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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F08%3A00005343%21RIV09-MSM-15310___
rdf:type
skos:Concept n12:Vysledek
dcterms:description
The quaternary benzo[c]phenanthridine alkaloid chelerythrine is widely used as an inhibitor of protein kinase C (PKC). However, in biological systems chelerythrine interacts with an array of proteins. In this study, we examined the effects of chelerythrine and sanguinarine on conventional PKCs (cPKCs) and PKC upstream kinase, phosphoinositide-dependent protein kinase 1 (PDK1), under complete inhibition conditions of PKC-dependent oxidative burst. In neutrophil-like HL-60 cells, sanguinarine and chelerythrine inhibited N-formyl-Met-Leu-Phe, phorbol 12-myristate 13-acetate (PMA)-, and A23187-induced oxidative burst with IC50 values not exceeding 4.6 mu mol/L, but the inhibition of PMA-stimulated cPKC activity in intact cells required at least fivefold higher alkaloid concentrations. At concentrations below 10 mu mol/L, sanguinarine and chelerythrine prevented phosphorylation of similar to 80 kDa protein and sequestered similar to 60 kDa phosphoprotein in cytosol. Moreover, neither sanguinarine nor chele The quaternary benzo[c]phenanthridine alkaloid chelerythrine is widely used as an inhibitor of protein kinase C (PKC). However, in biological systems chelerythrine interacts with an array of proteins. In this study, we examined the effects of chelerythrine and sanguinarine on conventional PKCs (cPKCs) and PKC upstream kinase, phosphoinositide-dependent protein kinase 1 (PDK1), under complete inhibition conditions of PKC-dependent oxidative burst. In neutrophil-like HL-60 cells, sanguinarine and chelerythrine inhibited N-formyl-Met-Leu-Phe, phorbol 12-myristate 13-acetate (PMA)-, and A23187-induced oxidative burst with IC50 values not exceeding 4.6 mu mol/L, but the inhibition of PMA-stimulated cPKC activity in intact cells required at least fivefold higher alkaloid concentrations. At concentrations below 10 mu mol/L, sanguinarine and chelerythrine prevented phosphorylation of similar to 80 kDa protein and sequestered similar to 60 kDa phosphoprotein in cytosol. Moreover, neither sanguinarine nor chele Kvartérní benzo[c]fenanthridinový alkaloid chelerythrin je široce využíván jako inhibitor protein kinasy C (PKC). V biologických systémech ale chelerythrin interaguje s plejádou proteinů. V této studii jsme zkoumali účinky chelerythrinu a sanguinarinu na konvenční PKCs (cPKCs) a PKC upstream kinasu, fosfoinositidedependent protein kinasu 1 (PDK1), za podmínek kompletní inhibice PKC-dependentního oxidativního vzplanutí. V neutrofilům podobných buňkách HL-60 cells, inhibovaly sanguinarin a chelerythrin N-formyl-Met-Leu-Phe, phorbol 12-myristate 13-acetate (PMA)-, a A23187-indukované oxidativní vzplanutí, s hodnotami IC50 nepřesahující 4.6 μmol/L, ale inhibice PMA-stimulované cPKC aktivity v intaktních buňkách vyžadovala nejméně pětkrát vyšší koncentraci alkaloidu. Sanguinarin a chelerythrin bránily fosforylaci 80 kDa proteinu a zadržovaly 60 kDa fosfoproteid v cytosolu v koncentracích pod 10 μmol/L. Navíc ani sanguinarin ani chelerythrin neblokovaly PMA-stimulovanou translokaci a
dcterms:title
Conventional protein kinase C isoenzymes undergo dephosphorylation in neutrophil-like HL-60 cells treated by chelerythrine or sanguinarine Conventional protein kinase C isoenzymes undergo dephosphorylation in neutrophil-like HL-60 cells treated by chelerythrine or sanguinarine Isoenzymy konvenční protein dinasy C podléhají defosforylaci v neutrofilům podobných HL-60 buňkách inkubovaných s chelerythrinem a sanguinarinem.
skos:prefLabel
Isoenzymy konvenční protein dinasy C podléhají defosforylaci v neutrofilům podobných HL-60 buňkách inkubovaných s chelerythrinem a sanguinarinem. Conventional protein kinase C isoenzymes undergo dephosphorylation in neutrophil-like HL-60 cells treated by chelerythrine or sanguinarine Conventional protein kinase C isoenzymes undergo dephosphorylation in neutrophil-like HL-60 cells treated by chelerythrine or sanguinarine
skos:notation
RIV/61989592:15310/08:00005343!RIV09-MSM-15310___
n5:aktivita
n16:P n16:Z
n5:aktivity
P(GP303/06/P193), Z(MSM6198959216)
n5:cisloPeriodika
1
n5:dodaniDat
n10:2009
n5:domaciTvurceVysledku
n14:1030957 n14:8069239 n14:2514559
n5:druhVysledku
n15:J
n5:duvernostUdaju
n19:S
n5:entitaPredkladatele
n9:predkladatel
n5:idSjednocenehoVysledku
361289
n5:idVysledku
RIV/61989592:15310/08:00005343
n5:jazykVysledku
n11:eng
n5:klicovaSlova
chelerythrine; HL-60 cells; oxidative burst; phosphoinositide-dependent protein kinase 1; protein kinase C; sanguinarine
n5:klicoveSlovo
n6:protein%20kinase%20C n6:oxidative%20burst n6:chelerythrine n6:sanguinarine n6:phosphoinositide-dependent%20protein%20kinase%201 n6:HL-60%20cells
n5:kodStatuVydavatele
NL - Nizozemsko
n5:kontrolniKodProRIV
[EC956DDA4268]
n5:nazevZdroje
Cell Biology and Toxicology
n5:obor
n13:CE
n5:pocetDomacichTvurcuVysledku
3
n5:pocetTvurcuVysledku
4
n5:projekt
n18:GP303%2F06%2FP193
n5:rokUplatneniVysledku
n10:2008
n5:svazekPeriodika
24
n5:tvurceVysledku
Ulrichová, Jitka Dvořák, Zdeněk Modrianský, Martin Vrba, Jiří
n5:zamer
n17:MSM6198959216
s:issn
0742-2091
s:numberOfPages
15
n3:organizacniJednotka
15310