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1

The lectin-binding pattern of nucleolin and its interaction with endogenous galectin-3

100%
Hoja-Lukowicz D., Kedracka-Krok S., Duda W., Litynska A.
Cellular and Molecular Biology Letters
|
2014
|
tom 19
|
nr 3
Unlike nuclear nucleolin, surface-expressed and cytoplasmic nucleolin exhibit Tn antigen. Here, we show localization-dependent differences in the glycosylation and proteolysis patterns of nucleolin. Our results provide evidence for different paths of nucleolin proteolysis in the nucleus, in the cytoplasm, and on the cell surface. We found that full-length nucleolin and some proteolytic fragments coexist within live cells and are not solely the result of the preparation procedure. Extranuclear nucleolin undergoes N- and O-glycosylation, and unlike cytoplasmic nucleolin, membrane-associated nucleolin is not fucosylated. Here, we show for the first time that nucleolin and endogenous galectin-3 exist in the same complexes in the nucleolus, the cytoplasm, and on the cell surface of melanoma cells. Assessments of the interaction of nucleolin with galectin-3 revealed nucleolar co-localization in interphase, suggesting that galectin-3 may be involved in DNA organization and ribosome biogenesis.
2

N-glycoproteins bearing beta1-6 branching oligosaccharides from A375 human melanoma cell line analysed by HPLC/MS

100%
Ochwat D., Hoja-Lukowicz D., Pochec E., Litynska A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
3

Oligosaccharide structures of N-cadherin from human normal and cancer bladder cell lines by matrix-assisted laser desorption mass spectrometry

88%
Hoja-Lukowicz D., Litynska A., Amoresano A., Ciolczyk-Wierzbicka D., Laidler P.
Acta Biologica Cracoviensia. Series Zoologia
|
2007
|
tom 49
31-39
4

Carbohydrate moieties of N-cadherin from human melanoma cell lines

88%
Ciolczyk-Wierzbicka D., Gil D., Hoja-Lukowicz D., Litynska A., Laidler P.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
Expression of N-cadherin an adhesion molecule of the cadherin family, in tumor cells is associated with their increased invasive potential. Many studies suggested the role of N-linked oligosaccharides as important factors that contribute to metastasis by influencing tumor cell invasion and adhesion. N-cadherin is a heavily glycosylated protein. We have analysed the carbohydrate profile of this protein synthesized in hu­man melanoma cell lines: WM35 from the primary tumor site and WM239, WM9, and A375 from different metastatic sites. N-cadherin was immunoprecipitated with anti-human N-cadherin polyclonal antibodies. Characterisation of its carbohydrate moieties was carried out by SDS/PAGE electrophoresis and blotting, followed by im- munochemical identification of the N-cadherin polypeptides and analysis of their glycans using highly specific digoxigenin or biotin labelled lectins. The positive reac­tion of N-cadherin from the WM35 cell line with Galanthus nivalis agglutinin (GNA), Datura stramonium agglutinin (DSA) and Sambucus nigra agglutinin (SNA) indicated the presence of high-mannose type glycans and biantennary complex type oligosac- charides with a2-6 linked sialic acid. N-cadherin from WM239, WM9, and A375 cell lines gave a positive reaction with Phaseolus vulgaris leukoagglutinin (L-PHA) and lo­tus Tetragonolobus purpureas agglutinin (LTA). This indicated the presence of tri- or tetra-antennary complex type glycans with a-fucose. In addition, N-cadherin from WM9 (lymphomodus metastatic site) and A375 (solid tumor metastatic site) contained complex type chains with 2–3 sialic acid (positive reaction with Maackia amurensis agglutinin — MAA). The results demonstrated that N-glycans of N-cadherin are altered in metastatic melanomas in a way characteristic for invasive tumor cells.
5

Identification of PNA-positive proteins in the primary uveal melanoma cell line by mass spectrometry

76%
Hoja-Lukowicz D., Litynska A., Pochec E., Przybylo M., Kremser E., Ciolczyk-Wierzbicka D., Laidler P.
Acta Biologica Cracoviensia. Series Zoologia
|
2006
|
tom 48
39-47
6

The structure of the oligosaccharides of alpha3beta1 integrin from human ureter epithelium [HCV29] cell line

76%
Litynska A., Pochec E., Hoja-Lukowicz D., Kremser E., Laidler P., Amoresano A., Monti C.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 2
There is a growing line of evidence that glycosylation of a and β subunits is impor­tant for the function of integrins. Integrin a3β1, from human ureter epithelium cell — line HCV29, was isolated by affinity chromatography on laminin GD6 peptide. Char­acterization of its carbohydrate moieties was carried out using sodium dodecyl sul- fate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide .-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spec- trometry. Our findings demonstrated, in both subunits of integrin a3β1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi- tri- and tetra- antennary structures were the most common, while high-mannose type structures were minor. Also the presence of short poly-. -acetyllactosamine entities was shown. These results show that while the predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.
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