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Wyszukujesz frazę "Jurkat cells" wg kryterium: Temat


Wyświetlanie 1-4 z 4
Tytuł:
Mitochondrial uncoupling does not influence the stability of the intracellular signal activating plasma membrane calcium channels.
Autorzy:
Zabłocki, Krzysztof
Makowska, Agnieszka
Duszyński, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1044178.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Jurkat cells
store-operated calcium entry
mitochondrial uncoupling
thapsigargin
Opis:
The effects of various concentrations of thapsigargin, a specific inhibitor of Ca2+-ATPase in the endoplasmic reticulum (ER) membrane, on calcium homeostasis in lymphoidal T cells (Jurkat) were investigated. Preincubation of these cells suspended in nominally calcium-free medium with 0.1 μM thapsigargin resulted in a complete release of Ca2+ from intracellular calcium stores. When the medium was supplemented with 3 mM CaCl2 the cells maintained constantly elevated level of cytosolic Ca2+. However, thapsigargin applied at lower concentration produced only a partial depletion of the stores. For example, in the cells pretreated with 1 nM thapsigargin and suspended in calcium-free medium approximately 75% of the calcium content was released from the intracellular stores. The addition of 3 mM CaCl2 to such cell suspension led to a transient increase in cytosolic calcium concentration, followed by a return to a lower steady-state. This phenomenon, related to the refilling of the ER by Ca2+, allowed to estimate the half-time for the process of cell recovery after activation of store-operated calcium channels. By this approach we have found that carbonyl cyanide m-chlorophenylhydrazone, which has been documented to inhibit calcium entry into Jurkat cells, does not influence the stability of the intracellular signal involved in the activation of store-operated calcium channels.
Źródło:
Acta Biochimica Polonica; 2001, 48, 1; 157-161
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Synthesis, immunosuppressive properties, mechanism of action and X-ray analysis of a new class of isoxazole derivatives
Autorzy:
Bąchor, Urszula
Ryng, Stanisław
Mączyński, Marcin
Artym, Jolanta
Kocięba, Maja
Zaczyńska, Ewa
Kochanowska, Iwona
Tykarska, Ewa
Zimecki, Michał
Powiązania:
https://bibliotekanauki.pl/articles/895268.pdf
Data publikacji:
2019-04-30
Wydawca:
Polskie Towarzystwo Farmaceutyczne
Tematy:
apoptosis
proliferation
isoxazoles
Passerini three-component reaction
Jurkat cells
Opis:
In the search for potential therapeutics, isoxazole derivatives are still objects of interest. Previously described immunoregulatory properties of 5-amino-3-methyl-4-isoxazolecarboxylic acid (AC) benzylamides prompted us to synthesize a new class of compounds of immunotropic activity. A series of new compounds containing the isoxazole moiety were synthesized using Passerini three-component reaction. The effects on phytohemagglutinin A (PHA)-induced proliferation of human peripheral blood mononuclear cells (PBMC), production of tumor necrosis factor alpha (TNF α) in human whole blood cultures stimulated with lipopolysaccharide (LPS) and two-way mixed lymphocyte reaction (MLR) of PBMC, were investigated. Also, the effect of 1-(cyclohexylcarbamoyl)cyclohexyl 5-amino-3-methylisoxazole-4-carboxylate (PUB1) on the expression of signaling molecules associated with cell apoptosis in Jurkat cells was also determined. The results showed that the compounds inhibited to various degree mitogen-induced PBMC proliferation in a dose-dependent manner and TNF α production at 10 μg/ml. PUB1 compound, selected on the basis of its strongest antiproliferative activity, was also shown to inhibit MLR. The molecular data suggest that immunosuppressive action of PUB1 depended on induction of Fas and elevation of caspase 8 expression. In summary, we revealed immunosuppressive properties of a new class of isoxazoles and established the mechanism of action of a representative PUB1 compound.
Źródło:
Acta Poloniae Pharmaceutica - Drug Research; 2019, 76, 2; 251-263
0001-6837
2353-5288
Pojawia się w:
Acta Poloniae Pharmaceutica - Drug Research
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Participation of phospholipase A2 isoforms in the control of calcium influx into electrically non-excitable cells
Autorzy:
Zabłocki, Krzysztof
Waśniewska, Magdalena
Duszyński, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1044292.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
MDCK cells
Jurkat cells
calcium influx
store-operated channels
phospholipase A2
Opis:
The participation of phospholipase A2 isoforms in capacitative store-operated Ca2+ influx into Jurkat leukemic T and MDCK cells was investigated. Preincubation of Jurkat cells with either bromophenacyl bromide (an inhibitor of secreted phospholipase A2, sPLA2) or Helss (an inhibitor of calcium independent phospholipase A2 - iPLA2) resulted in a significant inhibition of the calcium influx. The extent of this inhibition depended on the pH of the extracellular millieu; it increased with alkalisation. The rate of Ca2+ influx into MDCK cells was reduced by bromophenacyl bromide. Preincubation of these cells with Helss resulted in the stimulation of the influx. These observations suggest the participation of different PLA2 isoforms in the regulation of Ca2+ influx. They also show that the extent that PLA2 isoforms control the influx depends on the pH of the medium. Finally, these data indicate that various phospholipase A2 isoforms may play a role in the control of Ca2+ influx in different cell lines.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 591-599
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Calcium- and proton-dependent relocation of annexin A6 in Jurkat T cells stimulated for interleukin-2 secretion
Autorzy:
Podszywalow-Bartnicka, Paulina
Strzelecka-Kiliszek, Agnieszka
Bandorowicz-Pikula, Joanna
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1041071.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
interleukin-2
ionomycin
calcium
annexin A6
Jurkat T cells
vesicular traffic
Opis:
Annexin A6 (AnxA6) is a Ca2+-dependent membrane-binding protein involved in vesicular traffic. The likely participation of AnxA6 in the response of lymphocytes to Ca2+ signals has not been investigated yet. The present study focuses on intracellular relocation of AnxA6 in human Jurkat T lymphoblasts upon stimulation followed by transient increase of intracellular [Ca2+] and exocytosis of interleukin-2 (IL-2). Stimulation of the cells under different experimental conditions (by lowering pH and/or by rising extracellular [Ca2+] in the presence of ionomycin) induced time-dependent transients of intracellular [Ca2+] and concomitant changes in AnxA6 intracellular localization and in IL-2 secretion, with only minor effects on cell viability and apoptosis. In resting conditions (in the presence of EGTA or with no ionophore) AnxA6 was localized uniformly in the cytosol, whereas it translocated to vesicular structures beneath the plasma membrane within 5 min following stimulation of Jurkat T cells and rise of intracellular [Ca2+] at pH 7.4. Lowering the extracellular pH value from 7.4 to 6.0 significantly enhanced this process. AnxA6 changed its location from the cytosol to the secretory granules and early endosomes which seem to represent membranous targets for annexin. In conclusion, AnxA6 is sensitive to variations in intracellular [Ca2+] upon stimulation of Jurkat T cells, as manifested by a switch in its intracellular localization from the cytosol to vesicular structures located in close proximity to the plasma membrane, suggestive of participation of AnxA6 in calcium- and proton-dependent secretion of cytokines by lymphocytes.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 261-271
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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