. 358 18

An oligosaccharide alditol, dHex-GalNAc-Gal-Gal-GalNAcol, has been isolated from polysialoglycoprotein, which was derived from the unfertilized eggs of Savelinus leucomaenis pluvius (a salmonid fish, Iwana in Japanese), by alkaline borohydride treatment followed by exhaustive digestion with sialidase. First, the structure of the terminal dHex residue in the above pentasaccharide has been assigned as 6-deoxyaltrose (= dAlt in pyranoid form) by a combination of structural methods (GLC, TLC, mass spectrometry, and 400-MHz 1H-NMR spectroscopy). The occurrence of a 6-deoxyhexose other than L-fucose in glycoprotein has not been previously reported. Next, the absolute configuration of this unusual sugar residue has been assigned as D on the basis of the exciton-splitting study of tris-p-bromobenzoate derivatives of methyl 6-deoxyaltrosides. The usefullness of this circular dichroic exciton-splitting method in the determination of the absolute configuration of carbohydrate components, only available in minute amounts, is emphasized. The anomeric configuration of the glycosidic linkage of the D-altropyranosyl residue was deduced from 400-MHz 1H NMR spectroscopy. The 6-deoxy-beta-D-altropyranosyl residue thus established has the same configuration as alpha-L-fucose but with the C-5 methyl group inverted, suggesting that the biosynthetic incorporation of D-dAlt parallels that of L-fucose, and a possible pathway is also considered.
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PMID:Identification and determination of absolute and anomeric configurations of the 6-deoxyaltrose residue found in polysialoglycoprotein of Salvelinus leucomaenis pluvius eggs. The first demonstration of the presence of a 6-deoxyhexose other than fucose in glycoprotein. 366 14

A new human erythrocyte glycoprotein has been identified by immunoblotting with murine monoclonal antibodies under non-reducing conditions. The glycoprotein has a MW of 70,000 and carries Cromer-related blood group antigens. The monoclonal antibodies also react with normal peripheral blood leucocytes and platelets and several haemopoietic cell lines. The glycoprotein has a reduced MW after sialidase treatment. The MW is markedly reduced in Tn erythrocyte membranes and slightly increased in Cad erythrocyte membranes. These results suggest that the glycoprotein has a substantial content of O-glycans. The glycoprotein appears to be absent from, or grossly altered in, the erythrocytes of two individuals with the rare Inab phenotype.
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PMID:A human cell-surface glycoprotein that carries Cromer-related blood group antigens on erythrocytes and is also expressed on leucocytes and platelets. 367 86

In order to assess metabolic recycling of sialic acid, GM1 ganglioside [nomenclature of Svennerholm (1964) J. Lipid. Res. 5, 145-155; IUPAC-IUB Recommendations (1977) Lipids 12, 455-468], 14C-radiolabelled at the acetyl group of sialic acid, was intravenously injected into Wistar rats, and the presence of radioactive sialic acid in liver sialoglycolipids (gangliosides) and sialoglycoproteins was ascertained. A time-course study (20 min-72 h) showed that the radioactivity present in the liver distributed in the following fractions, with reciprocal proportion varying with time: the protein (glycoprotein) fraction, the ganglioside fraction and the diffusible fraction, which contained low-Mr compounds, including sialic acid. Ganglioside-linked radioactivity gradually decreased with time; protein-linked radioactivity appeared soon after injection (20 min), reached a maximum around 20 h, then slowly diminished; diffusible radioactivity provided a sharp peak at 4 h, then rapidly decreased till disappearing after 40 h. The behaviour of bound radioactivity in the individual liver gangliosides was as follows: (a) rapid diminution with time in GM1, although with a lower rate at the longer times after injection; (b) early appearance (20 min) with a peak at 1 h, followed by continuous diminution, in GM2; (c) early appearance (20 min), peak at 1 h, diminution till 4 h, followed by a plateau, in GM3; (d) appearance at 60 min, maximum around 40 h and slow diminution thereafter, in GD1a, GD1b and GT1b. A detailed study, accomplished at 40 h after injection, demonstrated that almost all radioactivity present in the protein fraction was released by mild acid treatment and recovered in purified sialic acid; most of radioactive glycoprotein-bound sialic acid was releasable by sialidase action. In addition, the radioactivity present in the different gangliosides was exclusively carried by sialic acid and present in both sialidase-resistant and sialidase-labile residues. Only in the case of GD1a was the specific radioactivity of sialidase-resistant sialic acid superior to that of sialidase-releasable sialic acid. The results obtained lead to the following conclusions: (a) radioactive GM3 and GM2 were produced by degradation of GM1 taken up; GM3 originated partly by a process of neosynthesis; (b) radioactive GM1 consisted in part of residual exogenous GM1 and in part of a neosynthetized product; (c) radioactive GD1a originated in part by direct sialylation of GM1 taken up and in part by a neosynthetic process; (d) radioactive GD1b and GT1b resulted only from neosynthesis.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:The sialic acid residue of exogenous GM1 ganglioside is recycled for biosynthesis of sialoglycoconjugates in rat liver. 368 44

