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Statements

Subject Item
n2:RIV%2F61989592%3A15110%2F08%3A00007391%21RIV09-MSM-15110___
rdf:type
n14:Vysledek skos:Concept
dcterms:description
We recently demonstrated that TLCK and TPCK could act as potent but nonspecific inhibitors of mature caspases [Frydrych and Mlejnek [2008] J Cell Biochem 103:1646-1656]. The question whether TLCK and TPCK inhibit simultaneously caspase activation and/or processing remained, however, open. In this article, we demonstrated that TPCK even enhanced caspase-3 and caspase-7 processing although it substantially inhibited caspase-3 and caspase-7 enzymatic (DEVDase) activity in HL-60 cells exposed to various cell death inducing stimuli. Under the same conditions, TLCK had no effect or affected caspase-3 and caspase-7 processing marginally depending on cell treatment used. Importantly, TLCK substantially inhibited caspase-3 and caspase-7 enzymatic (DEVDase) activity irrespectively to the treatment used. Interestingly, treatment of cells with toxic concentrations of TPCK alone was accompanied by full caspase-3 and -7 processing even if it induced necrosis. In contrast, treatment of cells with concentrations of T V nedávné době jsme ukázali, že TLCK a TPCK působí jako účinné, ale nespecifické inhibitory aktivovaných kaspáz [Frydrych and Mlejnek [2008] J Cell Biochem 103:1646-1656]. Nicméně otázka zda-li TLCK a TPCK současně inhibují aktivaci kaspáz zůstala otevřená. We recently demonstrated that TLCK and TPCK could act as potent but nonspecific inhibitors of mature caspases [Frydrych and Mlejnek [2008] J Cell Biochem 103:1646-1656]. The question whether TLCK and TPCK inhibit simultaneously caspase activation and/or processing remained, however, open. In this article, we demonstrated that TPCK even enhanced caspase-3 and caspase-7 processing although it substantially inhibited caspase-3 and caspase-7 enzymatic (DEVDase) activity in HL-60 cells exposed to various cell death inducing stimuli. Under the same conditions, TLCK had no effect or affected caspase-3 and caspase-7 processing marginally depending on cell treatment used. Importantly, TLCK substantially inhibited caspase-3 and caspase-7 enzymatic (DEVDase) activity irrespectively to the treatment used. Interestingly, treatment of cells with toxic concentrations of TPCK alone was accompanied by full caspase-3 and -7 processing even if it induced necrosis. In contrast, treatment of cells with concentrations of T
dcterms:title
Inhibitory serinových proteáz N-α-Tosyl-L-Lysinyl-Chloromethylketone (TLCK) a N-Tosyl-L-Phenylalaninyl-Chloromethylketone (TPCK) neinhibují aktivaci kaspázy-3 a kaspázy-7 u buněk vystavených působení pro-apoptotických podnětů Serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK) do not inhibit caspase-3 and caspase-7 processing in cells exposed to pro-apoptotic inducing stimuli Serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK) do not inhibit caspase-3 and caspase-7 processing in cells exposed to pro-apoptotic inducing stimuli
skos:prefLabel
Serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK) do not inhibit caspase-3 and caspase-7 processing in cells exposed to pro-apoptotic inducing stimuli Serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK) do not inhibit caspase-3 and caspase-7 processing in cells exposed to pro-apoptotic inducing stimuli Inhibitory serinových proteáz N-α-Tosyl-L-Lysinyl-Chloromethylketone (TLCK) a N-Tosyl-L-Phenylalaninyl-Chloromethylketone (TPCK) neinhibují aktivaci kaspázy-3 a kaspázy-7 u buněk vystavených působení pro-apoptotických podnětů
skos:notation
RIV/61989592:15110/08:00007391!RIV09-MSM-15110___
n3:aktivita
n9:Z
n3:aktivity
Z(MSM6198959216)
n3:cisloPeriodika
6
n3:dodaniDat
n5:2009
n3:domaciTvurceVysledku
n10:1076914 n10:3774007
n3:druhVysledku
n18:J
n3:duvernostUdaju
n6:S
n3:entitaPredkladatele
n17:predkladatel
n3:idSjednocenehoVysledku
394474
n3:idVysledku
RIV/61989592:15110/08:00007391
n3:jazykVysledku
n15:eng
n3:klicovaSlova
SERINE PROTEASE INHIBITORS; MATURE CASPASES; CASPASE-3 PROCESSING; CASPASE-7 PROCESSING; APOPTOSIS; NECROSIS
n3:klicoveSlovo
n7:CASPASE-7%20PROCESSING n7:CASPASE-3%20PROCESSING n7:SERINE%20PROTEASE%20INHIBITORS n7:APOPTOSIS n7:MATURE%20CASPASES n7:NECROSIS
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[65746941525D]
n3:nazevZdroje
Journal of Cellular Biochemistry
n3:obor
n4:FD
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
2
n3:rokUplatneniVysledku
n5:2008
n3:svazekPeriodika
105
n3:tvurceVysledku
Mlejnek, Petr Frydrych, Ivo
n3:zamer
n16:MSM6198959216
s:issn
0730-2312
s:numberOfPages
6
n13:organizacniJednotka
15110