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)

The inhibitory effect of various compounds on the activities of four types of rat sialidase was investigated. 2-Deoxy-2,3-dehydro-N-acetylneuraminic acid and N-acetylneuraminic acid were competitive inhibitors for the sialidases. The former was effective against cytosolic sialidase and intralysosomal sialidase more than two membrane-associated sialidases I and II, the latter being a much weaker inhibitor. A heavy metal ion such as Cu2+ (1 mM) and thiol-modifying 4-hydroxymercuribenzoate (50 microM) caused complete inhibition of the activities of cytosolic sialidase and membrane sialidase I, while no decrease in the activities of intralysosomal sialidase and membrane sialidase II was observed. When 4-nitrophenyloxamic acid and siastatin B, inhibitors of bacterial sialidases, and synthetic thioglycoside GM3 analogue Neu5Ac alpha-s-(2-6)Gal beta(1-4)Glc beta(1-1) ceramide, an inhibitor of influenza virus sialidase, were tested, they did not affect any activity of the rat sialidases. By the differential effect of these inhibitors, the four types of rat sialidase could be discriminated from one another and furthermore from viral and bacterial sialidases.
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PMID:Differential effect of various inhibitors on four types of rat sialidase. 835 26

The Kurloff cell (KC), a natural killer lymphocyte, contains a large (10-microns diameter) periodic acid-Schiff (PAS)-positive lysosome-like inclusion body called the Kurloff body (KB), which exhibits strong acid phosphatase activity. The presence of Sambucus nigra agglutinin (SNA)-reactive Neu5Ac(alpha 2,6)-D-Gal/Gal-NAc(beta 1,4)GlcNAc oligosaccharide sequences and the absence of the corresponding Neu5Ac(alpha 2,3) Maackia amurensis agglutinin (MAA)-reactive sequence in the major 35-kDa N-glycosylproteins of the complex or hybrid type extracted from purified KC were established by Western-lectin-blotting of cytosolic extracts from purified KC. Moreover, these SNA-reactive sequences, or at least part of them, were shown to be borne by sialidase-sensitive KC acid isophosphatases. Thymic sections rich in KC, from estrogenized guinea pigs were examined by affino-histochemistry with these sialic acid-reactive lectins. The SNA-reactivity of thymic sections was quasi-exclusively confined to KC clusters, whereas the whole thymic section was negative for MAA. KC were not SNA-reactive following preincubation and incubation with 200 mM lactose. When submitted to enzymatic or mild chemical desialylation processes, the SNA-reactivity of the KC clusters was enhanced. The SNA-reactivity of KC clusters was completely abolished following prolonged chemical desialylation, whereas the PAS-positivity of KB remained unchanged. Even after a prolonged sialidase treatment, this SNA-reactivity was only reduced. Moreover, after both these desialylation processes, KC developed a heavier Ricinus communis agglutinin-reactivity, thus confirming the presence of penultimate Gal residues in their abundant SNA-reactive oligosaccharide sequences Neu5Ac(alpha 2,6)Gal(beta 1,4)GlcNAc. Such a selective lectin histochemical property provides a marker for detecting KC.
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PMID:Glycoconjugates with Neu5Ac(alpha 2,6)Gal(beta 1,4)GlcNAc sequences: a selective lectin-histochemical property of Kurloff cells in guinea pig thymus. 844 37

