Wyniki wyszukiwania

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Purification of human anti-TF [Thomsen-Friedenreich] and anti-Tn antibodies by affinity chromatography on glycophorin A derivatives and characterization of the antibodies by microtiter plate ELISA

100%

Duk M., Lisowska E.

Archivum Immunologiae et Therapiae Experimentalis

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1998

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tom 46

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nr 2

2

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Kalibracja i ocena trwałości krajowego wzorca tromboblastyny do oznaczeń czasu protrombinowego

81%

Lopaciuk S., Witwicki J., Ziembinski W., Duk M.

Diagnostyka Laboratoryjna

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1988

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tom 24

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nr 2

3

Regresyjne modele zmian poziomu zanieczyszczeń powietrza atmosferycznego w Krakowie w okresie 1968-1984

81%

Seroka W., Duk M., Krzyzanowski M.

Roczniki Państwowego Zakładu Higieny

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1987

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tom 38

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nr 6

4

Paul-Bunnell antigen and a possible mechanism of formation of heterophile antibodies in patients with infectious mononucleosis

81%

Golaszewska E., Kurowska E., Duk M., Koscielak J.

Acta Biochimica Polonica

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2003

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tom 50

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nr 4

Sera of patients with infectious mononucleosis contain heterophile anti-Paul- Bunnell (PB) antibodies to erythrocytes of numerous mammalian species. Evidence is presented that the corresponding antigen of bovine erythrocytes is not, as previously described, a single molecule, but a series of glycoproteins with glycans terminated with .-glycolylneuraminic acid (Neu5Gc). The latter compound should be an important part of the PB epitope because, in agreement with the results of others, we found that desialylation of the PB antigen abolishes almost completely its activity. We examined three different preparations of GM3 ganglioside for their capacity to bind anti-PB and found that only GM3 from horse erythrocytes containing Neu5Gc exhibited a low although ELISA measurable PB activity. The other two GM3 preparations, from bovine milk and dog erythrocytes, containing .-acetylneuraminic acid (Neu5Ac) bound little if any anti-PB antibodies. This finding confirms a previous report that human erythrocyte Neu5Ac containing sialoglycoprotein with similar O-linked glycans as the PB-antigen of bovine erythrocytes exhibits only very low PB activity (Patarca & Fletcher, 1995, Crit Rev Oncogen., 6: 305). In conclusion, we present a hypothesis that anti-PB antibodies in patients with infectious mononucleosis are formed against infection-induced cell membrane glycoconjugates containing highly immunogenic Neu5Gc.

5

Subtle differences in glycosylation of blood group M and N type glycophorin A detected with anti-Tn lectins and confirmed by chemical analysis

81%

Krotkiewski H., Duk M., Lisowska E.

Acta Biochimica Polonica

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1995

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tom 42

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nr 1

A higher content of Tn and sialyl-Tn receptors in glycophorin A of blood group N than in that of blood group M was suggested by reactions with anti-Tn lectins. Analysis of [^-elimination products of two blood group M and two blood group N preparations by gas liquid chromatography-mass spectrometry showed that GalNAc- -ol was detectable in minor amounts in all analyzed samples and its content was higher in the products obtained from desialylated antigens. Moreover, the content of Gal N Ac- -ol detected in blood group N samples was almost twice as high as in respective blood group M samples. Since blood group M and N antigens differ in two amino-acid residues, our results support the existence of sequence-dependent differences in efficiency of substitution of glycophorin GalNAc-Ser/Thr residues with galactose.

6

The effect of carbohydrate moiety structure on the immunoregulatory activity of lactoferrin in vitro

71%

Zimecki M., Artym J., Kocieba M., Duk M., Kruzel M. L.

