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    Wyświetlanie 1-3 z 3
    Tytuł:
    Effect of α3β1 and αvβ3 integrin glycosylation on interaction of melanoma cells with vitronectin
    Autorzy:
    Janik, Marcelina
    Przybyło, Małgorzata
    Pocheć, Ewa
    Pokrywka, Małgorzata
    Lityńska, Anna
    Powiązania:
    https://bibliotekanauki.pl/articles/1040422.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    adhesion
    integrin
    glycosylation
    migration
    vitronectin
    Opis:
    The metastatic transformation of melanocytes is associated with altered expression of adhesion molecules, including αvβ3 and α3β1 integrins. Integrin αvβ3 is a primary vitronectin (VN) receptor, while both integrin types take part in adhesion to VN when they are in complex with uPAR. Although their role in melanoma cell interaction with VN is of great interest, the influence of N-oligosaccharides attached to these glycoproteins is still unappreciated. The present study assesses the role of αvβ3 and α3β1 integrins and the influence of their glycosylation status on WM9 and WM239 metastatic melanoma cell interactions with VN. Cell adhesion to and migration on VN were selected as the studied cell behaviour parameters. Functionblocking antibodies and swainsonine (SW) treatment were used in these tests. Both cell lines interacted with VN in an integrin-mediated but cell-line-specific manner. In WM9 cells, migration was not completely inhibited by antibodies against α3β1 or αvβ3 integrins, suggesting the participation of other VN receptors. In both cell lines in coprecipitation test the formation of an integrins/uPAR complex was shown. In the presence of SW formation of the complex did not occur, suggesting the participation of glycosylation in this proccess. Additionally, the adhesion properties of WM9 cells were changed after SW treatment. Our results suggest that in these two metastatic cell lines integrin-linked N-oligosaccharides influence the VN adhesion receptor activity and function.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 1; 55-61
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    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
    Powiązania:
    https://bibliotekanauki.pl/articles/1043727.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycosylation
    integrins
    bladder cell lines
    adhesion
    Opis:
    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 α2, a5 and β1 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 β1 integrin subunit. Antibodies to α3 integrin increased adhesion of cancer cells to collagen, LN and FN, but also of the HCV29 line with colagen. It seems that α3 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.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 3; 643-650
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The structure of the oligosaccharides of α3β1 integrin from human ureter epithelium (HCV29) cell line.
    Autorzy:
    Lityńska, Anna
    Pocheć, Ewa
    Hoja-Łukowicz, Dorota
    Kremser, Elżbieta
    Laidler, Piotr
    Amoresano, Angela
    Monti, Chiara
    Powiązania:
    https://bibliotekanauki.pl/articles/1043787.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycosylation
    α3β1 integrin
    cell line
    MALDI MS
    Opis:
    There is a growing line of evidence that glycosylation of α and β subunits is important for the function of integrins. Integrin α3β1, 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 α3β1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi- tri- and tetraantennary structures were the most common, while high-mannose type structures were minor. Also the presence of short poly-N-acetyllactosamine entities was shown. These results show that while the predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 491-500
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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