The major Kurloff cell glycoproteins: lectin affinities, glycosidase susceptibilities and relationship with the sialylated acid phosphatases of the Kurloff body

Landemore, Gérard; Oulhaj, Nourdine; Letaïef, Slim-Eric; Izard, Juan Francisco Martín

doi:10.1016/0304-4165(92)90107-6

Cited by 13 publications

(9 citation statements)

References 40 publications

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“…Using highly purified KC [29], soluble extracts obtained after dissociative extraction in either 4 M GnHCI or 7 M urea were subjected to ion exchange chromatography and the macromolecules responsible for these histochemical affinities were identified: i) unbound major 30-35 kDa glycoproteins designated as major KC GP [30,35] among which a fraction containing Neu5Ac(oc2,6)-D-Gal/Gal-NAc(~I,4)GIcNAc oligosaccharide sequences were shown to correspond to acid phosphatase subunits [33,42]; and it) protease-resistant chondroitin-4-sulphate proteoglycans eluted at 0.55 M NaCI [31,36] which correspond to PASpositivity and TB-metachromasia of the KB, respectively.…”

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confidence: 99%

Characterization of the non‐sulphated highly anionic kurloff cell glycoconjugates by lectin‐ and immunoblotting: Evidence for the presence of α(2,8)‐linked polysialic acid‐bearing molecules

Letaïef

Landemore

Oulhaj

et al. 1993

Biology of the Cell

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Urea or guanidine hydrochloride-soluble extracts from highly purified Kurloff cells (KC) radiolabelled in vitro were subjected to DEAE-cellulose chromatography. Among the three anionic peaks obtained, a major and non-sulphated peak (designated as peak IV) strongly affected by glucosamine-labelling and eluted at about 0.3 M NaCl was analyzed. Gel filtration on Sepharose CL4B and 10% SDS-PAGE indicated its heterogeneous size. Peak IV consisted mainly of N-glycans as shown by its susceptibility to tunicamycin. Further insight into its chemical nature was obtained by examining its binding capacity to different lectins and by immunodot analysis. It strongly interacted with concanavalin A (Con A) after dot-blot or Western blotting. A large amount of these glycoproteins is not of the high-mannose type since Galanthus nivalis agglutinin reacted weakly with peak IV. Moreover, bindings to Phaseolus vulgaris and to wheat germ agglutinins suggest the presence of bisecting N-acetylglucosamine residues. Bindings to Sambucus nigra and to Ricinus communis agglutinins, dramatically lessened and increased respectively after desialylation, suggest the presence of Neu5Ac alpha 2,6Gal/GalNAc sequences. The absence of outer sialic acid residues linked alpha 2,3 to galactose was demonstrated following Maackia amurensis agglutinin negativity. The use of poly(alpha 2,8-sialyl) endo-N-acylneuraminidase combined with immunodot procedure with a monoclonal antibody that specifically recognizes alpha 2,8-linked polysialic chains revealed that peak IV contains oligosaccharidic epitopes common to polysialylated neural cell adhesion molecules.

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confidence: 99%

Characterization of the non‐sulphated highly anionic kurloff cell glycoconjugates by lectin‐ and immunoblotting: Evidence for the presence of α(2,8)‐linked polysialic acid‐bearing molecules

Letaïef

Landemore

Oulhaj

et al. 1993

Biology of the Cell

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“…The sialidase-resistance of CB-reactive structures in Kurloff cells and particularly in the Kurloff body suggests that, although in close relationship, the CBpositive structures of the Kurloff body are distinct from the following glycoproteins described previously: (i) sialylated SNA-reactive glycoproteins and particularly 0r sialoacid phosphatases localized histochemically in the Kurloff body (Landemore et al, 1992; and (ii) highly anionic but non-sulphated Kurloff cell N-glycosylproteins containing ~2,8-1inked polysialic acid (Leta'fef, 1988;Leta'/ef et al, 1993). The specificity of CB in critical electrolyte concentration procedures for polysulphated proteoglycans has been thoroughly documented previously (Scott, 1980;Iozzo, 1984).…”