Cellular and Molecular Biology Letters

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2014

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tom 19

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nr 2

The aim of this study was to evaluate the immunoregulatory effects of recombinant human lactoferrin (rhLF) in two in vitro models: (1) the secondary humoral immune response to sheep erythrocytes (SRBC); and (2) the mixed lymphocyte reaction (MLR). We compared the non-sialylated glycoform of rhLF as expressed by glycoengineered Pichia pastoris with one that was further chemically sialylated. In an earlier study, we showed that sialylated rhLF could reverse methotrexate-induced suppression of the secondary immune response of mouse splenocytes to SRBC, and that the phenomenon is dependent on the interaction of lactoferrin (LF) with sialoadhesin (CD169). We found that the immunorestorative activity of sialylated rhLF is also dependent on its interaction with the CD22 antigen, a member of the immunoglobulin superfamily that is expressed by B lymphocytes. We also demonstrated that only sialylated rhLF was able to inhibit the MLR reaction. MLR was inhibited by bovine lactoferrin (bLF), a glycoform that has a more complex glycan structure. Desialylated bLF and lactoferricin, a bLF-derived peptide devoid of carbohydrates, did not express such inhibitory activity. We showed that the interaction of LF with sialic acid receptors is essential for at least some of the immunoregulatory activity of this glycoprotein.

7

Analysis of recombinant Duffy protein-linked N-glycans using lectins and glycosidases

71%

Grodecka M., Czerwinski M., Duk M., Lisowska E., Wasniowska K.

Acta Biochimica Polonica

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2010

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tom 57

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nr 1

49-53

Duffy antigen is a glycosylated blood group protein acting as a malarial and chemokine receptor. Using glycosylation mutants we have previously demonstrated, that all three potential glycosylation sites of the Duffy antigen are occupied by N-linked oligosaccharide chains. In this study, wild-type Duffy glycoprotein and three mutants, each containing a single N-glycan, were used to characterize the oligosaccharide chains by lectin blotting and endoglycosidase digestion. The positive reaction of all the recombinant Duffy forms with Datura stramonium and Sambucus nigra lectins showed that each Duffy N-linked glycan contains Galβ1-4GlcNAc units terminated by (α2-6)-linked sialic acid residues, typical of complex oligosaccharides. The reactivity with Aleuria aurantia and Lens culinaris lectins suggested the presence of (α1-6)-linked fucose at the N-glycan chitobiose core. The failure of the Galanthus nivalis and Canavalia ensiformis lectins to bind to any of the Duffy mutants or to the wild-type antigen indicated that none of the three Duffy N-glycosylation sites carries detectable levels of high-mannose oligosaccharide chains. Digestion of Duffy samples with peptide N-glycosidase F and endoglycosidase H confirmed the presence of N-linked complex oligosaccharides. Our results indicate that Duffy antigen N-glycans are mostly core-fucosylated complex type oligosaccharides rich in N-acetyllactosamine and terminated by (α2-6)-linked sialic acid residues.

8

Two monoclonal antibodies recognizing different epitopes of blood group N antigen

61%

Wasniowska K., Duk M., Steuden I., Czerwinski M., Wiedlocha A., Lisowska E.

Archivum Immunologiae et Therapiae Experimentalis

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1988

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tom 36

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nr 5

Ograniczanie wyników

Purification of human anti-TF [Thomsen-Friedenreich] and anti-Tn antibodies by affinity chromatography on glycophorin A derivatives and characterization of the antibodies by microtiter plate ELISA

Kalibracja i ocena trwałości krajowego wzorca tromboblastyny do oznaczeń czasu protrombinowego

Regresyjne modele zmian poziomu zanieczyszczeń powietrza atmosferycznego w Krakowie w okresie 1968-1984

Paul-Bunnell antigen and a possible mechanism of formation of heterophile antibodies in patients with infectious mononucleosis

Subtle differences in glycosylation of blood group M and N type glycophorin A detected with anti-Tn lectins and confirmed by chemical analysis

The effect of carbohydrate moiety structure on the immunoregulatory activity of lactoferrin in vitro

Analysis of recombinant Duffy protein-linked N-glycans using lectins and glycosidases

Two monoclonal antibodies recognizing different epitopes of blood group N antigen