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Article ; Online: Repurposing Two Old Friends to Fight Cancer: Caffeine and Statins.

Stouth, Derek W / Lebeau, Paul F / Austin, Richard C

2023 Volume 83, Issue 13, Page(s) 2091–2092

Abstract: Statins are a class of cholesterol-lowering drugs that inhibit 3-hydroxy-3-methylglutaryl-CoA reductase, the rate-limiting enzyme of the mevalonate pathway. Evidence suggests that certain cancers depend on the mevalonate pathway for growth and survival, ... ...

Abstract	Statins are a class of cholesterol-lowering drugs that inhibit 3-hydroxy-3-methylglutaryl-CoA reductase, the rate-limiting enzyme of the mevalonate pathway. Evidence suggests that certain cancers depend on the mevalonate pathway for growth and survival, and thus blocking the mevalonate pathway with statins may offer a viable therapeutic approach for treating cancer, or at least enhance the efficacy of existing cancer drugs. In this issue of Cancer Research, Tran and colleagues showed that caffeine works jointly with FOXM1 inhibition to enhance the antitumor activity of statins in neuroblastoma cells. They found that caffeine synergizes with statins by suppressing statin-induced feedback activation of the mevalonate pathway. Here, we reflect on the potential of combining caffeine and statin drugs as a strategy for potentiating anticancer activity. See related article by Tran et al., p. 2248.
MeSH term(s)	Humans ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/pharmacology ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/therapeutic use ; Caffeine/pharmacology ; Mevalonic Acid/metabolism ; Drug Repositioning ; Friends ; Neuroblastoma/drug therapy ; Dietary Supplements ; Forkhead Box Protein M1
Chemical Substances	Hydroxymethylglutaryl-CoA Reductase Inhibitors ; Caffeine (3G6A5W338E) ; Mevalonic Acid (S5UOB36OCZ) ; FOXM1 protein, human ; Forkhead Box Protein M1
Language	English
Publishing date	2023-07-05
Publishing country	United States
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-23-1066
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Article ; Online: Calcium as a reliable marker for the quantitative assessment of endoplasmic reticulum stress in live cells.

Lebeau, Paul F / Platko, Khrystyna / Byun, Jae Hyun / Austin, Richard C

The Journal of biological chemistry

2021 Volume 296, Page(s) 100779

Abstract: ... Calcium ( ... ...

Abstract	Calcium (Ca
MeSH term(s)	Calcium/analysis ; Calcium/metabolism ; Cell Line ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress ; HEK293 Cells ; Hep G2 Cells ; Humans ; Microscopy, Fluorescence ; Unfolded Protein Response
Chemical Substances	Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-05-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100779
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Article: The Emerging Roles of Intracellular PCSK9 and Their Implications in Endoplasmic Reticulum Stress and Metabolic Diseases.

Lebeau, Paul F / Platko, Khrystyna / Byun, Jae Hyun / Makda, Yumna / Austin, Richard C

Metabolites

2022 Volume 12, Issue 3

Abstract: The importance of the proprotein convertase subtilisin/kexin type-9 ( ...

Abstract	The importance of the proprotein convertase subtilisin/kexin type-9 (
Language	English
Publishing date	2022-02-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2662251-8
ISSN	2218-1989
ISSN	2218-1989
DOI	10.3390/metabo12030215
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Book: Hommage à Paul Lebeau

Lebeau, Paul

Fac. de Pharmacie de Paris, 28. Nov. 1957

(Annales pharmaceutiques Françaises ; 16,3, Suppl.)

1958

Series title	Annales pharmaceutiques Françaises ; 16,3, Suppl. Annales pharmaceutiques françaises
Collection	Annales pharmaceutiques françaises
Language	French
Size	19 S. ; 8-o
Publisher	Masson
Publishing place	Paris
Publishing country	France
Document type	Book
Note	[Umschl.T.]
HBZ-ID	HT009028919
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: MAPping the kinase landscape of macrophage activation.

Platko, Khrystyna / Lebeau, Paul / Austin, Richard C

The Journal of biological chemistry

2018 Volume 293, Issue 25, Page(s) 9910–9911

Abstract: ARL11 is a tumor suppressor gene with established pro-apoptotic properties, but its function beyond this role is poorly understood. A new analysis of macrophage activation has identified ARL11 as a novel regulator of a mitogen-activated protein kinase ( ... ...

