Overexpression of Protein Kinase C-η Attenuates Caspase Activation and Tumor Necrosis Factor-α-Induced Cell Death

Akkaraju, Giridhar R.; Basu, Alakananda

doi:10.1006/bbrc.2000.3903

Cited by 35 publications

(24 citation statements)

References 29 publications

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“…We have previously shown that PKC activators caused induction of nPKC in MCF-7 cells and that upregulation of nPKC correlated with the ability of PKC activators to protect cells against TNF cytotoxicity (25). Furthermore, overexpression of nPKC in MCF-7 cells attenuated caspase activation and TNF-induced cell death (20). We have found that cells that contained little nPKC were, however, resistant to TNF.…”

Section: Discussionmentioning

confidence: 76%

“…It is conceivable that BIM can induce activation of another caspase or a protease, which further degrades the catalytic fragments. Since nPKC, which was not a substrate for caspase-3 also blocked caspase activation and TNF-induced cell death (20) and BIM induced downregulation of nPKC, we speculate that novel PKC isozymes negatively regulates TNF induced cell death and that depletion of these isozymes either by downregulation or by proteolytic cleavage enhanced cell death by TNF.…”

Section: Discussionmentioning

confidence: 87%

“…MCF-7 cells, however, do not express functional caspase-3 but do respond to PKC inhibitor-mediated sensitization to TNF (19). We have recently shown that overexpression of novel PKC attenuates TNF-induced cell death in MCF-7 cells (20). In the present study, we have compared several breast cancer cell lines to determine if there is any association between PKC isozyme expression and sensitivity of breast cancer cells to TNF.…”

mentioning

confidence: 88%

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Differential Sensitivity of Breast Cancer Cells to Tumor Necrosis Factor-α: Involvement of Protein Kinase C

Basu

Mohanty

Sun

2001

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 76%

Section: Discussionmentioning

confidence: 87%

mentioning

confidence: 88%

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Differential Sensitivity of Breast Cancer Cells to Tumor Necrosis Factor-α: Involvement of Protein Kinase C

Basu

Mohanty

Sun

2001

Biochemical and Biophysical Research Communications

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“…PKC -mediated inhibition of proapoptotic JNK activity protects breast cancer cells from chemotherapy and irradiation therapy [71]. In addition, overexpression of PKC delays TNF-induced cell death in MCF-7 cells by reducing the activation of caspase-8 and caspase-7 [72]. In spite of low levels of PKC being found in most invasive breast cancer lesions (75%), invasive cancers containing high PKC are associated with positive lymph node status [73].…”

Section: Pkc Isozymes and Cancermentioning

confidence: 99%

Protein Kinase C (PKC) Isozymes and Cancer

Kang

2014

New Journal of Science

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Protein kinase C (PKC) is a family of phospholipid-dependent serine/threonine kinases, which can be further classified into three PKC isozymes subfamilies: conventional or classic, novel or nonclassic, and atypical. PKC isozymes are known to be involved in cell proliferation, survival, invasion, migration, apoptosis, angiogenesis, and drug resistance. Because of their key roles in cell signaling, PKC isozymes also have the potential to be promising therapeutic targets for several diseases, such as cardiovascular diseases, immune and inflammatory diseases, neurological diseases, metabolic disorders, and multiple types of cancer. This review primarily focuses on the activation, mechanism, and function of PKC isozymes during cancer development and progression.

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“…In some of these studies, the mechanism of action involved modulation of cell cycle components (20,21,30,42,43,61). Recent studies suggest that PKC has a special role in the response to stress and regulation of apoptosis (2,46). It provides protection against apoptosis induced by the chemotherapeutic drugs camptothecin and doxorubicin in Hodgkin's lymphoma lines and breast adenocarcinoma MCF-7 cells (1,59).…”

mentioning

confidence: 99%

Translational Control of Protein Kinase Cη by Two Upstream Open Reading Frames

Raveh-Amit¹,

Maissel²,

Poller³

et al. 2009

Molecular and Cellular Biology

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Protein kinase C (PKC) represents a family of serine/threonine kinases that play a central role in the regulation of cell growth, differentiation, and transformation. Posttranslational control of the PKC isoforms and their activation have been extensively studied; however, not much is known about their translational regulation. Here we report that the expression of one of the PKC isoforms, PKC, is regulated at the translational level both under normal growth conditions and during stress imposed by amino acid starvation, the latter causing a marked increase in its protein levels. The 5 untranslated region (5 UTR) of PKC is unusually long and GC rich, characteristic of many oncogenes and growth regulatory genes. We have identified two conserved upstream open reading frames (uORFs) in its 5 UTR and show their effect in suppressing the expression of PKC in MCF-7 growing cells. While the two uORFs function as repressive elements that maintain low basal levels of PKC in growing cells, they are required for its enhanced expression upon amino acid starvation. We show that the translational regulation during stress involves leaky scanning and is dependent on eIF-2␣ phosphorylation by GCN2. Our work further suggests that translational regulation could provide an additional level for controlling the expression of PKC family members, being more common than currently recognized.Studies over the last several years have focused on the activation of protein kinase C (PKC) members and their regulation by phosphorylation, membrane recruitment, and downregulation by proteolysis; however, not much is known about the regulatory mechanisms leading to PKC synthesis. Most cellular mRNAs have short 5Ј untranslated regions (UTRs

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Overexpression of Protein Kinase C-η Attenuates Caspase Activation and Tumor Necrosis Factor-α-Induced Cell Death

Cited by 35 publications

References 29 publications

Differential Sensitivity of Breast Cancer Cells to Tumor Necrosis Factor-α: Involvement of Protein Kinase C

Differential Sensitivity of Breast Cancer Cells to Tumor Necrosis Factor-α: Involvement of Protein Kinase C

Protein Kinase C (PKC) Isozymes and Cancer

Translational Control of Protein Kinase Cη by Two Upstream Open Reading Frames

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