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Article ; Online: Combined transcriptomics and proteomics unveil the impact of vitamin C in modulating specific protein abundance in the mouse liver.

Aumailley, Lucie / Bodein, Antoine / Adjibade, Pauline / Leclercq, Mickaël / Bourassa, Sylvie / Droit, Arnaud / Mazroui, Rachid / Lebel, Michel

Biological research

2024 Volume 57, Issue 1, Page(s) 26

Abstract: Background: Vitamin C (ascorbate) is a water-soluble antioxidant and an important cofactor for various biosynthetic and regulatory enzymes. Mice can synthesize vitamin C thanks to the key enzyme gulonolactone oxidase (Gulo) unlike humans. In the current ...

Abstract	Background: Vitamin C (ascorbate) is a water-soluble antioxidant and an important cofactor for various biosynthetic and regulatory enzymes. Mice can synthesize vitamin C thanks to the key enzyme gulonolactone oxidase (Gulo) unlike humans. In the current investigation, we used Gulo Results: Principal component analyses revealed distinctive differences in the mRNA and protein profiles as a function of sex between all the mouse cohorts. Despite such sexual dimorphism, Spearman analyses of transcriptomics data from females and males revealed correlations of hepatic ascorbate levels with transcripts encoding a wide array of biological processes involved in glucose and lipid metabolisms as well as in the acute-phase immune response. Moreover, integration of the proteomics data showed that ascorbate modulates the abundance of various enzymes involved in lipid, xenobiotic, organic acid, acetyl-CoA, and steroid metabolism mainly at the transcriptional level, especially in females. However, several proteins of the mitochondrial complex III significantly correlated with ascorbate concentrations in both males and females unlike their corresponding transcripts. Finally, poly(ribo)some profiling did not reveal significant enrichment difference for these mitochondrial complex III mRNAs between Gulo Conclusions: Thus, the abundance of several subunits of the mitochondrial complex III are regulated by ascorbate at the post-transcriptional levels. Our extensive omics analyses provide a novel resource of altered gene expression patterns at the transcriptional and post-transcriptional levels under ascorbate deficiency.
MeSH term(s)	Animals ; Ascorbic Acid/metabolism ; Liver/metabolism ; Liver/drug effects ; Female ; Male ; Proteomics ; Mice ; L-Gulonolactone Oxidase/genetics ; L-Gulonolactone Oxidase/metabolism ; Gene Expression Profiling ; Transcriptome ; Principal Component Analysis ; Antioxidants/metabolism
Chemical Substances	Ascorbic Acid (PQ6CK8PD0R) ; L-Gulonolactone Oxidase (EC 1.1.3.8) ; Antioxidants
Language	English
Publishing date	2024-05-12
Publishing country	England
Document type	Journal Article
ZDB-ID	1138990-4
ISSN	0717-6287 ; 0716-9760
ISSN (online)	0717-6287
ISSN	0716-9760
DOI	10.1186/s40659-024-00509-x
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Article ; Online: The Identification of Nuclear FMRP Isoform Iso6 Partners.

Ledoux, Nassim / Lelong, Emeline I J / Simard, Alexandre / Hussein, Samer / Adjibade, Pauline / Lambert, Jean-Philippe / Mazroui, Rachid

Cells

2023 Volume 12, Issue 24

Abstract: A deficiency of FMRP, a canonical RNA-binding protein, causes the development of Fragile X Syndrome (FXS), which is characterised by multiple phenotypes, including neurodevelopmental disorders, intellectual disability, and autism. Due to the alternative ... ...

Abstract	A deficiency of FMRP, a canonical RNA-binding protein, causes the development of Fragile X Syndrome (FXS), which is characterised by multiple phenotypes, including neurodevelopmental disorders, intellectual disability, and autism. Due to the alternative splicing of the encoding
MeSH term(s)	Fragile X Mental Retardation Protein/genetics ; Proteasome Endopeptidase Complex/metabolism ; Protein Isoforms/metabolism ; Alternative Splicing ; DNA/metabolism
Chemical Substances	Fragile X Mental Retardation Protein (139135-51-6) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Protein Isoforms ; DNA (9007-49-2)
Language	English
Publishing date	2023-12-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells12242807
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Article ; Online: Control of mRNA turnover: implication of cytoplasmic RNA granules.

