Autor: Gajewska, J. - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Role of extracellular matrix and prolactin in functional differentiation of bovine BME-UV1 mammary epithelial cells
Autorzy:: Kozlowski, M.
Wilczak, J.
Motyl, T.
Gajewska, M.
Powiązania:: https://bibliotekanauki.pl/articles/31562.pdf
Data publikacji:: 2011
Wydawca:: Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:: Interactions between extracellular matrix (ECM) and epithelial cells are necessary for proper organisation and function of the epithelium. In the present study we show that bovine mammary epithelial cell line BME-UV1 cultured on ECM components, commercially available as Matrigel™, constitutes a good model for studying mechanisms controlling functional differentiation of the bovine mammary gland. In contact with Matrigel BME-UV1 cells induce apicobasal polarity, and within 16 days form three dimensional (3D) acinar structures with a centrally localized hollow lumen, which structurally resemble mammary alveoli present in the functionally active mammary gland. We have shown that the 3D culture system enables a high expression and proper localisation of integrin receptors and tight junction proteins in BME-UV1 cells to be induced. This effect was not obtained in cells grown in the classical 2D culture system on plastic. Moreover, ECM highly stimulated the synthesis of one of the major milk proteins, β-casein, even in the absence of prolactin. Our results show that contact with ECM plays an important role in the lactogenic activity of bovine MECs, however, prolactin is necessary for the efficient secretion of milk proteins.
Źródło:: Polish Journal of Veterinary Sciences; 2011, 14, 3
1505-1773
Pojawia się w:: Polish Journal of Veterinary Sciences
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Interleukin-1beta stimulates early myogenesis of mouse C2C12 myoblasts: the impact on myogenic regulatory factors, extracellular matrix components, IGF binding proteins and protein kinases
Autorzy:: Grabiec, K.
Tokarska, J.
Milewska, M.
Blaszczyk, M.
Gajewska, M.
Grzelkowska-Kowalczyk, K.
Powiązania:: https://bibliotekanauki.pl/articles/30341.pdf
Data publikacji:: 2013
Wydawca:: Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:: The purpose of the study was to examine the mechanisms important for early myogenesis in mouse C2C12 myogenic cells exposed to interleukin-1β. Cyclin A and cyclin B1 were increased by interleukin-1β (1 ng/ml), but the level of cyclin D1 and total DNA content was unaffected. Fusion index and the rate of protein synthesis was increased in the presence of IL-1β, but these effects were limited to 3-day-treatment. IL-1β increased the level of MyoD, myogenin and MHC on the 3rd day of differentiation, without altering the content of the active form of myostatin, as well as it augmented the level of fibronectin, integrin β1 and full length 100 kDa form of ADAM12. IL-1β caused a decrease in IGFBP-4 and IGFBP-6 levels and a marked increase in IGFBP-5. The phosphorylation of PKB and ERK1/2 and the cellular content of p38 were elevated by IL-1β. We conclude that the myogenic effect of IL-1β was limited to the onset of myoblast fusion and was associated with: i) increase in the level of myogenic transcription factors i.e. MyoD and myogenin expression, ii) modification of extracellular matrix assembly and signaling, manifested by an increase in fibronectin, integrin-β1 and ADAM12 content, iii) drop in IGFBP-4 and IGFBP-6, and an increase in IGFBP-5, that could alter the local IGF-1 bioavailability, and iv) increase in phosphorylation of PKB and ERK1/2, and the expression of p38 kinase, leading to activation of intracellular pathways essential for myogenic differentiation.
Źródło:: Polish Journal of Veterinary Sciences; 2013, 16, 2
1505-1773
Pojawia się w:: Polish Journal of Veterinary Sciences
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 3.

Tytuł:: Tumor necrosis factor - Alpha alters integrins and metalloprotease ADAM12 levels and signaling in differentiating myoblasts
Autorzy:: Grzelkowska-Kowalczyk, K.
Tokarska, J.
Grabiec, K.
Gajewska, M.
Milewska, M.
Blaszczyk, M.
Powiązania:: https://bibliotekanauki.pl/articles/31937.pdf
Data publikacji:: 2016
Wydawca:: Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:: The extracellular matrix (ECM) is important in the regulation of myogenesis. We hypothesized that tumor necrosis factor-α (TNF-α) modifies ECM during differentiation of mouse C2C12 myoblasts. Exogenous TNF-α (1 ng/ml) stimulated myoblast fusion on the 3rd day (by 160% vs control) but not on the 5th day of myogenesis. The level of integrin α5 was significantly augmented by TNF-α during 5 day-differentiation; however, integrin β1 was higher than control only on the 3rd day of cytokine treatment. Both the abundance of integrin α5 bound to actin and the level of integrin β1 complexed with integrin α5 increased in the presence of TNF-α, especially on the 3rd day of differentiation. Similarly, the stimulatory effects of TNF-α on integrin α3, metalloprotease ADAM12 and kinases related to integrins, FAK and ILK, were limited to the 3rd day of differentiation. We concluded that TNF-α-induced changes in ECM components in differentiating myogenic cells, i.e. i) increased expression of integrin α5, β1, α3, and metalloprotease ADAM12, ii) enhanced formation of α5β1 integrin receptors and interaction of integrin α5-cytoskeleton, and iii) increased expression of kinases associated with integrin signaling, FAK and ILK, were temporarily associated with the onset of myocyte fusion.
Źródło:: Polish Journal of Veterinary Sciences; 2016, 19, 2
1505-1773
Pojawia się w:: Polish Journal of Veterinary Sciences
Dostawca treści:: Biblioteka Nauki

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