Addition of sialic acid residues in the human pathogen Trypanosoma cruzi glycoconjugates is mediated by a trans-sialidase and not by a CMP-sialic acid:glycoconjugate sialyltransferase. Incubation of trans-sialidase with N-[galactose-14C]acetyllactosamine and O-linked oligosaccharides, N-linked glycopeptides (both obtained from fetuin) or sialyllactose showed that the last three compounds were donors of sialic acid residues to the first one. Moreover, N- and O-linked oligosaccharides in asialofetuin and asialomucin, respectively, served as acceptors of sialic acid units. Gangliosides GM3, GD1a and GT1b but not GM2, GM1a nor GD1b donated sialic acid units to N-acetyllactos amine when incubated with trans-sialidase. This showed that only sialic acid units bound to terminal galactosyl residues were transferred. GM1a was converted to GD1a, and GD1b to GT1b when incubated with the appropriate donor. The fact that asialo-GM1a was converted to a ganglioside migrating as GD1a on thin-layer chromatography suggested that sialic acid units may be transferred to internal galactosyl residues, although once linked to those residues they can not be further transferred to other glycoconjugates. Sialic acid residues linked alpha 2,3- but not alpha 2,6- or alpha 2,8- were transferred by the trans-sialidase. Methyl beta-galactoside but not methyl alpha-galactoside served as acceptor of sialic acid units, thus suggesting that terminal alpha-linked galactosyl units in T. cruzi and mammalian glycoproteins are not sialylated by the enzyme. As the trans-sialidase employed in these experiments has been shown to be located on the external surface of the parasite and to be shed to the medium, the relatively broad specificity shown by the enzyme with respect to protein- and lipid-linked oligosaccharides strongly suggests that infection by T. cruzi might alter the sialic acid distribution in glycoproteins and glycolipids of the mammalian host.
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PMID:The action of Trypanosoma cruzi trans-sialidase on glycolipids and glycoproteins. 847 49

Sialyl-linkage specificity of the sialidase of influenza B viruses isolated in different years from 1940 through 1990 (B/Lee/40,B/Setagaya/3/56,B/Tokyo/7/66,B/Kagoshima/1/68, B/Gifu/2/73, B/Kanagawa/3/76, B/Ibaraki/2/85, B/Yamagata/16/88, and B/Bangkok/163/90) was studied with N-acetylneuraminyl (alpha 2-3)- and (alpha 2-6)-lactoses, GM3 gangliosides containing the same sialyl-oligosaccharide sequences as sialyllactose, and also with type I and type II lacto-series gangliosides carrying Neu5Ac alpha 2-3Gal and NeuAc alpha 2-6Gal linkages as substrates. From an examination of up to nine strains, the sialidases of all viruses preferentially hydrolyze substrates with Neu5Ac alpha 2-3Gal linkage rather than the Neu5Ac alpha 2-6Gal linkage. It was found that the sialidase activity toward Neu5Ac alpha 2-6Gal linkage relative to Neu5Ac alpha 2-3Gal linkage is increased in later strains, whether sialyllactose or ganglioside is used as the substrate. These results suggested that the sialidase of influenza B virus isolates has shown a drift in linkage specificity which correlates with the year of isolation.
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PMID:Drift of the sialyl-linkage specific recognition of the sialidase of influenza B virus isolates. 848 3

The submandibular and buccal glands of the Giant Ant-eater (Myrmecophaga tridactyla) have been studied by means of a series of carbohydrate histochemical methods, including a broad spectrum of PO-lectin procedures. The seromucous cells (Gl. submandibularis) and mucous cells (Gl. buccalis) of the glandular acini, as well as the secretion in the excretory duct system exhibited very strong to strong reactions for neutral and acidic glycoconjugates. The serous cells of the buccal glands and the excretory duct cells reacted rather weakly. The different controls applied particularly emphasized that sialoglycoconjugates are the predominant ingredients of the saliva secreted. Lectin histochemical differentiation demonstrated a varying pattern of saccharide residues in these substances. In the submandibular glands the glycoconjugates (mostly proteoglycans) of the seromucous cells and the luminal secretion normally contained terminal beta-galactose and minor contents of terminal alpha-N-acetylglucosamine. After sialidase digestion this cell type exhibited distinct amounts of sialic acid-beta-galactose and sialic acid-alpha-N-acetylgalactosamine. Sialic acid was also clearly present in the tough interlobular connective tissue. The buccal glands showed a similar distribution of saccharide residues in the mucous cells. In the serous cells, however, acidic glycoproteins with sialyl residues were observed, also containing terminal alpha-D-mannosyl, alpha-N-acetylgalactosaminyl, and beta-D-galactosyl residues. The cells of the excretory duct system of both gland types reacted weakly to moderately for terminal sugar residues (N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, beta-D-galactose). The results obtained are discussed in view of the specific feeding mode of the Giant Ant-eater, whereby high contents of sialoglycoconjugates (proteoglycans, glycoproteins) produced by the salivary glands warrant for the main function of the non-sticky saliva; i.e., to act as an effective lubricant during tongue movement.
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PMID:Lectin histochemistry of salivary glands in the giant ant-eater (Myrmecophaga tridactyla). 849 Feb 58

