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)

Conventional and scanning electron microscopy of calcigerous renal calculi discloses typical concentric laminations, radial striations and microspherules. Random axial distribution of oxalate crystals and their coating by electron-dense matrix fibers with a definite parallel orientation and cross-linkages are evident. The biochemical relationship of uromucoid to matrix substance A is described. It is suggested that renal sialidase may convert the urinary uromucoid to matrix substance A, whose apatite-covered fibers may be responsible for epitaxial nucleation of some crystal systems. Our studies indicate that the intimate apatite-matrix relationship occurs in the human nephron, probably as an intracellular phenomenon. Subsequent extrusion of these mineralized complexes into the lumen of the nephron (intranephronic calculosis) may, in some instances, represent the initial microanatomic stage of renal calculogenesis.
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PMID:Observations on the ultrastructure and genesis of urinary calculi. 83 98

Although many risk factors and theories exist in the literature for urinary stone formation, a hypothesis is suggested for the pathogenesis of renal stones. According to the matrix theory, a protein such as uromucoid activates the initial crystallisation process by promoting the formation of calcium oxalate and calcium phosphate crystals as well as clumping in whole urine. We put forward a theory whereby one of the most important factors in the matrix theory would be the composition and concentration of the protein. In support of this hypothesis, emphasis is placed on the activities of urokinase and sialidase.
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PMID:Pathogenesis of kidney stones. 180 56

Many hypotheses have been proposed for renal stone formation. It has been argued that with infection-induced renal stones the hydrolysis of urea by bacterial urease increases urinary pH, with consequent stone formation. Unfortunately, this theory is not applicable to the micro-organisms that do not produce urease (e.g. Escherichia coli). It has been recently reported that E. coli reduces the urinary urokinase activity of male rats, but does not influence the urinary sialidase activity. This study has now been expanded to the urease-producing bacteria Proteus mirabilis, Staphylococcus aureus, S. epidermidis, Pseudomonas aeruginosa and Micrococcus luteus. Subcutaneous injections with these bacteria were found to significantly (P < 0.003) reduce the UK activity of extrarenally obstructed kidneys. The urease-producing mammalian skin bacterium, M. luteus, was, however, the exception (P = 0.1079). In contrast to S. epidermidis, P. aeruginosa and M. luteus (P < 0.0213), P. mirabilis and S. aureus had no effect on renal sialidase activity (P < 0.4047). These results may explain why Proteus species are predominant in infection-induced renal stones. According to the urokinase-sialidase hypothesis, a decrease in urinary urokinase activity should increase the uromucoid levels, whilst no effect on the urinary sialidase activity should favour conversion of urinary uromucoid to mineralizable matrix. These conditions may lead to renal stone formation. An increase in urinary pH resulting from urease-producing micro-organisms will increase salt precipitation on the uromucoid. It is thus concluded that urease-producing bacteria may play a double role in renal stone formation.
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PMID:In vivo effects of urease-producing bacteria involved with the pathogenesis of infection-induced urolithiasis on renal urokinase and sialidase activity. 883 91

The primary structures of 32 sulfated di-, tri- and tetraantennary N-glycans of human Tamm-Horsfall glycoprotein (THP) have been determined. THP was isolated from the urine of one healthy male donor. The intact carbohydrate chains were released by PNGase-F and fractionated via FPLC on Resource Q, HPLC on LiChrosorb-NH2, and high-pH anion-exchange chromatography on CarboPac PA-1. Characterizations were performed using 500-MHz and 600-MHz 1H-NMR spectroscopy, in combination with sialidase treatments. The type of characterized N-glycans ranged from monosulfated to trisulfated N-glycans, whereby the sulfate groups were present as 3-O-sulfated Gal (Gal3S) and 4-O-sulfated GalNAc (GalNAc4S). A compilation of the established structures is shown below. [structure in text]
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PMID:Sulfated di-, tri- and tetraantennary N-glycans in human Tamm-Horsfall glycoprotein. 976 Jan 89