Adjibade, Pauline / Mazroui, Rachid

Seminars in cell & developmental biology

2014 Volume 34, Page(s) 15–23

Abstract: The control of mRNA turnover is essential for the cell to rationalize its mRNA content both under physiological conditions and upon stress. Several mechanisms involved in the control of mRNA turnover have been elucidated. These include surveillance ... ...

Abstract	The control of mRNA turnover is essential for the cell to rationalize its mRNA content both under physiological conditions and upon stress. Several mechanisms involved in the control of mRNA turnover have been elucidated. These include surveillance mechanisms such as nonsense-mediated decay, non-stop mediated decay and non-go-mediated decay that eliminate aberrant mRNAs, and regulatory mechanisms including AU-mediated decay, GU-mediated decay, and CDE-mediated decay that ensure mRNA plasticity. In general, the mechanisms of RNA decay rely on interactions between specific cis-acting RNA elements and selected RNA-binding proteins that either prevent the degradation of mRNA targets or induce the recruitment of decaying effectors leading to mRNA degradation. Formation of cytoplasmic RNA granules including processing bodies, stress granules, UV granules, and exosome granules have recently emerged as an additional mechanism that control mRNA turnover of selected mRNAs. Here we will review briefly review the main mechanisms that control mRNA decay and highlight possible implication of RNA granules in such mechanisms.
MeSH term(s)	Animals ; Cytoplasmic Granules/metabolism ; Gene Expression Regulation ; Humans ; RNA Stability ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/physiology ; Stress, Physiological
Chemical Substances	RNA, Messenger ; RNA-Binding Proteins
Language	English
Publishing date	2014-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2014.05.013
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Article ; Online: Prostate cancer resistance leads to a global deregulation of translation factors and unconventional translation.

Lelong, Emeline I J / Khelifi, Gabriel / Adjibade, Pauline / Joncas, France-Hélène / Grenier St-Sauveur, Valérie / Paquette, Virginie / Gris, Typhaine / Zoubeidi, Amina / Audet-Walsh, Etienne / Lambert, Jean-Philippe / Toren, Paul / Mazroui, Rachid / Hussein, Samer M I

NAR cancer

2022 Volume 4, Issue 4, Page(s) zcac034

Abstract: Emerging evidence associates translation factors and regulators to tumorigenesis. However, our understanding of translational changes in cancer resistance is still limited. Here, we generated an enzalutamide-resistant prostate cancer (PCa) model, which ... ...

Abstract	Emerging evidence associates translation factors and regulators to tumorigenesis. However, our understanding of translational changes in cancer resistance is still limited. Here, we generated an enzalutamide-resistant prostate cancer (PCa) model, which recapitulated key features of clinical enzalutamide-resistant PCa. Using this model and poly(ribo)some profiling, we investigated global translation changes that occur during acquisition of PCa resistance. We found that enzalutamide-resistant cells exhibit an overall decrease in mRNA translation with a specific deregulation in the abundance of proteins involved in mitochondrial processes and in translational regulation. However, several mRNAs escape this translational downregulation and are nonetheless bound to heavy polysomes in enzalutamide-resistant cells suggesting active translation. Moreover, expressing these corresponding genes in enzalutamide-sensitive cells promotes resistance to enzalutamide treatment. We also found increased association of long non-coding RNAs (lncRNAs) with heavy polysomes in enzalutamide-resistant cells, suggesting that some lncRNAs are actively translated during enzalutamide resistance. Consistent with these findings, expressing the predicted coding sequences of known lncRNAs
Language	English
Publishing date	2022-11-04
Publishing country	England
Document type	Journal Article
ISSN	2632-8674
ISSN (online)	2632-8674
DOI	10.1093/narcan/zcac034
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Article ; Online: Treatment of cancer cells with Lapatinib negatively regulates general translation and induces stress granules formation.

