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Article ; Online: Caspase-2 regulates oncogene-induced senescence.

Gitenay, Delphine / Lallet-Daher, Hélène / Bernard, David

2014 Volume 5, Issue 14, Page(s) 5845–5847

Abstract: Cellular senescence is activated by numerous cellular insults, in particular those driving cancer formation, resulting in stable proliferation arrest and acquisition of specific features. By self-opposing to oncogenic stimulation, senescence is ... ...

Abstract	Cellular senescence is activated by numerous cellular insults, in particular those driving cancer formation, resulting in stable proliferation arrest and acquisition of specific features. By self-opposing to oncogenic stimulation, senescence is considered as a failsafe program, allowing, when functional, to inhibit cancers occurrence. Compelling evidences suggest a tumor suppressive activity of caspase-2, eventually independently of its effect on cell death. The original results described here demonstrate that this tumor suppressive activity of caspase-2 is mediated, at least in part, by its pro-senescing activity. Indeed, we have demonstrated in vitro and in vivo that loss of function of caspase-2 allows to escape oncogenic stress induced senescence. These results are discussed in the context of known tumor suppressive activity of caspase-2.
MeSH term(s)	Caspase 2/genetics ; Caspase 2/metabolism ; Cellular Senescence/genetics ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; DNA Damage ; Humans ; Mammary Glands, Human/enzymology ; Oncogenes ; RNA, Small Interfering/administration & dosage ; RNA, Small Interfering/genetics
Chemical Substances	RNA, Small Interfering ; CASP2 protein, human (EC 3.4.22.-) ; Caspase 2 (EC 3.4.22.-) ; Cysteine Endopeptidases (EC 3.4.22.-)
Language	English
Publishing date	2014-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.2286
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Article ; Online: Glucose metabolism and hexosamine pathway regulate oncogene-induced senescence.

Gitenay, D / Wiel, C / Lallet-Daher, H / Vindrieux, D / Aubert, S / Payen, L / Simonnet, H / Bernard, D

Cell death & disease

2014 Volume 5, Page(s) e1089

Abstract: Oncogenic stress-induced senescence (OIS) prevents the ability of oncogenic signals to induce tumorigenesis. It is now largely admitted that the mitogenic effect of oncogenes requires metabolic adaptations to respond to new energetic and bio constituent ... ...

Abstract	Oncogenic stress-induced senescence (OIS) prevents the ability of oncogenic signals to induce tumorigenesis. It is now largely admitted that the mitogenic effect of oncogenes requires metabolic adaptations to respond to new energetic and bio constituent needs. Yet, whether glucose metabolism affects OIS response is largely unknown. This is largely because of the fact that most of the OIS cellular models are cultivated in glucose excess. In this study, we used human epithelial cells, cultivated without glucose excess, to study alteration and functional role of glucose metabolism during OIS. We report a slowdown of glucose uptake and metabolism during OIS. Increasing glucose metabolism by expressing hexokinase2 (HK2), which converts glucose to glucose-6-phosphate (G6P), favors escape from OIS. Inversely, expressing a glucose-6-phosphatase, [corrected] pharmacological inhibition of HK2, or adding nonmetabolizable glucose induced a premature senescence. Manipulations of various metabolites covering G6P downstream pathways (hexosamine, glycolysis, and pentose phosphate pathways) suggest an unexpected role of the hexosamine pathway in controlling OIS. Altogether, our results show that decreased glucose metabolism occurs during and participates to OIS.
MeSH term(s)	Cells, Cultured ; Cellular Senescence/drug effects ; Energy Metabolism/drug effects ; Enzyme Inhibitors/pharmacology ; Epithelial Cells/drug effects ; Epithelial Cells/metabolism ; Epithelial Cells/pathology ; Female ; Glucose/metabolism ; Glucose-6-Phosphate/metabolism ; Glycolysis ; Hexokinase/antagonists & inhibitors ; Hexokinase/genetics ; Hexokinase/metabolism ; Hexosamines/metabolism ; Humans ; Kinetics ; Mammary Glands, Human/drug effects ; Mammary Glands, Human/metabolism ; Mammary Glands, Human/pathology ; Oncogenes ; Pentose Phosphate Pathway ; Time Factors ; Transfection
Chemical Substances	Enzyme Inhibitors ; Hexosamines ; Glucose-6-Phosphate (56-73-5) ; Hexokinase (EC 2.7.1.1) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2014-02-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/cddis.2014.63
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Article ; Online: Endoplasmic reticulum calcium release through ITPR2 channels leads to mitochondrial calcium accumulation and senescence.