Abstract	ARL11 is a tumor suppressor gene with established pro-apoptotic properties, but its function beyond this role is poorly understood. A new analysis of macrophage activation has identified ARL11 as a novel regulator of a mitogen-activated protein kinase (MAPK). These findings expand on the function of ARL11 beyond its tumor suppressor activity and highlight a novel role as a regulator of macrophage activation and inflammatory response.
MeSH term(s)	ADP-Ribosylation Factors/genetics ; ADP-Ribosylation Factors/metabolism ; Extracellular Signal-Regulated MAP Kinases/genetics ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; Lipopolysaccharides/pharmacology ; Macrophage Activation/drug effects ; Macrophages/drug effects ; Macrophages/enzymology ; Phosphorylation ; Signal Transduction ; p38 Mitogen-Activated Protein Kinases/genetics ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Lipopolysaccharides ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; ADP-Ribosylation Factors (EC 3.6.5.2) ; ARL11 protein, human (EC 3.6.5.2)
Language	English
Publishing date	2018-06-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.H118.003380
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Article ; Online: A Metabolic Enhancer Protects against Diet-Induced Obesity and Liver Steatosis and Corrects a Pro-Atherogenic Serum Profile in Mice.

Platko, Khrystyna / Lebeau, Paul F / Nederveen, Joshua P / Byun, Jae Hyun / MacDonald, Melissa E / Bourgeois, Jacqueline M / Tarnopolsky, Mark A / Austin, Richard C

Nutrients

2023 Volume 15, Issue 10

Abstract: Objective: Metabolic Syndrome (MetS) affects hundreds of millions of individuals and constitutes a major cause of morbidity and mortality worldwide. Obesity is believed to be at the core of metabolic abnormalities associated with MetS, including ... ...

Abstract	Objective: Metabolic Syndrome (MetS) affects hundreds of millions of individuals and constitutes a major cause of morbidity and mortality worldwide. Obesity is believed to be at the core of metabolic abnormalities associated with MetS, including dyslipidemia, insulin resistance, fatty liver disease and vascular dysfunction. Although previous studies demonstrate a diverse array of naturally occurring antioxidants that attenuate several manifestations of MetS, little is known about the (i) combined effect of these compounds on hepatic health and (ii) molecular mechanisms responsible for their effect. Methods: We explored the impact of a metabolic enhancer (ME), consisting of 7 naturally occurring antioxidants and mitochondrial enhancing agents, on diet-induced obesity, hepatic steatosis and atherogenic serum profile in mice. Results: Here we show that a diet-based ME supplementation and exercise have similar beneficial effects on adiposity and hepatic steatosis in mice. Mechanistically, ME reduced hepatic ER stress, fibrosis, apoptosis, and inflammation, thereby improving overall liver health. Furthermore, we demonstrated that ME improved HFD-induced pro-atherogenic serum profile in mice, similar to exercise. The protective effects of ME were reduced in proprotein convertase subtilisin/kexin 9 (PCSK9) knock out mice, suggesting that ME exerts it protective effect partly in a PCSK9-dependent manner. Conclusions: Our findings suggest that components of the ME have a positive, protective effect on obesity, hepatic steatosis and cardiovascular risk and that they show similar effects as exercise training.
MeSH term(s)	Mice ; Animals ; Proprotein Convertase 9/metabolism ; Antioxidants/metabolism ; Diet, High-Fat/adverse effects ; Obesity/metabolism ; Liver/metabolism ; Metabolic Syndrome/etiology ; Metabolic Syndrome/prevention & control ; Metabolic Syndrome/metabolism ; Non-alcoholic Fatty Liver Disease/etiology ; Non-alcoholic Fatty Liver Disease/prevention & control ; Non-alcoholic Fatty Liver Disease/metabolism ; Insulin Resistance ; Mice, Inbred C57BL
Chemical Substances	PCSK9 protein, human (EC 3.4.21.-) ; Proprotein Convertase 9 (EC 3.4.21.-) ; Antioxidants
Language	English
Publishing date	2023-05-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu15102410
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Article: The trypan blue cellular debris assay: a novel low-cost method for the rapid quantification of cell death

Lebeau, Paul F / Chen, Jack / Byun, Jae Hyun / Platko, Khrystyna / Austin, Richard C

MethodsX. 2019, v. 6

2019

Abstract: Cell death is a common driver of human disease and is frequently studied in a variety of in vitro settings. There currently exists a range of commercially available assays to examine cell death, however, most are costly and require assay-specific ... ...