Adjibade, Pauline / Simoneau, Bryan / Ledoux, Nassim / Gauthier, William-Naud / Nkurunziza, Melisse / Khandjian, Edouard W / Mazroui, Rachid

PloS one

2020 Volume 15, Issue 5, Page(s) e0231894

Abstract: Stress granules (SG) are cytoplasmic RNA granules that form during various types of stress known to inhibit general translation, including oxidative stress, hypoxia, endoplasmic reticulum stress (ER), ionizing radiations or viral infection. Induction of ... ...

Abstract	Stress granules (SG) are cytoplasmic RNA granules that form during various types of stress known to inhibit general translation, including oxidative stress, hypoxia, endoplasmic reticulum stress (ER), ionizing radiations or viral infection. Induction of these SG promotes cell survival in part through sequestration of proapoptotic molecules, resulting in the inactivation of cell death pathways. SG also form in cancer cells, but studies investigating their formation upon treatment with chemotherapeutics are very limited. Here we identified Lapatinib (Tykerb / Tyverb®), a tyrosine kinase inhibitor used for the treatment of breast cancers as a new inducer of SG in breast cancer cells. Lapatinib-induced SG formation correlates with the inhibition of general translation initiation which involves the phosphorylation of the translation initiation factor eIF2α through the kinase PERK. Disrupting PERK-SG formation by PERK depletion experiments sensitizes resistant breast cancer cells to Lapatinib. This study further supports the assumption that treatment with anticancer drugs activates the SG pathway, which may constitute an intrinsic stress response used by cancer cells to resist treatment.
MeSH term(s)	Cell Line, Tumor ; Cytoplasmic Granules/drug effects ; Cytoplasmic Granules/metabolism ; Cytoplasmic Granules/pathology ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/genetics ; Endoplasmic Reticulum Stress/drug effects ; Endoplasmic Reticulum Stress/genetics ; Eukaryotic Initiation Factor-2/metabolism ; Humans ; Lapatinib/pharmacology ; Lapatinib/therapeutic use ; MCF-7 Cells ; Neoplasms/drug therapy ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/pathology ; Phosphorylation/drug effects ; Protein Biosynthesis/drug effects ; Up-Regulation/drug effects ; Up-Regulation/genetics ; eIF-2 Kinase/metabolism
Chemical Substances	Eukaryotic Initiation Factor-2 ; Lapatinib (0VUA21238F) ; PERK kinase (EC 2.7.11.1) ; eIF-2 Kinase (EC 2.7.11.1)
Language	English
Publishing date	2020-05-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0231894
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Article: Analysis of translation initiation during stress conditions by polysome profiling

Coudert, Laëtitia / Adjibade, Pauline / Mazroui, Rachid

Journal of visualized experiments. 2014 May 19, , no. 87

2014

Abstract: Precise control of mRNA translation is fundamental for eukaryotic cell homeostasis, particularly in response to physiological and pathological stress. Alterations of this program can lead to the growth of damaged cells, a hallmark of cancer development, ... ...

Abstract	Precise control of mRNA translation is fundamental for eukaryotic cell homeostasis, particularly in response to physiological and pathological stress. Alterations of this program can lead to the growth of damaged cells, a hallmark of cancer development, or to premature cell death such as seen in neurodegenerative diseases. Much of what is known concerning the molecular basis for translational control has been obtained from polysome analysis using a density gradient fractionation system. This technique relies on ultracentrifugation of cytoplasmic extracts on a linear sucrose gradient. Once the spin is completed, the system allows fractionation and quantification of centrifuged zones corresponding to different translating ribosomes populations, thus resulting in a polysome profile. Changes in the polysome profile are indicative of changes or defects in translation initiation that occur in response to various types of stress. This technique also allows to assess the role of specific proteins on translation initiation, and to measure translational activity of specific mRNAs. Here we describe our protocol to perform polysome profiles in order to assess translation initiation of eukaryotic cells and tissues under either normal or stress growth conditions.
Keywords	carcinogenesis ; cell death ; eukaryotic cells ; fractionation ; homeostasis ; messenger RNA ; neoplasms ; neurodegenerative diseases ; proteins ; ribosomes ; sucrose ; tissues ; translation (genetics) ; ultracentrifugation
Language	English
Dates of publication	2014-0519
Size	p. e51164.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/51164
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Analysis of translation initiation during stress conditions by polysome profiling.