Wiel, Clotilde / Lallet-Daher, Hélène / Gitenay, Delphine / Gras, Baptiste / Le Calvé, Benjamin / Augert, Arnaud / Ferrand, Mylène / Prevarskaya, Natalia / Simonnet, Hélène / Vindrieux, David / Bernard, David

Nature communications

2014 Volume 5, Page(s) 3792

Abstract: Senescence is involved in various pathophysiological conditions. Besides loss of retinoblastoma and p53 pathways, little is known about other pathways involved in senescence. Here we identify two calcium channels; inositol 1,4,5-trisphosphate receptor, ... ...

Abstract	Senescence is involved in various pathophysiological conditions. Besides loss of retinoblastoma and p53 pathways, little is known about other pathways involved in senescence. Here we identify two calcium channels; inositol 1,4,5-trisphosphate receptor, type 2 (ITPR2) (also known as inositol 1,4,5-triphosphate receptor 2 (IP3R2)) and mitochondrial calcium uniporter (MCU) as new senescence regulators in a loss-of-function genetic screen. We show that loss of ITPR2, known to mediate endoplasmic reticulum (ER) calcium release, as well as loss of MCU, necessary for mitochondrial calcium uptake, enable escape from oncogene-induced senescence (OIS). During OIS, ITPR2 triggers calcium release from the ER, followed by mitochondrial calcium accumulation through MCU channels. Mitochondrial calcium accumulation leads to a subsequent decrease in mitochondrial membrane potential, reactive oxygen species accumulation and senescence. This ER-mitochondria calcium transport is not restricted to OIS, but is also involved in replicative senescence. Our results show a functional role of calcium release by the ITPR2 channel and its subsequent accumulation in the mitochondria.
MeSH term(s)	Calcium/metabolism ; Cellular Senescence ; Endoplasmic Reticulum/metabolism ; Humans ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Membrane Potential, Mitochondrial ; Mitochondria/metabolism ; Oncogenes ; Oxidative Stress
Chemical Substances	ITPR2 protein, human ; Inositol 1,4,5-Trisphosphate Receptors ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2014-05-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms4792
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Article ; Online: Lysyl oxidase activity regulates oncogenic stress response and tumorigenesis.

Wiel, C / Augert, A / Vincent, D F / Gitenay, D / Vindrieux, D / Le Calvé, B / Arfi, V / Lallet-Daher, H / Reynaud, C / Treilleux, I / Bartholin, L / Lelievre, E / Bernard, D

Cell death & disease

2013 Volume 4, Page(s) e855

Abstract: Cellular senescence, a stable proliferation arrest, is induced in response to various stresses. Oncogenic stress-induced senescence (OIS) results in blocked proliferation and constitutes a fail-safe program counteracting tumorigenesis. The events that ... ...

Abstract	Cellular senescence, a stable proliferation arrest, is induced in response to various stresses. Oncogenic stress-induced senescence (OIS) results in blocked proliferation and constitutes a fail-safe program counteracting tumorigenesis. The events that enable a tumor in a benign senescent state to escape from OIS and become malignant are largely unknown. We show that lysyl oxidase activity contributes to the decision to maintain senescence. Indeed, in human epithelial cell the constitutive expression of the LOX or LOXL2 protein favored OIS escape, whereas inhibition of lysyl oxidase activity was found to stabilize OIS. The relevance of these in vitro observations is supported by in vivo findings: in a transgenic mouse model of aggressive pancreatic ductal adenocarcinoma (PDAC), increasing lysyl oxidase activity accelerates senescence escape, whereas inhibition of lysyl oxidase activity was found to stabilize senescence, delay tumorigenesis, and increase survival. Mechanistically, we show that lysyl oxidase activity favors the escape of senescence by regulating the focal-adhesion kinase. Altogether, our results demonstrate that lysyl oxidase activity participates in primary tumor growth by directly impacting the senescence stability.
MeSH term(s)	Adenocarcinoma/enzymology ; Adenocarcinoma/pathology ; Animals ; Biocatalysis/drug effects ; Carcinogenesis/metabolism ; Carcinogenesis/pathology ; Carcinoma, Pancreatic Ductal/enzymology ; Carcinoma, Pancreatic Ductal/pathology ; Cellular Senescence/drug effects ; Enzyme Activation/drug effects ; Enzyme Inhibitors/pharmacology ; Epithelial Cells/drug effects ; Epithelial Cells/enzymology ; Epithelial Cells/pathology ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; Humans ; Mice ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Models, Biological ; Neoplasms/enzymology ; Neoplasms/pathology ; Protein-Lysine 6-Oxidase/antagonists & inhibitors ; Protein-Lysine 6-Oxidase/metabolism ; Stress, Physiological/drug effects
Chemical Substances	Enzyme Inhibitors ; Protein-Lysine 6-Oxidase (EC 1.4.3.13) ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2)
Language	English
Publishing date	2013-10-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/cddis.2013.382
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Article ; Online: Potassium channel KCNA1 modulates oncogene-induced senescence and transformation.

