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  1. Article ; Online: The

    Kerr, Rex A / Roux, Antoine E / Goudeau, Jérôme / Kenyon, Cynthia

    Frontiers in aging

    2022  Volume 3, Page(s) 932656

    Abstract: Organisms undergo a variety of characteristic changes as they age, suggesting a substantial commonality in the mechanistic basis of aging. Experiments in model organisms have revealed a variety of cellular systems that impact lifespan, but technical ... ...

    Abstract Organisms undergo a variety of characteristic changes as they age, suggesting a substantial commonality in the mechanistic basis of aging. Experiments in model organisms have revealed a variety of cellular systems that impact lifespan, but technical challenges have prevented a comprehensive evaluation of how these components impact the trajectory of aging, and many components likely remain undiscovered. To facilitate the deeper exploration of aging trajectories at a sufficient scale to enable primary screening, we have created the
    Language English
    Publishing date 2022-08-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 3076785-4
    ISSN 2673-6217 ; 2673-6217
    ISSN (online) 2673-6217
    ISSN 2673-6217
    DOI 10.3389/fragi.2022.932656
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Addendum: A lysosomal switch triggers proteostasis renewal in the immortal C. elegans germ lineage.

    Goudeau, Jérôme / Samaddar, Madhuja / Bohnert, K Adam / Kenyon, Cynthia

    Nature

    2020  Volume 580, Issue 7802, Page(s) E5

    Language English
    Publishing date 2020-03-11
    Publishing country England
    Document type Journal Article ; Published Erratum
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-020-2108-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  3. Article ; Online: A genetic screen identifies new steps in oocyte maturation that enhance proteostasis in the immortal germ lineage.

    Samaddar, Madhuja / Goudeau, Jérôme / Sanchez, Melissa / Hall, David H / Bohnert, K Adam / Ingaramo, Maria / Kenyon, Cynthia

    eLife

    2021  Volume 10

    Abstract: Somatic cells age and die, but the germ-cell lineage is immortal. ... ...

    Abstract Somatic cells age and die, but the germ-cell lineage is immortal. In
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Genetic Testing ; Germ Cells/physiology ; Oocytes/physiology ; Proteostasis
    Chemical Substances Caenorhabditis elegans Proteins
    Language English
    Publishing date 2021-04-13
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.62653
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  4. Article ; Online: Split-wrmScarlet and split-sfGFP: tools for faster, easier fluorescent labeling of endogenous proteins in Caenorhabditis elegans.

    Goudeau, Jérôme / Sharp, Catherine S / Paw, Jonathan / Savy, Laura / Leonetti, Manuel D / York, Andrew G / Updike, Dustin L / Kenyon, Cynthia / Ingaramo, Maria

    Genetics

    2021  Volume 217, Issue 4

    Abstract: We create and share a new red fluorophore, along with a set of strains, reagents and protocols, to make it faster and easier to label endogenous Caenorhabditis elegans proteins with fluorescent tags. CRISPR-mediated fluorescent labeling of C. elegans ... ...

    Abstract We create and share a new red fluorophore, along with a set of strains, reagents and protocols, to make it faster and easier to label endogenous Caenorhabditis elegans proteins with fluorescent tags. CRISPR-mediated fluorescent labeling of C. elegans proteins is an invaluable tool, but it is much more difficult to insert fluorophore-size DNA segments than it is to make small gene edits. In principle, high-affinity asymmetrically split fluorescent proteins solve this problem in C. elegans: the small fragment can quickly and easily be fused to almost any protein of interest, and can be detected wherever the large fragment is expressed and complemented. However, there is currently only one available strain stably expressing the large fragment of a split fluorescent protein, restricting this solution to a single tissue (the germline) in the highly autofluorescent green channel. No available C. elegans lines express unbound large fragments of split red fluorescent proteins, and even state-of-the-art split red fluorescent proteins are dim compared to the canonical split-sfGFP protein. In this study, we engineer a bright, high-affinity new split red fluorophore, split-wrmScarlet. We generate transgenic C. elegans lines to allow easy single-color labeling in muscle or germline cells and dual-color labeling in somatic cells. We also describe a novel expression strategy for the germline, where traditional expression strategies struggle. We validate these strains by targeting split-wrmScarlet to several genes whose products label distinct organelles, and we provide a protocol for easy, cloning-free CRISPR/Cas9 editing. As the collection of split-FP strains for labeling in different tissues or organelles expands, we will post updates at doi.org/10.5281/zenodo.3993663.
    MeSH term(s) Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Genetic Engineering/methods ; Germ Cells/cytology ; Germ Cells/metabolism ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Protein Transport ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Red Fluorescent Protein
    Chemical Substances Caenorhabditis elegans Proteins ; Luminescent Proteins ; Recombinant Proteins ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2021-02-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1093/genetics/iyab014
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    In stock of ZB MED Cologne/Königswinter

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  5. Article ; Online: Coelomocytes Regulate Starvation-Induced Fat Catabolism and Lifespan Extension through the Lipase LIPL-5 in Caenorhabditis elegans.