Abstract	Cell death is a common driver of human disease and is frequently studied in a variety of in vitro settings. There currently exists a range of commercially available assays to examine cell death, however, most are costly and require assay-specific experimental conditions that may not be suitable for many cell types. Here, we show that cellular debris occurring as a result of cell death can be used to quantify cell death using trypan blue. Furthermore, we demonstrate that the data generated using this technique are comparable to the widely-used lactate dehydrogenase (LDH) assay. Overall, we describe a novel application for trypan blue, a stain found in most biology laboratories, as a novel and cost-effective method for the quantification of cell death via staining of cell debris.
Keywords	cell death ; cost effectiveness ; human diseases ; lactate dehydrogenase ; staining
Language	English
Size	p. 1174-1180.
Publishing place	Elsevier B.V.
Document type	Article
ISSN	2215-0161
DOI	10.1016/j.mex.2019.05.010
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Pharmacologic inhibition of S1P attenuates ATF6 expression, causes ER stress and contributes to apoptotic cell death.

Lebeau, Paul / Byun, Jae Hyun / Yousof, Tamana / Austin, Richard C

Toxicology and applied pharmacology

2018 Volume 349, Page(s) 1–7

Abstract: Mammalian cells express unique transcription factors embedded in the endoplasmic reticulum (ER) membrane, such as the sterol regulatory element-binding proteins (SREBPs), that promote de novo lipogenesis. Upon their release from the ER, the SREBPs ... ...

Abstract	Mammalian cells express unique transcription factors embedded in the endoplasmic reticulum (ER) membrane, such as the sterol regulatory element-binding proteins (SREBPs), that promote de novo lipogenesis. Upon their release from the ER, the SREBPs require proteolytic activation in the Golgi by site-1-protease (S1P). As such, inhibition of S1P, using compounds such as PF-429242 (PF), reduces cholesterol synthesis and may represent a new strategy for the management of dyslipidemia. In addition to the SREBPs, the unfolded protein response (UPR) transducer, known as the activating transcription factor 6 (ATF6), is another ER membrane-bound transcription factor that requires S1P-mediated activation. ATF6 regulates ER protein folding capacity by promoting the expression of ER chaperones such as the 78-kDa glucose-regulated protein (GRP78). ER-resident chaperones like GRP78 prevent and/or resolve ER polypeptide accumulation and subsequent ER stress-induced UPR activation by folding nascent polypeptides. Here we report that pharmacological inhibition of S1P reduced the expression of ATF6 and GRP78 and induced the activation of UPR transducers inositol-requiring enzyme-1α (IRE1α) and protein kinase RNA-like ER kinase (PERK). As a consequence, S1P inhibition also increased the susceptibility of cells to ER stress-induced cell death. Our findings suggest that S1P plays a crucial role in the regulation of ER folding capacity and also identifies a compensatory cross-talk between UPR transducers in order to maintain adequate ER chaperone expression and activity.
MeSH term(s)	Activating Transcription Factor 6/antagonists & inhibitors ; Activating Transcription Factor 6/biosynthesis ; Animals ; Apoptosis/drug effects ; Apoptosis/genetics ; Cell Line ; Endoplasmic Reticulum Chaperone BiP ; Endoplasmic Reticulum Stress/drug effects ; Endoplasmic Reticulum Stress/genetics ; Endoribonucleases/antagonists & inhibitors ; Endoribonucleases/metabolism ; Enzyme Activation/drug effects ; Heat-Shock Proteins/biosynthesis ; Hepatocytes/drug effects ; Humans ; Mice ; Mice, Inbred C57BL ; Molecular Chaperones/biosynthesis ; Protein Serine-Threonine Kinases/antagonists & inhibitors ; Protein Serine-Threonine Kinases/metabolism ; Reactive Oxygen Species ; Sp1 Transcription Factor/antagonists & inhibitors ; Unfolded Protein Response/drug effects ; eIF-2 Kinase/antagonists & inhibitors ; eIF-2 Kinase/metabolism
Chemical Substances	ATF6 protein, human ; Activating Transcription Factor 6 ; Endoplasmic Reticulum Chaperone BiP ; HSPA5 protein, human ; Heat-Shock Proteins ; Hspa5 protein, mouse ; Molecular Chaperones ; Reactive Oxygen Species ; Sp1 Transcription Factor ; SP1 protein, human ; EIF2AK3 protein, human (EC 2.7.11.1) ; ERN1 protein, human (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; eIF-2 Kinase (EC 2.7.11.1) ; Endoribonucleases (EC 3.1.-)
Language	English
Publishing date	2018-04-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	204477-8
ISSN	1096-0333 ; 0041-008X
ISSN (online)	1096-0333
ISSN	0041-008X
DOI	10.1016/j.taap.2018.04.020
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Article: The trypan blue cellular debris assay: a novel low-cost method for the rapid quantification of cell death.

