Structural Study on the Carbohydrate Moiety of Human Placental Alkaline Phosphatase12

Endo, Tamao; Ohbayashi, Hirokazu; Hayashi, Yasumasa; Ikehara, Yukio; Kochibe, Naohisa; Kobata, Akira

doi:10.1093/oxfordjournals.jbchem.a122228

Cited by 62 publications

(42 citation statements)

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“…Both fucosylated and nonfucosylated trimannosyl cores were found in the sugar chains. The structure of these sugar chains was thus quite different from that of human PLAP that contained biantennary complex-type oligosaccharides only [546]. Since the two enzymes show almost 90 % sequence identity, this provides further evidence for cell-specific patterns of AP glycosylation.…”

Section: Glycosylationmentioning

confidence: 83%

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Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

872

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: Glycosylationmentioning

confidence: 83%

“…The structure of the N-linked glycan has been determined for human PLAP [546]. It was concluded that an enzyme monomer contains a single N-linked sugar chain.…”

Section: Glycosylationmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

872

922

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“…DISCUSSION Kochibe and Matta (13) originally observed that PVL primarily recognizes GlcNAc residues and agglutinates human erythrocytes, although ambiguity about the nature of the glycan receptor on erythrocytes remained. The subsequent conclusion that the carbohydrate-binding specificity of PVL was the nonreducing terminal ␤-GlcNAc residue, but not GalNAc or NeuAc, was based on the behavior of various complex-type and human milk oligosaccharides on a PVL column (14). When we used PVL to characterize plasma glycoproteins, however, a number of glycoproteins in normal plasma reacted positively with PVL on the membrane, which re-opened the question about the reported specificity.…”

Section: Pa-trisialooligosaccharide Structures Of Native P- R- Andmentioning

confidence: 99%

“…In contrast to other GlcNAc-specific lectins from higher plants that recognize ␤1,4-linked GlcNAc preferentially in the oligosaccharide sequence (16), PVL exhibits a strong preference for the GlcNAc monomer over the chitooligosaccharides and binds nonreducing terminal GlcNAc of other linkages better than that of the ␤1,4-linkage (13,14). Because glycosylation with exposed GlcNAc residues lacking terminal galactosylation, or sialylation, has been reported for several pathological markers, such as IgGs from rheumatoid arthritis patients (17) and rat hepatoma (18), the remarkable specificity toward nonreducing terminal GlcNAc prompted PVL use as a GlcNAc-detection reagent in diagnostic analyses (19 -22).…”

mentioning

confidence: 94%

“…A lectin from the fruiting body of Psathyrella velutina (PVL) has been known as a GlcNAc-specific lectin (13)(14)(15). In contrast to other GlcNAc-specific lectins from higher plants that recognize ␤1,4-linked GlcNAc preferentially in the oligosaccharide sequence (16), PVL exhibits a strong preference for the GlcNAc monomer over the chitooligosaccharides and binds nonreducing terminal GlcNAc of other linkages better than that of the ␤1,4-linkage (13,14).…”

mentioning

confidence: 99%

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Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Ueda¹,