Coudert, Laëtitia / Adjibade, Pauline / Mazroui, Rachid

Journal of visualized experiments : JoVE

2014 , Issue 87

Abstract	Precise control of mRNA translation is fundamental for eukaryotic cell homeostasis, particularly in response to physiological and pathological stress. Alterations of this program can lead to the growth of damaged cells, a hallmark of cancer development, or to premature cell death such as seen in neurodegenerative diseases. Much of what is known concerning the molecular basis for translational control has been obtained from polysome analysis using a density gradient fractionation system. This technique relies on ultracentrifugation of cytoplasmic extracts on a linear sucrose gradient. Once the spin is completed, the system allows fractionation and quantification of centrifuged zones corresponding to different translating ribosomes populations, thus resulting in a polysome profile. Changes in the polysome profile are indicative of changes or defects in translation initiation that occur in response to various types of stress. This technique also allows to assess the role of specific proteins on translation initiation, and to measure translational activity of specific mRNAs. Here we describe our protocol to perform polysome profiles in order to assess translation initiation of eukaryotic cells and tissues under either normal or stress growth conditions.
MeSH term(s)	Animals ; Centrifugation, Density Gradient/methods ; Drosophila ; HeLa Cells ; Humans ; Mice ; Peptide Chain Initiation, Translational ; Polyribosomes/chemistry ; Polyribosomes/genetics ; RNA, Messenger/genetics ; RNA, Messenger/isolation & purification ; Ribosomes/chemistry ; Ribosomes/genetics ; Stress, Physiological/genetics
Chemical Substances	RNA, Messenger
Language	English
Publishing date	2014-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/51164
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Article: Rôle de l'heme regulated inhibitor (HRI) dans la résistance à l'apoptose.

Joncas, France-Hélène / Adjibade, Pauline / Mazroui, Rachid

Medecine sciences : M/S

2014 Volume 30, Issue 10, Page(s) 882–888

Abstract: When exposed to environmental stresses, cells activate defence mechanisms to adapt stress and inhibit apoptotic pathways leading to their survival. Stressed cells also reduce their general metabolism in part by inhibiting mRNA translation, thereby saving ...

Title translation	Role of HRI in apoptosis resistance.
Abstract	When exposed to environmental stresses, cells activate defence mechanisms to adapt stress and inhibit apoptotic pathways leading to their survival. Stressed cells also reduce their general metabolism in part by inhibiting mRNA translation, thereby saving energy needed to repair stress-induced damages. Under stress conditions, the inhibition of mRNA translation occurs mainly at its initiation step through the phosphorylation of the translation initiation factor eIF2α. One of the four kinases known to phosphorylate eIF2α is heme-regulated inhibitor (HRI). The activation of HRI occurs under conditions of heme deficiency, oxidative stress and treatment with anti-cancer drugs such as proteasome inhibitors. In this article, we discuss the role of HRI in promoting cell resistance to stress-mediated apoptosis.
MeSH term(s)	Animals ; Apoptosis/genetics ; Cytoplasmic Granules/metabolism ; Erythroblasts/physiology ; Heme/physiology ; Humans ; Oxidative Stress/physiology ; Protein Biosynthesis/genetics ; Stress, Physiological/physiology ; eIF-2 Kinase/physiology
Chemical Substances	Heme (42VZT0U6YR) ; eIF-2 Kinase (EC 2.7.11.1)
Language	French
Publishing date	2014-10
Publishing country	France
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/20143010015
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Article ; Online: The RabGAP TBC-11 controls Argonaute localization for proper microRNA function in C. elegans.

