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Conventional protein kinase C isoenzymes undergo dephosphorylation in neutrophil-like HL-60 cells treated by chelerythrine or sanguinarine

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F08%3A00006992" target="_blank" >RIV/61989592:15110/08:00006992 - isvavai.cz</a>

  • Alternative codes found

    RIV/61989592:15310/08:00005343

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Conventional protein kinase C isoenzymes undergo dephosphorylation in neutrophil-like HL-60 cells treated by chelerythrine or sanguinarine

  • Original language 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 IC(50) values not exceeding 4.6 mumol/L, but the inhibition of PMA-stimulated cPKC activity in intact cells required at least fivefold higher alkaloid concentrations. At concentrations below 10 mumol/L, sanguinarine and chelerythrine prevented phosphorylation of approximately 80 kDa protein and sequestered approximately 60 kDa phosphoprotein in cytosol.

  • Czech name

    Isoenzymy konvenční protein kinasy C podléhají defosforylaci v neutrofilům podobných HL-60 buňkách inkubovaných s chelerythrinem a sanguinarinem.

  • Czech description

    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 nakonvenční 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 ?mol/L, ale inhibice PMA-stimulované cPKC aktivity v intaktních buňkách vyžadovala nejméně pětkrát vyšší koncentracialkaloidu. Sanguinarin a chelerythrin bránily fosforylaci 80 kDa proteinu a zadržovaly 60 kDa fosfoproteid v cytosolu v koncentracích pod 10 ?mol/L. Navíc ani sanguinarin ani chelerythrin neblokovaly PMA-stimulovanou translokaci

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GP303%2F06%2FP193" target="_blank" >GP303/06/P193: Changes of expression of pro-inflammatory enzymes caused by isoquinoline alkaloids during differentiation of promyelocytes into neutrophils</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2008

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Cell Biology and Toxicology

  • ISSN

    0742-2091

  • e-ISSN

  • Volume of the periodical

    24

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    15

  • Pages from-to

  • UT code for WoS article

  • EID of the result in the Scopus database