Wynik wyszukiwania w bazie Polska Bibliografia Lekarska GBL

Zapytanie: LITYŃSKA
Liczba odnalezionych rekordów: 3



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Tytuł oryginału: Adhesion properties of human bladder cell lines with extracellular matrix components: the role of integrins and glycosylation.
Autorzy: Lityńska Anna, Przybyło Małgorzata, Pocheć Ewa, Laidler Piotr
Źródło: Acta Bioch. Pol. 2002: 49 (3) s.643-650, il., bibliogr. s. 649-650
Sygnatura GBL: 303,116

Hasła klasyfikacyjne GBL:
  • onkologia
  • urologia

    Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • in vitro

    Streszczenie angielskie: Integrin subunits present on human bladder cells displayed heterogeneous functional specificity in adhesion to extracellular matrix proteins (ECM). The non-malignant cell line (HCV29) showed significantly higher adhesion efficiency to collagen IV, laminin (LN) and fibronectin (FN) than cancer (T24, Hu456) and v-raf transfected (BC3726) cell lines. Specific antibodies to the ŕ2, ŕ5 and á1 integrin subunits inhibited adhesion of the non-malignant cells, indicating these integrin participation in the adhesion to ECM proteins. in contrast, adhesion of cancer cells was not inhibited by specific antibodies to the á1 integrin subunit. Antiboedies to ŕ3 integrin increased adhesion of cancer cells to collagen, LN and FN, but also of the HCV29 line with colagen. It seems that ŕ3 subunit plays a major role in modulation of other integrin receptors especially in cancer cells. Differences in adhesion to ECM proteins between the non-malignant and cancer cell lines in response to Gal and Fuc were not evident, except for the v-raf transfected cell line which showed a distinct about 6-fold increased adhesion to LN on addition of both saccharides. N-Acetylneuraminic acid inhibited adhesion of all cell lines to LN and FN irrespective of their malignancy.

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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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