A ganglioside preparation containing two structurally related minor gangliosides (Gg 1 + 2) was isolated from bovine brain ganglioside mixture and characterized. Treatment of 50 g ganglioside mixture with Clostridium perfrigens sialidase, followed by chromatography on DEAE-Sepharose and silica gel columns, yielded 20 mg Gg 1 + 2. By chemical analyses, 1H- and 13C-NMR spectroscopy, enzymic hydrolyses using human beta-hexosaminidase A and clostridial sialidase, and TLC overlay with the conjugated cholera toxin B subunit, the two novel gangliosides Gg 1 and Gg 2 were identified to be: Gg 1, GalNAc-GD1a(Neu5Ac/Neu5Gc), beta-GalNAc-(1-4)-[alpha-Neu5Ac-(2-3)]-beta- Gal-(1-3)-beta-GalNAc-(1-4)-[alpha-Neu5Gc-(2-3)]-beta-Gal-(1-4)-be ta- Glc-(1-1)-Cer; Gg 2, GalNAc-GD1a(Neu5Gc/Neu5Ac), beta-GalNAc-(1-4)-[alpha-Neu5Gc-(2-3)]- beta-Gal-(1-3)-beta-GalNAc-(1-4)-[alpha-Neu5Ac-(2-3)]-beta-Gal-(1- 4)-beta- Glc-(1-1)-Cer. These two gangliosides contain the identical pentasaccharide backbone except that the substitution of the two sialic acids, Neu5Ac and Neu5Gc, are in the reversed position of the external and the internal Gal residues. Our analyses showed that the content of Gg 1 and Gg 2 were approximately 0.12% and 0.08%, respectively, of the total brain ganglioside mixture.
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PMID:Isolation and structural characterization of N-acetyl- and N-glycolylneuraminic-acid-containing GalNAc-GD1a isomers, IV4GalNAcIV3Neu5AcII3Neu5GcGgOse4Cer and IV4GalNAcIV3Neu5GcII3Neu5AcGgOse4Cer, from bovine brain. 857 36

The 9-amino or 9-N-acyl-5-trifluoroacetyl methyl alpha-ketosides (1a-c) and their 2,3-didehydro analogs (2a-c) have been synthesized through Neu5Ac aldolase-catalyzed aldol reaction of 6-azido-2-benzyloxycarbonylamino-2-deoxy-D-mannose with sodium pyruvate. The six compounds were investigated as inhibitors of sialidase from influenza virus. Compound 2b, a 2,3-didehydro type, showed the most potent inhibitory activity (IC50 > 7.8 microM) against the enzyme, whereas, compounds 1a-c as the methyl alpha-glycosides were found to be practically inactive (IC50 > 100 microM).
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PMID:Chemoenzymatic synthesis of neuraminic acid analogs structurally varied at C-5 and C-9 as potential inhibitors of the sialidase from influenza virus. 858 91

