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Wyszukujesz frazę "phosphatidylinositol 3-kinase" wg kryterium: Temat

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    Wyświetlanie 1-4 z 4
    Tytuł:
    Interplay between phosphoinositides and Ca2plus in phototropin1- and phototropin2-mediated chloroplast movements in Arabidopsis
    Autorzy:
    Aggarwal, C.
    Labuz, J.
    Gabrys, H.
    Powiązania:
    https://bibliotekanauki.pl/articles/80183.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    phototropin
    plasma membrane
    Arabidopsis thaliana
    phosphoinositide
    chloroplast movement
    phosphatidylinositol 3-kinase
    phosphatidylinositol
    Źródło:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
    0860-7796
    Pojawia się w:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Ganoderma lucidum extract stimulates glucose uptake in L6 rat skeletal muscle cells
    Autorzy:
    Jung, Kyung
    Ha, Eunyoung
    Kim, Mi-Ja
    Uhm, Yoon
    Kim, Hye
    Hong, Seung-Jae
    Chung, Joo-Ho
    Yim, Sung-Vin
    Powiązania:
    https://bibliotekanauki.pl/articles/1041224.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Ganoderma lucidum extract
    skeletal muscle
    phosphatidylinositol 3-kinase
    AMP-activated protein kinase
    glucose uptake
    Opis:
    The effect of Ganoderma lucidum extract on glucose uptake was studied in L6 rat skeletal muscle cells. G. lucidum extract increased glucose uptake about 2-fold compared to control. The extract stimulated the activity of phosphatidylinositol (PI) 3-kinase which is a major regulatory molecule in the glucose uptake pathway. About 7-fold increased activity of a PI 3-kinase was observed after treatment with G. lucidum extract, whereas PI 3-kinase inhibitor, LY294002, blocked the G. lucidum extract-stimulated PI 3-kinase activity in L6 skeletal muscle cells. Protein kinase B, a downstream mediator of PI 3-kinase, was also activated by G. lucidum extract. We then assessed the activity of AMP-activated protein kinase (AMPK), another regulatory molecule in the glucose uptake pathway. G. lucidum extract increased the phosphorylation level of both AMPK α1 and α2. Activity of p38 MAPK, a downstream mediator of AMPK, was also increased by G. lucidum extract. Taken together, these results suggest that G. lucidum extract may stimulate glucose uptake, through both PI 3-kinase and AMPK in L6 skeletal muscle cells thereby contributing to glucose homeostasis.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 3; 597-601
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Bidirectional regulation of renal cortical Na+,K+-ATPase by protein kinase C.
    Autorzy:
    Bełtowski, Jerzy
    Marciniak, Andrzej
    Jamroz-Wiśniewska, Anna
    Borkowska, Ewelina
    Wójcicka, Grażyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1041555.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    phosphatidylinositol-3-kinase
    protein kinase C
    cytochrome P450-dependent arachidonate metabolites
    Na+,K+-ATPase
    Opis:
    We examined the role of protein kinase C (PKC) in the regulation of Na+,K+- ATPase activity in the renal cortex. Male Wistar rats were anaesthetized and the investigated reagents were infused into the abdominal aorta proximally to the renal arteries. A PKC-activating phorbol ester, phorbol 12,13-dibutyrate (PDBu), had a dose-dependent effect on cortical Na+,K+-ATPase activity. Low dose of PDBu (10-11 mol/kg per min) increased cortical Na+,K+-ATPase activity by 34.2%, whereas high doses (10-9 and 10-8 mol/kg per min) reduced this activity by 22.7% and 35.0%, respectively. PDBu administration caused changes in Na+,K+-ATPase Vmax without affecting K0.5 for Na+, K+ and ATP as well as Ki for ouabain. The effects of PDBu were abolished by PKC inhibitors, staurosporine, GF109203X, and Gö 6976. The inhibitory effect of PDBu was reversed by pretreatment with inhibitors of cytochrome P450-dependent arachidonate metabolism, ethoxyresorufin and 17-octadecynoic acid, inhibitors of phosphatidylinositol 3-kinase (PI3K), wortmannin and LY294002, and by actin depolymerizing agents, cytochalasin D and latrunculin B. These results suggest that PKC may either stimulate or inhibit renal cortical Na+,K+-ATPase. The inhibitory effect is mediated by cytochrome P450-dependent arachidonate metabolites and PI3K, and is caused by redistribution of the sodium pump from the plasma membrane to the inactive intracellular pool.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 3; 757-772
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Side-chain modified vitamin D analogs require activation of both PI 3-K and erk1,2 signal transduction pathways to induce differentiation of human promyelocytic leukemia cells.
    Autorzy:
    Marcinkowska, Ewa
    Kutner, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1043768.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    CD11b
    cytosolic phospholipase A2
    p70S6K
    nuclear vitamin D receptor
    CD14
    analogs
    phosphatidylinositol 3-kinase
    extracellular-signal regulated kinase
    1,25-dihydroxyvitamin D3
    HL-60 cells
    differentiation
    Opis:
    Synthetic analogs of vitamin D for potential use in differentiation therapy should selectively regulate genes necessary for differentiation without inducing any perturbations in calcium homeostasis. PRI-1906, an analog of vitamin D2, and PRI-2191, an analog of vitamin D3 bind nuclear vitamin D receptor (nVDR) with substantially lower affinity than 1,25-dihydroxyvitamin D3 (1,25-D3), but have higher differentiation-inducing activity as estimated in HL-60 leukemia cell model. To examine how their increased differentiation-inducing activity is regulated we tested the hypothesis that membrane-mediated events, unrelated to nVDR, take part in the differentiation in response to PRI-1906 and PRI-2191. The induction of leukemia cell differentiation in response to the analogs of vitamin D was inhibited by LY294002 (phosphatidylinositol 3-kinase inhibitor), PD98059 (inhibitor of MEK1,2, an upstream regulator of extracellular-signal regulated kinase) and rapamycin (p70S6K inhibitor) pointing out that activation of signal transduction pathways unrelated to nVDR is necessary for differentiation. On the other hand, inhibition of cytosolic phospholipase A2 accelerated the differentiation of HL-60 cells induced by either 1,25-D3 or by the vitamin D analogs suggesting possible existence of a feedback loop between extracellular-signal regulated kinases and phospholipase A2.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 393-406
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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