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confidence: 74%

The proteoglycan skeleton of the Kurloff body as evidenced by Cuprolinic Blue staining

et al. 1994

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This study deals with the ultrastructure of the chondroitin sulphate proteoglycans of the Kurloff body, a large lysosome organelle, metachromatic towards Toluidine Blue, of a blood cell unique to the guinea pig and called the Kurloff cell. Splenic Kurloff cell from oestrogen-treated guinea pig cells were examined after staining with Cuprolinic Blue, a cationic phthalocyanine-like dye, in the presence of MgCl2 in a critical electrolyte concentration method. Better results were obtained when the fixation-staining by the glutaraldehyde Cuprinolinic Blue MgCl2 mixture was preceded by a glutaraldehyde pre-fixation. On light microscopy, Kurloff bodies generally exhibited an overall pink and glassy metachromasia, sometimes with additional darker metachromatic small dots at their peripheries. At the ultrastructural level, the metachromatic central matrix of the Kurloff body usually exhibited, as a major feature, a typical network pattern of ribbon-like or stellate electron-dense precipitates suggesting the presence of a skeleton of Cuprolinic Blue-reactive filamentous structures. Taking into account their high anionicity (as shown by the stability of the dye binding in the presence of 0.3 M MgCl2) and their susceptibility to chondroitinase ABC, these anionic structures were assumed to be related to the proteochondroitin-4-sulphate previously characterized as the only major sulphated glycoconjugate of the Kurloff cell.

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“…MAA and SNA lectins are considered as highly specific in their recognition of sialic acid. SNA was isolated by Broekaert et al (1984) and its binding exhibit the presence of Neu5Ac~2-6Gal/GalNAc sequences (Landemore et al 1992). MAA isolated by Wang and Cummings (1988) has a definitive carbohydrate requirement of the trisaccharide sequence Neu5Accz2-3GalJ31-4GlcNAc/Glc.…”

Section: Discussionmentioning

confidence: 99%

Glycosylation pattern and enzyme activities in atrophic, angulated skeletal muscle fibres from ageing rats

Kirkeby

1994

Vichows Archiv A Pathol Anat

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In this study enzyme activities and lectin binding patterns in skeletal muscle from very old rats were investigated in order to evaluate changes in enzyme activity or carbohydrate expression in senile muscle. Activities for adenosine triphosphatase (ATPase), succinic dehydrogenase, non-specific esterase and the binding pattern for 31 lectins were investigated in the soleus muscles from very old (36 months) and young (3 months) rats. In ageing muscles atrophic, angulated muscle fibres are frequent. In cryostat sections these fibres were mostly but not always type II defined by the myosin ATPase reaction; few showed a strong esterase activity. Some showed strong activity for succinic dehydrogenase while others were weakly reacting. A number of lectins strongly bound to the sarcoplasm in angulated fibres while the binding to normal fibres in both old and young rat muscle was much weaker or even absent. Preferential binding to the ageing, angulated fibres was seen with Aleuria aurentia, Galantus nivalis, Caragana abborecens, Triticum vulgaris, Maackia amurensis, Sambucus nigra, Phaseolus vulgaris erythroagglutinin, and Phaseolus coccineus. Samples of homogenized and centrifuged muscles were run by electrophoresis and the gels blotted to nitrocellulose paper. Subsequent lectin staining of the blots detected that two glycoproteins with molecular weights around 25,000 and 21,000 daltons were present in old muscle, but not in young. Aberrant or elevated expression of sarcoplasmic glycoconjugates is involved in ageing muscle atrophy.

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The major Kurloff cell glycoproteins: lectin affinities, glycosidase susceptibilities and relationship with the sialylated acid phosphatases of the Kurloff body

Cited by 13 publications

References 40 publications

Characterization of the non‐sulphated highly anionic kurloff cell glycoconjugates by lectin‐ and immunoblotting: Evidence for the presence of α(2,8)‐linked polysialic acid‐bearing molecules

Characterization of the non‐sulphated highly anionic kurloff cell glycoconjugates by lectin‐ and immunoblotting: Evidence for the presence of α(2,8)‐linked polysialic acid‐bearing molecules

The proteoglycan skeleton of the Kurloff body as evidenced by Cuprolinic Blue staining

Glycosylation pattern and enzyme activities in atrophic, angulated skeletal muscle fibres from ageing rats

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