Lallet-Daher, Hélène / Wiel, Clotilde / Gitenay, Delphine / Navaratnam, Naveenan / Augert, Arnaud / Le Calvé, Benjamin / Verbeke, Stéphanie / Carling, David / Aubert, Sébastien / Vindrieux, David / Bernard, David

Cancer research

2013 Volume 73, Issue 16, Page(s) 5253–5265

Abstract: Oncogene-induced senescence (OIS) constitutes a failsafe program that restricts tumor development. However, the mechanisms that link oncogenesis to senescence are not completely understood. We carried out a loss-of-function genetic screen that identified ...

Abstract	Oncogene-induced senescence (OIS) constitutes a failsafe program that restricts tumor development. However, the mechanisms that link oncogenesis to senescence are not completely understood. We carried out a loss-of-function genetic screen that identified the potassium channel KCNA1 as a determinant of OIS escape that can license tumor growth. Oncogenic stress triggers an increase in KCNA1 expression and its relocation from the cytoplasm to the membrane. Mechanistically, this relocation is due to a loss of protein kinase A (PKA)-induced phosphorylation at residue S446 of KCNA1. Accordingly, sustaining PKA activity or expressing a KCNA1 phosphomimetic mutant maintained KCNA1 in the cytoplasm and caused escape from OIS. KCNA1 relocation to the membrane induced a change in membrane potential that invariably resulted in cellular senescence. Restoring KCNA1 expression in transformation-competent cells triggered variation in membrane potential and blocked RAS-induced transformation, and PKA activation suppressed both effects. Furthermore, KCNA1 expression was reduced in human cancers, and this decrease correlated with an increase in breast cancer aggressiveness. Taken together, our results identify a novel pathway that restricts oncogenesis through a potassium channel-dependent senescence pathway.
MeSH term(s)	Animals ; Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Growth Processes/physiology ; Cell Line ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cell Transformation, Neoplastic/genetics ; Cellular Senescence/genetics ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytoplasm/genetics ; Cytoplasm/metabolism ; Down-Regulation ; Humans ; Kv1.1 Potassium Channel/genetics ; Kv1.1 Potassium Channel/metabolism ; Mammary Glands, Human/metabolism ; Mammary Glands, Human/pathology ; Membrane Potentials/genetics ; Mice ; NIH 3T3 Cells ; Phosphorylation/genetics ; Signal Transduction/genetics
Chemical Substances	Kv1.1 Potassium Channel (147173-20-4) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
Language	English
Publishing date	2013-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-12-3690
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Article ; Online: PLA2R1 mediates tumor suppression by activating JAK2.

Vindrieux, David / Augert, Arnaud / Girard, Christophe A / Gitenay, Delphine / Lallet-Daher, Helene / Wiel, Clotilde / Le Calvé, Benjamin / Gras, Baptiste / Ferrand, Mylène / Verbeke, Stéphanie / de Launoit, Yvan / Leroy, Xavier / Puisieux, Alain / Aubert, Sébastien / Perrais, Michael / Gelb, Michael / Simonnet, Hélène / Lambeau, Gérard / Bernard, David

Cancer research

2013 Volume 73, Issue 20, Page(s) 6334–6345

Abstract: Little is known about the physiological role of the phospholipase A2 receptor (PLA2R1). PLA2R1 has been described as regulating the replicative senescence, a telomerase-dependent proliferation arrest. The downstream PLA2R1 signaling and its role in ... ...

