Wynik wyszukiwania w bazie Polska Bibliografia Lekarska GBL

Zapytanie: HOJA-ŁUKOWICZ
Liczba odnalezionych rekordów: 2



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Tytuł oryginału: The structure of the oligosaccharides of ŕ3á1 integrin from human ureter epithelium (HCV29) cell line.
Autorzy: Lityńska Anna, Pocheć Ewa, Hoja-Łukowicz Dorota, Kremser Elżbieta, Laidler Piotr, Amoresano Angela, Monti Chiara
Źródło: Acta Bioch. Pol. 2002: 49 (2) s.491-500, il., tab., bibliogr. s. 499-500
Sygnatura GBL: 303,116

Hasła klasyfikacyjne GBL:
  • urologia

    Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • in vitro

    Streszczenie angielskie: There is a growing line of evidence that glycosylation of ŕ and á subunits is important for the function of integrins. Integrin ŕ3á1, 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 sulfate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide N-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spectrometry. Our findings demonstrated, in both subunits of integrin ŕ3á1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi-tri- and tetraantennary structures were the most common, while hig-mannose type structures were minor. Also the presence of short poly-N-acetyllactosamine entities was shown. These results show that while tha predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.

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    Tytuł oryginału: Carbohydrate moieties of N-cadherin from human melanoma cell lines.
    Autorzy: Ciołczyk-Wierzbicka Dorota, Gil Dorota, Hoja-Łukowicz Dorota, Lityńska Anna, Laidler Piotr
    Źródło: Acta Bioch. Pol. 2002: 49 (4) s.991-998, il., tab., bibliogr. 997-998
    Sygnatura GBL: 303,116

    Hasła klasyfikacyjne GBL:
  • hematologia
  • onkologia
  • dermatologia i wenerologia

    Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Streszczenie angielskie: Expression of N-cadherin an adhesion molecule of the cadherin family, in tumor cells as 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 inhuman melanoma cell lines: WM35 from the primary tumor site and WM239, WM9, and A375 from different metastatic sits. N-cadherin was immunoprecipitated with anti-human N-cadherin plyclonal antibodies. Characterisation of its carbohydrate moieties was carried out by SDS/PAGE electrophoresis and blotting, followed by immunochemical identification of the N-catherin polypeptides and analysis of their hlycans using highly specifica digoxigenin or biotin labaelled 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 oligosaccharides with ŕ2-6 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 ŕ-fucose. In addition, N-cadherin from WM (lymphomodus metastatic site) adn A375 (solid tumor metastatic site) contained complex type chains with ŕ2-3 sialic acid (positive reaction with Maackia amurensis agglutinin - MAA). The results demonstrated that N-glcans of N-cadherin are altered in metastatic melanomas in a way charakteristic for invasive tumor cells.

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