Tamm-Horsfall glycoprotein (THGP) and the oligosaccharide fraction liberated from THGP by hydrazinolysis inhibited tetanus toxoid-induced T cell proliferation. Intact THGP showed approximately 100-fold more inhibitory activity than the free oligosaccharides. After fractionating the oligosaccharides by anion-exchange column chromatography, the inhibitory activity could be detected in a sialidase-resistant acidic oligosaccharide fraction (fraction AR). The inhibitory activity of fraction AR was not observed when the fraction was added to the T cell culture medium 24 h after the addition of tetanus toxoid. Increased concentration of interleukin (IL) 1beta and decreased concentration of IL-2 were observed in the T cell culture medium after the addition of fraction AR. The oligosaccharides in fraction AR also inhibited the growth of an IL-1-dependent cell line, D10-G4. These results strongly suggested that the oligosaccharides in fraction AR bind to IL-1beta and suppress its cytokine activity. IL-1beta actually bound to the fraction AR immobilized on an amino-bonded thin layer plate. Fractionation of the oligosaccharides indicated that only oligosaccharides containing an N-acetylgalactosamine residue and a sulfate residue bound specifically to IL-1beta. Removal of either the sulfate residue or the N-acetylgalactosamine residue from the oligosaccharides abolished both the proliferation-inhibition and IL-1beta binding activities. Since IL-1beta did not bind to thyroid-stimulating hormone, which has the sulfate group at C-4 of the N-acetylgalactosamine residue in its N-linked sugar chains, the binding of IL-1beta toward oligosaccharides in fraction AR was considered to be highly specific.
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PMID:Detection of novel carbohydrate binding activity of interleukin-1. 993 50

Glycosylphosphatidylinositol (GPI)-anchored proteins are ubiquitous in eukaryotes. The minimum conserved GPI core structure of all GPI-anchored glycans has been determined as EtN-PO4-6Manalpha1-2Manalpha1-6Manalpha1-4GlcN-myo-inositol-PO3H. Human placental alkaline phosphatase (AP) has been reported to be a GPI-anchored membrane protein. AP carries one N-glycan, (NeuAcalpha2-->3)2Gal2GlcNAc2Man3GlcNAc(+/-Fuc)GlcNAc, and a GPI anchor, which contains an ethanolamine phosphate diester group, as a side chain. However, we found that both sialidase-treated soluble AP (sAP) and its GPI-anchored glycan bound to a Psathyrella velutina lectin (PVL)-Sepharose column, which binds beta-GlcNAc residues. PVL binding of asialo-sAP and its GPI-anchored glycan was diminished by digestion with diplococcal beta-N-acetylhexosaminidase or by mild acid treatment. After sequential digestion of asialo-sAP with beta-N-acetylhexosaminidase and acid phosphatase, the elution patterns on chromatofocusing gels were changed in accordance with the negative charges of phosphate residues. Trypsin-digested sAP was analyzed by liquid chromatography/electrospray ionization mass spectrometry, and the structures of two glycopeptides with GPI-anchored glycans were confirmed as peptide-EtN-PO4-6Manalpha1-->2(GlcNAcbeta1-PO4-->6)Manalpha1-6(+/-EtN-PO4-->)Manalpha1-->4GlcN, which may be produced by endo-alpha-glucosaminidase. In addition to AP, GPI-anchored carcinoembryonic antigen, cholinesterase, and Tamm-Horsfall glycoprotein also bound to a PVL-Sepharose column, suggesting that the beta-N-acetylglucosaminyl phosphate diester residue is widely distributed in human GPI-anchored glycans. Furthermore, we found that the beta-N-acetylglucosaminyl phosphate diester residue is important for GPI anchor recognition of aerolysin, a channel-forming toxin derived from Aeromonas hydrophila.
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PMID:A beta-N-acetylglucosaminyl phosphate diester residue is attached to the glycosylphosphatidylinositol anchor of human placental alkaline phosphatase: a target of the channel-forming toxin aerolysin. 1285 98