Protein kinase C beta in postischemic brain mitochondria

Kowalczyk, Joanna E.; Kawalec, Maria; Beresewicz, M; Dębski, Janusz; Dadlez, Michał; Zabłocka, Barbara

doi:10.1016/j.mito.2011.06.002

Cited by 19 publications

(23 citation statements)

References 28 publications

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“…In the present study, we demonstrated that Smh-3 inhibited the activity of AKT in HL-60 cells (Fig. 8A and B), leading to that BAD was reported to be deposphorylated and then induced apoptosis in Smh-3-treated HL-60 cells (11,28).…”

Section: Discussionsupporting

confidence: 50%

“…8C), which may lead to activation of Bax and inactivation BCL-2, then triggering apoptosis. It has been reported that AKT is involved in survival signaling pathway by phosphorylating BAD (11). The phospho-BAD bound to 14-3-3 proteins, but not BCL-2.…”

Section: Discussionmentioning

confidence: 98%

“…A recent study has also demonstrated that the BCL-2 family proteins such as BAD can regulated mitochondria-mediated apoptotic pathway (11). It is thought that the ability of BAD to bind to BCL-2 is abrogated when BAD becomes phosphorylated at Ser136 by AKT protein kinase (12,13).…”

Section: Introductionmentioning

confidence: 99%

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The novel synthesized 2-(3-(methylamino)phenyl)-6-(pyrrolidin-1-yl)quinolin-4-one (Smh-3) compound induces G2/M phase arrest and mitochondrial-dependent apoptotic cell death through inhibition of CDK1 and AKT activity in HL-60 human leukemia cells

et al. 2011

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Abstract. 2-Phenyl-4-quinolone series compounds have exhibited growth inhibitory influence on several human cancer cell lines. In this study, we investigated the effects of 2-(3-(methylamino)phenyl)-6-(pyrrolidin-1-yl)quinolin-4-one (Smh-3) on viability, cell cycle and apoptotic cell death which occurred in different leukemia cell lines (HL-60, U937 and K562) in a dose-and time-dependent manner, but which did not obviously impair the viability of normal human umbilical vein endothelial cells (HUVEC) in vitro. The approximate IC 50 was 103.26±4.59 nM for a 48 h treatment in HL-60 cells. Cell cycle analysis showed that 100 nM Smh-3 induced significant G 2 /M arrest in examined cells. Within 0, 12, 24 and 48 h of treatment, Smh-3 inhibited CDK1 activity and decreased protein levels of CDK1, cyclin A and cyclin B. Smh-3-induced chromatin condensation and DNA fragmentation were determined by DAPI and TUNEL staining. Cell apoptosis was significantly reduced after pretreatment with a pan-caspase inhibitor (Z-VAD-fmk) and results indicated that Smh-3-induced apoptosis was mainly mediated by activation of the caspase cascade in HL-60 cells. Results from colorimetric assays and Western blot analysis indicated that activities of caspase-9, -7 and -3 were promoted in Smh-3-treated HL-60 cells during cell apoptosis. Smh-3-induced apoptosis in HL-60 cells was accompanied by an apparent increase in ROS production, and protein levels of cytosolic cytochrome c, apoptotic protease activating factor-1 (Apaf-1) and apoptosisinducing factor (AIF). Strikingly, Smh-3 induced apoptosis in HL-60 cells by simultaneously suppressing protein levels of AKT, p-AKT, p-mTOR and p-BAD and inducing BAD protein levels. Taken together, we conclude that Smh-3 acts against leukemia cells in vitro via G 2 /M phase arrest, down-regulation of AKT activity and induction of mitochondrial-dependent apoptotic pathways.

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Section: Discussionsupporting

confidence: 50%

Section: Discussionmentioning

confidence: 98%

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The novel synthesized 2-(3-(methylamino)phenyl)-6-(pyrrolidin-1-yl)quinolin-4-one (Smh-3) compound induces G2/M phase arrest and mitochondrial-dependent apoptotic cell death through inhibition of CDK1 and AKT activity in HL-60 human leukemia cells

et al. 2011

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“…PDGF-mediated tyrosine phosphorylation of the ␦-subunit of ATP synthase has also been reported in other cell types (9). F 0 F 1 -ATPase associates and interacts with protein kinase C ␦ (PKC-␦) in cardiac myocytes and with PKC-␤ in the hippocampus after transient ischemia (21,22). In vitro incubation of F 0 F 1 -ATPase with the recombinant PKC-␦ inhibits F 0 F 1 -ATPase activity (21).…”

mentioning

confidence: 89%

Protein Kinase C-α Interaction with F0F1-ATPase Promotes F0F1-ATPase Activity and Reduces Energy Deficits in Injured Renal Cells

Nowak

Bakajsova

2015

Journal of Biological Chemistry

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“…19,20 PRKCB localization at the mitochondrial level has been known for some time, and this kinase is implicated in the regulation of mitochondrial integrity and oxidative phosphorylation. 21,22 Mitochondria are the primary energy producers of the cell and are recognized as key participants and transducers of several cell death pathways. 23 Moreover, dysfunctions in mitochondrial physiology contribute to the pathophysiology of several disorders.…”

Section: Introductionmentioning

confidence: 99%

PRKCB/protein kinase C, beta and the mitochondrial axis as key regulators of autophagy

et al. 2013

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autophagy is the major intracellular system of degradation, and it plays an essential role in various biological events. Recent observations indicate that autophagy is modulated in response to the energy status of the mitochondrial compartment. however, the exact signaling mechanism that controls autophagy under these conditions remains unclear. in this study, we report that the activation of protein kinase c β (PRKcB), a member of the classical PRKcs, negatively modulates the mitochondrial energy status and inhibits autophagy. Furthermore, cells treated with a pharmacological PRKcB inhibitor, and prkcb knockout MeFs showed an increase in autophagy both in vitro and in vivo, as well as an increased mitochondrial membrane potential (Ψ m ), suggesting a strong involvement of mitochondrial energy in the modulation of the autophagy machinery. Finally, we show that factors that increase the Ψ m oppose the PRKcB-dependent inhibition of autophagy. altogether, these data underscore the importance of PRKcB in the regulation of autophagy; moreover, the finding that a pharmacological modulation of the Ψ m modifies autophagy levels may be useful in fighting pathologies (including various types of cancer and neurodegenerative disorders) that are characterized by reduced levels of autophagy.

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Protein kinase C beta in postischemic brain mitochondria

Cited by 19 publications

References 28 publications

The novel synthesized 2-(3-(methylamino)phenyl)-6-(pyrrolidin-1-yl)quinolin-4-one (Smh-3) compound induces G2/M phase arrest and mitochondrial-dependent apoptotic cell death through inhibition of CDK1 and AKT activity in HL-60 human leukemia cells

The novel synthesized 2-(3-(methylamino)phenyl)-6-(pyrrolidin-1-yl)quinolin-4-one (Smh-3) compound induces G2/M phase arrest and mitochondrial-dependent apoptotic cell death through inhibition of CDK1 and AKT activity in HL-60 human leukemia cells

Protein Kinase C-α Interaction with F0F1-ATPase Promotes F0F1-ATPase Activity and Reduces Energy Deficits in Injured Renal Cells

PRKCB/protein kinase C, beta and the mitochondrial axis as key regulators of autophagy

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