Sialidase in human liver was localized predominantly in the lysosomal fraction. Microsomal and nuclear fractions contained some activity but no cytosolic enzyme could be detected. The lysosomal enzyme fraction is active with gangliosides, fetuin, mucus glycoprotein, sialyllactose and other sialyloligosaccharides. The preferred rate of enzymic hydrolysis of sialyl linkages is alpha(2-3) greater than alpha(2-6) greater than alpha(2-8) and this is governed by the Vmax values, as Km values were similar for all substrates tested. N-Acetyl-neuraminic acid is released faster than N-glycoloylneuraminic acid. Using the inhibitors N-acetyl-2-deoxy-2,3-didehydroneuraminic acid and N-(4-nitrophenyl)oxamic acid with selected substrates the existence of at least two types of sialidase activity could be demonstrated. One is active preferentially with gangliosides and sialyllactose and the other with fetuin and sialyhexasaccharides. Strong inhibition by Cu2+ and Hg2+ was found with ganglioside and sialyllactose as substrates. The presence of a sialate O-acetylesterase acting on hematoside containing N-glycoloyl-4-O-acetylneuraminic acid was established.
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PMID:Properties of human liver lysosomal sialidase. 376 40

Crude extracts from Salvia sclarea seeds were known to contain a lectin which specifically agglutinates Tn erythrocytes (Bird, G. W. G., and Wingham, G. (1974) Vox Sang. 26, 163-166). We have purified the lectin to homogeneity by ion-exchange chromatography and affinity chromatography. The agglutinin was found to be a glycoprotein of Mr = 50,000, composed of two identical subunits of Mr = 35,000 linked together by disulfide bonds. The purified lectin agglutinates specifically Tn erythrocytes and, at higher concentrations, also Cad erythrocytes. Native A, B, or O red blood cells are not agglutinated by the lectin and, even after treatment with sialidase or papain, these cells are not recognized. Tn red cells present 1.45 X 10(6) accessible sites to the lectin which binds to these erythrocytes with an association constant of 1.8 X 10(6) M-1. On Cad red cells, 1.73 X 10(6) sites are accessible to the lectin which binds with an association constant of 1.0 X 10(6) M-1. The carbohydrate specificity of the S. sclarea lectin has been determined in detail, using well defined monosaccharide, oligosaccharide, and glycopeptide structures. The lectin was found to be specific for terminal N-acetylgalactosamine (GalNAc) residues. It binds preferentially alpha GalNAc determinants either linked to Ser or Thr (as in Tn structures) or linked in 1-3 to a beta GalNAc or to an unsubstituted beta Gal. Although more weakly, the lectin binds beta GalNAc residues linked in 1-4 to a beta Gal (as in Cad structures). It does not recognize beta GalNAc determinants linked in 1-3 to a Gal (as in globoside) or the alpha GalNAc residues of blood group A structures.
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PMID:Isolation and characterization of an N-acetylgalactosamine specific lectin from Salvia sclarea seeds. 377 23


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