CBP70, a glycosylated nuclear lectin

Rousseau, C.; Felin, Murielle; Doyennette-Moyne, Marie-Agnès; Sève, Annie-Pierre

doi:10.1002/(sici)1097-4644(19970901)66:3<370::aid-jcb9>3.0.co;2-m

Cited by 19 publications

(6 citation statements)

References 48 publications

(54 reference statements)

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“…Indeed, these data are consistent with the hypothesis that PrP can shuttle into the nucleus via a complex with other protein(s) targeted to this cellular compartment [Jaegly et al, 1998]. It was shown that CBP70, which is present in the nucleus and in the cytoplasm [Hadj‐Sahraoui et al, 1996; Rousseau et al, 2000], is a glycoprotein whose glycosylation differs depending on its subcellular localization(s) [Rousseau et al, 1997]. It was suggested that sugar residues might be nuclear‐targeting signals and could define a new nuclear import mechanism [Duverger et al, 1996].…”

Section: Discussionsupporting

confidence: 74%

The cellular prion protein: A new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells*

Rybner

Finel-Szermanski

Felin

et al. 2001

J of Cellular Biochemistry

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Prion diseases are characterized by the presence of an abnormal isoform of the cellular prion protein (PrPc) whose physiological role still remains elusive. To better understand the function of PrPc, it is important to identify the different subcellular localization(s) of the protein and the different partners with which it might be associated. In this context, the PrPc-lectins interactions are investigated because PrPc is a sialoglycoprotein which can react with lectins which are carbohydrate-binding proteins. We have previously characterized a nuclear lectin CBP70 able to recognize N-acetyl-beta-D-glucosamine residues in HL60 cells. Using confocal immunofluorescence, flow-cytofluorometry, and Western-blotting, we have found that PrPc is expressed in the nucleus of the NB4 human promyelocytic leukemia cell line. It was also found that the lectin CBP70 is localized in NB4 cell nuclei. Moreover, several approaches revealed that PrPc and CBP70 are colocalized in the nucleus. Immunoprecipitation experiments showed that these proteins are coprecipitated and interact via a sugar-dependent binding moiety. In conclusion, PrPc and CBP70 are colocalized in the nuclear compartment of NB4 cells and this interaction may be important to better understand the biological function and possibly the conversion process of PrPc into its pathological form (PrPsc).

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Section: Discussionsupporting

confidence: 74%

The cellular prion protein: A new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells*

Rybner

Finel-Szermanski

Felin

et al. 2001

J of Cellular Biochemistry

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“…3C, fractions 3-7). The major component of the eluted fractions changed successively from transferrin (fractions [22][23][24] to fetuin (fractions 23-30) and subsequently to ␣ 1 -acid glycoprotein (fractions 24 -34). The elution order of the glycoproteins was correlated with their apparent sialic acid concentrations: 3.3, 14, and 17 mol/mol for transferrin, fetuin, and ␣ 1 -acid glycoprotein, respectively.…”

Section: Comparison Of Sialic Acid-specific Lectins In the Reactivitymentioning

confidence: 99%

“…On affinity chromatography of sialoglycoproteins on a PVL-Sepharose column, 20 drops of each fraction (0.56 ml) were collected. Fractions are indicated by a bar in B: pass-through fractions (P, fractions 3 and 4), retarded fractions (R, fractions 5-7), and fractions bound to the PVL column and eluted with 10 mM GlcNAc (B, fractions [22][23][24][25][26][27][28][29][30][31][32][33][34]. Arrows X-Z indicate the elution positions of PA-oligosaccharides: X, xylose-PA.…”

Section: Lectin Blotting Studies Of Native P ϩ R- and B-transferrinmentioning

confidence: 99%

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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“…The remarkable specificity towards the non‐reducing terminal GlcNAc residue leads to the expectation that PVL would be a useful reagent for glycoconjugate separation and histochemical detection of specific markers because glycosylation lacking terminal galactosylation or sialylation has been reported in several indicators of pathological states, such as IgGs from rheumatoid arthritis patients [10]and rat hepatoma [11]. In fact, the use of PVL as a GlcNAc detection reagent in diagnostic and biochemical analyses is increasing [12–15].…”

Section: Introductionmentioning

confidence: 99%

Interaction of a lectin from Psathyrella velutina mushroom with N‐acetylneuraminic acid

et al. 1999

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A lectin from the fruiting body of Psathyrella velutina has been used as a specific probe for non-reducing terminal Nacetylglucosamine residues. We reveal in this report that P. velutina lectin recognizes a non-reducing terminal N-acetylneuraminic acid residue in glycoproteins and oligosaccharides. Binding of biotinyl P. velutina lectin to N-acetylneuraminic acid residues was prevented by desialylation of glycoconjugates and was distinguished from the binding to N-acetylglucosamine. Sialooligosaccharides were retarded or bound and eluted with Nacetylglucosamine on a P. velutina lectin column, being differentiated from each other and also from the oligosaccharides with non-reducing terminal N-acetylglucosamine which bound more strongly to the column.z 1999 Federation of European Biochemical Societies.

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CBP70, a glycosylated nuclear lectin

Cited by 19 publications

References 48 publications

The cellular prion protein: A new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells*

The cellular prion protein: A new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells*

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

Interaction of a lectin from Psathyrella velutina mushroom with N‐acetylneuraminic acid

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