Abstract	Little is known about the physiological role of the phospholipase A2 receptor (PLA2R1). PLA2R1 has been described as regulating the replicative senescence, a telomerase-dependent proliferation arrest. The downstream PLA2R1 signaling and its role in cancer are currently unknown. Senescence induction in response to activated oncogenes is a failsafe program of tumor suppression that must be bypassed for tumorigenesis. We now present evidence that PLA2R1 functions in vitro as a tumor suppressor, the depletion of which is sufficient to escape oncogene-induced senescence (OIS), thereby facilitating oncogenic cell transformation. Furthermore, mice that are genetically deficient in PLA2R1 display increased sensitivity to RAS-induced tumorigenesis by facilitating OIS escape, highlighting its physiological role as a tumor suppressor. Unexpectedly, PLA2R1 activated JAK2 and its effector signaling, with PLA2R1-mediated inhibition of cell transformation largely reverted in JAK2-depleted cells. This finding was unexpected as the JAK2 pathway has been associated mainly with protumoral functions and several inhibitors are currently in clinical trials. Taken together, our findings uncover an unanticipated tumor suppressive role for PLA2R1 that is mediated by targeting downstream JAK2 effector signaling.
MeSH term(s)	Animals ; Cell Culture Techniques ; Cell Growth Processes/physiology ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/metabolism ; Cellular Senescence/genetics ; Cellular Senescence/physiology ; Enzyme Activation ; Humans ; Immunohistochemistry ; Janus Kinase 2/genetics ; Janus Kinase 2/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; NIH 3T3 Cells ; Receptors, Phospholipase A2/genetics ; Receptors, Phospholipase A2/metabolism ; Skin Neoplasms/enzymology ; Skin Neoplasms/genetics ; Skin Neoplasms/pathology ; Transfection
Chemical Substances	PLA2R1 protein, human ; Pla2r1 protein, mouse ; Receptors, Phospholipase A2 ; Janus Kinase 2 (EC 2.7.10.2)
Language	English
Publishing date	2013-09-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-13-0318
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Article ; Online: Intermediate-conductance Ca2+-activated K+ channels (IKCa1) regulate human prostate cancer cell proliferation through a close control of calcium entry.

Lallet-Daher, H / Roudbaraki, M / Bavencoffe, A / Mariot, P / Gackière, F / Bidaux, G / Urbain, R / Gosset, P / Delcourt, P / Fleurisse, L / Slomianny, C / Dewailly, E / Mauroy, B / Bonnal, J L / Skryma, R / Prevarskaya, N

Oncogene

2009 Volume 28, Issue 15, Page(s) 1792–1806

Abstract: Accumulating data point to K(+) channels as relevant players in controlling cell cycle progression and proliferation of human cancer cells, including prostate cancer (PCa) cells. However, the mechanism(s) by which K(+) channels control PCa cell ... ...

Abstract	Accumulating data point to K(+) channels as relevant players in controlling cell cycle progression and proliferation of human cancer cells, including prostate cancer (PCa) cells. However, the mechanism(s) by which K(+) channels control PCa cell proliferation remain illusive. In this study, using the techniques of molecular biology, biochemistry, electrophysiology and calcium imaging, we studied the expression and functionality of intermediate-conductance calcium-activated potassium channels (IK(Ca1)) in human PCa as well as their involvement in cell proliferation. We showed that IK(Ca1) mRNA and protein were preferentially expressed in human PCa tissues, and inhibition of the IK(Ca1) potassium channel suppressed PCa cell proliferation. The activation of IK(Ca1) hyperpolarizes membrane potential and, by promoting the driving force for calcium, induces calcium entry through TRPV6, a cation channel of the TRP (Transient Receptor Potential) family. Thus, the overexpression of the IK(Ca1) channel is likely to promote carcinogenesis in human prostate tissue.
MeSH term(s)	Benzimidazoles/pharmacology ; Calcium/metabolism ; Calcium Channels/physiology ; Cell Line, Tumor ; Cell Proliferation ; Cyclin-Dependent Kinase Inhibitor p21/analysis ; Cyclin-Dependent Kinase Inhibitor p21/genetics ; Cyclin-Dependent Kinase Inhibitor p27 ; G1 Phase ; Humans ; Intermediate-Conductance Calcium-Activated Potassium Channels/analysis ; Intermediate-Conductance Calcium-Activated Potassium Channels/physiology ; Intracellular Signaling Peptides and Proteins/analysis ; Male ; Membrane Potentials ; Prostatic Neoplasms/metabolism ; Prostatic Neoplasms/pathology ; RNA, Messenger/analysis ; S100 Proteins/analysis ; TRPV Cation Channels/physiology ; Tumor Suppressor Protein p53/physiology
Chemical Substances	Benzimidazoles ; CDKN1A protein, human ; CDKN1B protein, human ; Calcium Channels ; Cyclin-Dependent Kinase Inhibitor p21 ; Intermediate-Conductance Calcium-Activated Potassium Channels ; Intracellular Signaling Peptides and Proteins ; RNA, Messenger ; S100 Proteins ; TRPV Cation Channels ; TRPV6 protein, human ; Tumor Suppressor Protein p53 ; Cyclin-Dependent Kinase Inhibitor p27 (147604-94-2) ; 1-ethyl-2-benzimidazolinone (M82W79SS4W) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2009-04-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/onc.2009.25
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Article: Identification of a novel antigen of Schistosoma mansoni shared with Plasmodium falciparum and evaluation of different cross-reactive antibody subclasses induced by human schistosomiasis and malaria.