Recently, we reported the discovery of a new type of sialidase, KDNase, which specifically hydrolyzes the ketosidic linkages of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), but not N-acylneuraminyl linkages. We now report that this enzyme, designated KDNase SM, is an inducible enzyme that is localized in the periplasm of Sphingobacterium multivorum. Growth of S. multivorum in the presence of KDN-containing oligosaccharide alditols, KDNalpha2-->3Galbeta1-->3GalNAc alpha1-->3[KDNalpha2--> (8KDN alpha2-->)n-->6]GalNAcol, as a sole carbon source induced KDNase SM activity 15 40-fold, compared with growth in the absence of inducer. KDN, Neu5Ac, or Neu5Ac oligomers were ineffective as inducers. The enzyme was released from the periplasm of induced cells by cold osmotic shock and purified 700-fold to homogeneity. The specific activity of the pure enzyme was 82,100 units/mg of protein. KDNase SM activity resided in a single polypeptide chain with an estimated molecular weight of approximately 47,500. Enzyme activity was maximal at near neutral pH. The availability of pure KDNase will now make it possible to study the structure and functional role of KDN-glycoconjugates and to determine the molecular mechanism whereby the enzyme can discriminate between KDN and N-acylneuraminic acid.
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PMID:Induction, localization, and purification of a novel sialidase, deaminoneuraminidase (KDNase), from Sphingobacterium multivorum. 862 79

Sialic acid on the red cell surface plays a major role in invasion by the malaria parasite Plasmodium falciparum. The NeuAc(alpha 2,3) Gal motif on the O-linked tetrasaccharides of the red cell glycophorins is a recognition site for the parasite erythrocyte-binding antigen (EBA-175). Consequently, the interaction of P. falciparum and the red cell might share homology with that of the influenza virus. The cellular interactions of P. falciparum were examined for their sensitivity to 4-guanidino-2,3-didehydro-D-N-acetyl neuraminic acid (4-guanidino Neu5Ac2en), a potent inhibitor of influenza virus sialidase. Parasite invasion and subsequent development was unaffected by the sialidase inhibitor. The inhibitor did not affect rosette formation of parasite-infected erythrocytes with uninfected cells nor their cytoadherence to C32 melanoma cells. Furthermore, we were unable to confirm the presence of a previously reported parasite sialidase using sensitive fluorometric or haemagglutination assays, neither was any malarial trans-sialidase identified. We conclude that P. falciparum possesses neither sialidase nor trans-sialidase activity and that an inhibitor of influenza virus sialidase has no effect on important cellular interactions of this parasite.
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PMID:Plasmodium falciparum lacks sialidase and trans-sialidase activity. 867 33

Homopolymers of alpha 2,8-linked N-acetylneuraminic acid [poly(alpha 2,8-Neu5Ac)] of the neural cell adhesion molecule NCAM have been shown to be temporally expressed during lung development and represent a marker for small cell lung carcinoma. We report the presence of a further polysialic acid in lung that consists of oligo/polymers of alpha 2,8-linked deaminoneuraminic acid residues [poly (alpha 2,8-KDN)], as detected with a monoclonal antibody in conjunction with a specific sialidase. Although the various cell types forming the bronchi, alveolar septs, and blood vessels were positive for poly (alpha 2,8-KDN) by immunohistochemistry, this polysialic acid was found on a single 150-kDa glycoprotein by immunoblot analysis. The poly(alpha 2,8-KDN)-bearing glycoprotein was not related to an NCAM protein based on immunochemical criteria. The expression of the poly (alpha 2,8-KDN) was developmentally regulated as evidenced by its gradual disappearance in the rat lung parenchyma commencing 1 week after birth. In adult lung the blood vessel endothelia and the smooth muscle fibers of both blood vessels and bronchi were positive but not the bronchial and alveolar epithelium. The poly (alpha 2,8-KDN)-bearing 150-kDa glycoprotein became reexpressed in various histological types of lung carcinomas and cell lines derived from them and represents a new oncodevelopmental antigen in lung.
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PMID:Poly (alpha 2,8-deaminoneuraminic acid) is expressed in lung on a single 150-kDa glycoprotein and is an oncodevelopmental antigen. 879 42


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