Michaud, Pascale / Shah, Vivek Nilesh / Adjibade, Pauline / Houle, Francois / Quévillon Huberdeau, Miguel / Rioux, Rachel / Lavoie-Ouellet, Camille / Gu, Weifeng / Mazroui, Rachid / Simard, Martin J

PLoS genetics

2021 Volume 17, Issue 4, Page(s) e1009511

Abstract: Once loaded onto Argonaute proteins, microRNAs form a silencing complex called miRISC that targets mostly the 3'UTR of mRNAs to silence their translation. How microRNAs are transported to and from their target mRNA remains poorly characterized. While ... ...

Abstract	Once loaded onto Argonaute proteins, microRNAs form a silencing complex called miRISC that targets mostly the 3'UTR of mRNAs to silence their translation. How microRNAs are transported to and from their target mRNA remains poorly characterized. While some reports linked intracellular trafficking to microRNA activity, it is still unclear how these pathways coordinate for proper microRNA-mediated gene silencing and turnover. Through a forward genetic screen using Caenorhabditis elegans, we identified the RabGAP tbc-11 as an important factor for the microRNA pathway. We show that TBC-11 acts mainly through the small GTPase RAB-6 and that its regulation is required for microRNA function. The absence of functional TBC-11 increases the pool of microRNA-unloaded Argonaute ALG-1 that is likely associated to endomembranes. Furthermore, in this condition, this pool of Argonaute accumulates in a perinuclear region and forms a high molecular weight complex. Altogether, our data suggest that the alteration of TBC-11 generates a fraction of ALG-1 that cannot bind to target mRNAs, leading to defective gene repression. Our results establish the importance of intracellular trafficking for microRNA function and demonstrate the involvement of a small GTPase and its GAP in proper Argonaute localization in vivo.
MeSH term(s)	3' Untranslated Regions/genetics ; Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Gene Expression Regulation, Developmental/genetics ; Gene Silencing ; MicroRNAs/genetics ; Protein Biosynthesis ; RNA, Messenger/genetics ; RNA-Binding Proteins/genetics ; rab GTP-Binding Proteins/genetics
Chemical Substances	3' Untranslated Regions ; ALG-1 protein, C elegans ; Caenorhabditis elegans Proteins ; MicroRNAs ; RNA, Messenger ; RNA-Binding Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-04-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1009511
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Article ; Online: The chemotherapeutic agent bortezomib induces the formation of stress granules

Gareau Cristina / Fournier Marie-Josée / Mazroui Rachid

Cancer Cell International, Vol 10, Iss 1, p

2010 Volume 12

Abstract: Abstract Background Cytoplasmic stress granules (SGs) are specialized storage sites of untranslated mRNAs whose formation occurs under different stress conditions and is often associated with cell survival. SGs-inducing stresses include radiations, ... ...

Abstract	Abstract Background Cytoplasmic stress granules (SGs) are specialized storage sites of untranslated mRNAs whose formation occurs under different stress conditions and is often associated with cell survival. SGs-inducing stresses include radiations, hypoxia, viral infections, and chemical inhibitors of specific translation initiation factors. The FDA-approved drug bortezomib (Velcade ® ) is a peptide boronate inhibitor of the 26S proteasome that is very efficient for the treatment of myelomas and other hematological tumors. Solid tumors are largely refractory to bortezomib. In the present study, we investigated the formation of SGs following bortezomib treatment. Results We show that bortezomib efficiently induces the formation of SGs in cancer cells. This process involves the phosphorylation of translation initiation factor eIF2α by heme-regulated inhibitor kinase (HRI). Depletion of HRI prevents bortezomib-induced formation of SGs and promotes apoptosis. Conclusions This is the first study describing the formation of SGs by a chemotherapeutic compound. We speculate that the activation of HRI and the formation of SGs might constitute a mechanism by which cancer cells resist bortezomib-mediated apoptosis.
Keywords	Neoplasms. Tumors. Oncology. Including cancer and carcinogens ; RC254-282 ; Internal medicine ; RC31-1245 ; Medicine ; R ; DOAJ:Oncology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
Language	English
Publishing date	2010-04-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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