Pierrot, Christine / Wilson, Shona / Lallet, Hélène / Lafitte, Sophia / Jones, Frances M / Daher, Wassim / Capron, Monique / Dunne, David W / Khalife, Jamal

Infection and immunity

2006 Volume 74, Issue 6, Page(s) 3347–3354

Abstract: Plasmodium falciparum and Schistosoma mansoni are often found in human coinfections, and cross-reactive antibodies to different components of the two parasites have been detected. In this work, we identified a cross-reactive S. mansoni gene product, ... ...

Abstract	Plasmodium falciparum and Schistosoma mansoni are often found in human coinfections, and cross-reactive antibodies to different components of the two parasites have been detected. In this work, we identified a cross-reactive S. mansoni gene product, referred to as SmLRR, that seems to belong to the leucine-rich repeat protein family. Comparative analysis of SmLRR revealed 57% similarity with a putative gene product encoded in the P. falciparum genome. Antibodies to SmLRR were found in experimental infections and in both S. mansoni- and P. falciparum-infected individuals. Correlative analysis of human anti-SmLRR responses in Kenya and Uganda suggested that malaria and schistosomiasis drive the immunoglobulin G3 (IgG3) and IgG4 isotypes, respectively, against SmLRR, suggesting that there is differential regulation of cross-reactive isotypes depending on the infection. In addition, the levels of anti-SmLRR IgG4, but not the levels of IgG3, correlated positively with the intensity of S. mansoni infection.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Helminth/blood ; Antibodies, Protozoan/blood ; Antigens, Helminth/chemistry ; Antigens, Helminth/immunology ; Cross Reactions ; Humans ; Immunoglobulin G/classification ; Malaria, Falciparum/immunology ; Molecular Sequence Data ; Plasmodium falciparum/immunology ; Schistosoma mansoni/immunology ; Schistosomiasis mansoni/immunology
Chemical Substances	Antibodies, Helminth ; Antibodies, Protozoan ; Antigens, Helminth ; Immunoglobulin G
Language	English
Publishing date	2006-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.01724-05
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Article ; Online: Caspase-2 regulates oncogene-induced senescence.

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Article ; Online: Glucose metabolism and hexosamine pathway regulate oncogene-induced senescence.

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Article ; Online: Endoplasmic reticulum calcium release through ITPR2 channels leads to mitochondrial calcium accumulation and senescence.

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Article ; Online: Lysyl oxidase activity regulates oncogenic stress response and tumorigenesis.

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Article ; Online: Potassium channel KCNA1 modulates oncogene-induced senescence and transformation.

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Article ; Online: PLA2R1 mediates tumor suppression by activating JAK2.

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Article ; Online: Intermediate-conductance Ca2+-activated K+ channels (IKCa1) regulate human prostate cancer cell proliferation through a close control of calcium entry.

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Article: Identification of a novel antigen of Schistosoma mansoni shared with Plasmodium falciparum and evaluation of different cross-reactive antibody subclasses induced by human schistosomiasis and malaria.

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