Matsumoto²,

Takahashi³

et al. 2002

Journal of Biological Chemistry

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A lectin from the fruiting body of the Psathyrella velutina mushroom (PVL) was found to bind specifically to N-acetylneuraminic acid, as well as to GlcNAc (Ueda, H., Kojima, K., Saitoh, T., and Ogawa, H. (1999) FEBS Lett. 448, 75-80). In this study, the glycan sequences that PVL recognizes with high affinity on sialoglycoproteins were revealed. Among sialic acid-specific lectins only PVL could reveal the sialylated N-acetyllactosamine structure of glycoproteins in blotting studies, based on the dual specificity. The affinity of PVL to fetuin was measured by surface plasmon resonance to be 10 7 M ؊1 , which is an order of magnitude higher than those of Sambucus nigra agglutinin and Maackia amurensis mitogen, whereas affinity to asialofetuin was ϳ0 and to asialoagalactofetuin was 10 8 M ؊1 , suggesting that PVL exhibits remarkably high affinities toward glycoproteins possessing trisialo-or GlcNAc-exposed glycans. Transferrin was separated into fractions that correspond to the sialylation states on an immobilized PVL column. Transferrin-possessing trisialoglycans containing ␣2,3-linked N-acetylneuraminic acid on the ␤1,4-linked GlcNAc branch bound to the PVL column and eluted with GlcNAc; those containing only ␣2,6-linked sialic acids were retarded, whereas other transferrin fractions passed through the column. These results indicate that PVL is a lectin with potential for separation and detection of sialoglycoproteins because of its dual specificity toward sialoglycans and GlcNAc exposed glycans.Sialic acids play an important role as ligands in cell sociology. Sialylation of glycoproteins changes under pathological conditions as well as during developmental stages, and altered sialylation often has significant implications in the physiological role of glycoproteins (1-3). Lectins that recognize the linkages or modifications of sialic acid are therefore indispensable as reagents in biochemical research and diagnostic analyses.Among sialic acid-specific lectins purified from plants and other sources, several lectins have been employed as tools for the detection and separation of sialic acid-containing glycoconjugates (3, 4). Lectins that distinguish various linkages of sialic acid are elderberry bark lectin (SNA 1 ; Sambucus nigra agglutinin) (5), Japanese elderberry lectin (SSA; S. sieboldiana agglutinin) (6), and Polyporus squamosus lectin (7) that are specific for NeuAc␣2,6Gal/GalNAc sequences; Maackia amurensis mitogen (MAL) that reacts with greatest affinity to the trisaccharide sequence NeuAc/Gc␣2,3Gal␤1,4GlcNAc/Glc, which is usually present in N-linked oligosaccharides (8), and the hemagglutinin from the same source (MAH) that displays higher affinity for a disialylated tetrasaccharide found in the O-linked oligosaccharide, NeuAc␣2,3Gal␤1,3(NeuAc␣2,6)GalNAc␣ (9). In contrast to these sequence-specific lectins, wheat germ lectin (WGA) and Limax flavus lectin have been used as general tools to bind sialylated glycoconjugates (10, 11). A mushroom lectin from Hericum erinaceum recognizes N-glycolylneuraminic acid...

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Effects of retinoic acid onN-glycosylation and mRNA stability of the liver/bone/kidney alkaline phosphatase in neuronal cells

et al. 2000

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Alkaline phosphatase (ALP) is a glycoenzyme that is highly expressed during carcinogenesis and is induced by retinoic acid (RA) in various cells. We investigated the effects of RA on N-linked glycosylation of the tissue nonspecific liver/bone/kidney- type of ALP (L/B/K ALP), on ALP transcripts, and on total protein glycosylation in two neuronal cell lines, P19 and NG108CC15, and in primary cultures of neonatal rat brain. ALP activity was determined in cell extracts and found to be induced by RA. Tunicamycin was used at various concentrations to inhibit protein N-glycosylation. After treatment of cells with low concentrations (0.1 and 0.125 microgram/ml) of tunicamycin for 48 h, uninduced and RA-induced ALP activity declined while incubation with a protease inhibitor restored activity, indicating that the L/B/K ALP bear N-linked oligosaccharide chains important for maintaining enzymatic activity. Interestingly, ALP activity in RA-treated cultures was less inhibited by tunicamycin compared to untreated controls suggesting that RA may have an impact on ALP N-glycosylation. To investigate effects of RA on ALP glycosylation further, incorporation of [(14)C]mannose and [(35)S]methionine into ALP protein was determined in the presence or absence of RA. The ratio of mannosylation and biosynthesis demonstrate that incubation of cells with RA increased [(14)C]mannose incorporation into ALP molecules. Also, the release of free [(14)C]mannose from ALP molecules relative to the amount of protein by N-Glycanase was increased in RA-treated cultures. In addition, mannosylation of total protein was found to be induced in cells after exposure to RA. Analysis of biosynthesized ALP monomers revealed that RA increased glycosylation of the polypeptides. Furthermore, tunicamycin decreased the stability of ALP mRNA, an effect that was reduced by cotreatment with RA. Thus, the degree of N-glycosylation of the L/B/K ALP as well as mRNA and protein levels of this enzyme are affected by RA. The P19 cell line provides a useful model system to study the molecular mechanism(s) underlying the action of RA on glycosylation during neuronal differentiation further.

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Structural Study on the Carbohydrate Moiety of Human Placental Alkaline Phosphatase12

Cited by 62 publications

References 0 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Effects of retinoic acid onN-glycosylation and mRNA stability of the liver/bone/kidney alkaline phosphatase in neuronal cells

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