Lebeau, Paul F / Chen, Jack / Byun, Jae Hyun / Platko, Khrystyna / Austin, Richard C

MethodsX

2019 Volume 6, Page(s) 1174–1180

Abstract: Cell death is a common driver of human disease and is frequently studied in a variety ... ...

Abstract	Cell death is a common driver of human disease and is frequently studied in a variety of
Language	English
Publishing date	2019-05-15
Publishing country	Netherlands
Document type	Journal Article
ISSN	2215-0161
ISSN	2215-0161
DOI	10.1016/j.mex.2019.05.010
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Article ; Online: Diet-induced hepatic steatosis abrogates cell-surface LDLR by inducing

Lebeau, Paul F / Byun, Jae Hyun / Platko, Khrystyna / MacDonald, Melissa E / Poon, Samantha V / Faiyaz, Mahi / Seidah, Nabil G / Austin, Richard C

The Journal of biological chemistry

2019 Volume 294, Issue 23, Page(s) 9037–9047

Abstract: The worldwide prevalence of non-alcoholic fatty liver disease (NAFLD) is increasing rapidly. Although this condition is generally benign, accumulating evidence now suggests that patients with NAFLD are also at increased risk of cardiovascular disease ( ... ...

Abstract	The worldwide prevalence of non-alcoholic fatty liver disease (NAFLD) is increasing rapidly. Although this condition is generally benign, accumulating evidence now suggests that patients with NAFLD are also at increased risk of cardiovascular disease (CVD); the leading cause of death in developed nations. Despite the well-established role of the liver as a central regulator of circulating low-density lipoprotein (LDL) cholesterol levels, a known driver of CVD, the mechanism(s) by which hepatic steatosis contributes to CVD remains elusive. Interestingly, a recent study has shown that circulating proprotein convertase subtilisin/kexin type 9 (PCSK9) levels correlate positively with liver steatosis grade. Given that PCSK9 degrades the LDL receptor (LDLR) and prevents the removal of LDL from the blood into the liver, in the present study we examined the effect of hepatic steatosis on LDLR expression and circulating LDL cholesterol levels. We now report that in a manner consistent with findings in patients, diet-induced steatosis increases circulating PCSK9 levels as a result of
MeSH term(s)	Animals ; Apolipoproteins B/blood ; Cholesterol, LDL/blood ; Diet, High-Fat ; Endoplasmic Reticulum Stress/drug effects ; Fatty Liver/metabolism ; Fatty Liver/pathology ; Hep G2 Cells ; Humans ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Organophosphorus Compounds/pharmacology ; Proprotein Convertase 9/blood ; Proprotein Convertase 9/genetics ; Proprotein Convertase 9/metabolism ; Receptors, LDL/genetics ; Receptors, LDL/metabolism ; Sterol Regulatory Element Binding Protein 2/genetics ; Sterol Regulatory Element Binding Protein 2/metabolism
Chemical Substances	Apolipoproteins B ; Cholesterol, LDL ; Organophosphorus Compounds ; Receptors, LDL ; Sterol Regulatory Element Binding Protein 2 ; N-hydroxy-4-phosphonobutanamide (146086-80-8) ; Pcsk9 protein, mouse (EC 3.4.21.-) ; Proprotein Convertase 9 (EC 3.4.21.-)
Language	English
Publishing date	2019-04-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.008094
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