    Buis, Alexia / Bellemin, Stéphanie / Goudeau, Jérôme / Monnier, Léa / Loiseau, Nicolas / Guillou, Hervé / Aguilaniu, Hugo

    Cell reports

    2019  Volume 28, Issue 4, Page(s) 1041–1049.e4

    Abstract: Dietary restriction is known to extend the lifespan and reduce fat stores in most species tested to date, but the molecular mechanisms linking these events remain unclear. Here, we found that bacterial deprivation of Caenorhabditis elegans leads to ... ...

    Abstract Dietary restriction is known to extend the lifespan and reduce fat stores in most species tested to date, but the molecular mechanisms linking these events remain unclear. Here, we found that bacterial deprivation of Caenorhabditis elegans leads to lifespan extension with concomitant mobilization of fat stores. We find that LIPL-5 expression is induced by starvation and that the LIPL-5 lipase is present in coelomocyte cells and regulates fat catabolism and longevity during the bacterial deprivation response. Either LIPL-5 or coelomocyte deficiency prevents the rapid mobilization of intestinal triacylglycerol and enhanced lifespan extension in response to bacterial deprivation, whereas the combination of both defects has no additional or synergistic effect. Thus, the capacity to mobilize fat via LIPL-5 is directly linked to an animal's capacity to withstand long-term nutrient deprivation. Our data establish a role for LIPL-5 and coelomocytes in regulating fat consumption and lifespan extension upon DR.
    MeSH term(s) Animals ; Bacteria/metabolism ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/microbiology ; Caenorhabditis elegans Proteins/metabolism ; Lipase/metabolism ; Lipid Metabolism ; Longevity/physiology ; Lysosomes/metabolism ; Mutation/genetics ; Starvation/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; lipl-5 protein, C elegans (EC 3.1.1.-) ; Lipase (EC 3.1.1.3)
    Language English
    Publishing date 2019-07-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2019.06.064
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Carbonylated proteins are eliminated during reproduction in C. elegans.

    Goudeau, Jérôme / Aguilaniu, Hugo

    Aging cell

    2010  Volume 9, Issue 6, Page(s) 991–1003

    Abstract: Oxidatively damaged proteins accumulate with age in many species (Stadtman (1992) Science257, 1220-1224). This means that damage must be reset at the time of reproduction. To visualize this resetting in the roundworm Caenorhabditis elegans, a novel ... ...

    Abstract Oxidatively damaged proteins accumulate with age in many species (Stadtman (1992) Science257, 1220-1224). This means that damage must be reset at the time of reproduction. To visualize this resetting in the roundworm Caenorhabditis elegans, a novel immunofluorescence technique that allows the detection of carbonylated proteins in situ was developed. The application of this technique revealed that carbonylated proteins are eliminated during C. elegans reproduction. This purging occurs abruptly within the germline at the time of oocyte maturation. Surprisingly, the germline was markedly more oxidized than the surrounding somatic tissues. Because distinct mechanisms have been proposed to explain damage elimination in yeast and mice (Aguilaniu et al. (2003) Science299, 1751-1753; Hernebring et al. (2006) Proc Natl Acad Sci USA103, 7700-7705), possible common mechanisms between worms and one of these systems were tested. The results show that, unlike in yeast (Aguilaniu et al. (2003) Science299, 1751-1753; Erjavec et al. (2008) Proc Natl Acad Sci USA105, 18764-18769), the elimination of carbonylated proteins in worms does not require the presence of the longevity-ensuring gene, SIR-2.1. However, similar to findings in mice (Hernebring et al. (2006) Proc Natl Acad Sci USA103, 7700-7705), proteasome activity in the germline is required for the resetting of carbonylated proteins during reproduction in C. elegans. Thus, oxidatively damaged proteins are eliminated during reproduction in worms through the proteasome. This finding suggests that the resetting of damaged proteins during reproduction is conserved, therefore validating the use of C. elegans as a model to study the molecular basis of damage elimination.
    MeSH term(s) Animals ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Fluorescent Antibody Technique ; Longevity/genetics ; Oxidation-Reduction ; Proteasome Endopeptidase Complex/metabolism ; Protein Carbonylation ; Reproduction/physiology ; Sirtuins/genetics ; Sirtuins/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; SIR-2.1 protein, C elegans (EC 3.5.1.-) ; Sirtuins (EC 3.5.1.-)
    Language English
    Publishing date 2010-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2113083-8
    ISSN 1474-9726 ; 1474-9718
    ISSN (online) 1474-9726
    ISSN 1474-9718
    DOI 10.1111/j.1474-9726.2010.00625.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Novel insights from a multiomics dissection of the Hayflick limit.

    Chan, Michelle / Yuan, Han / Soifer, Ilya / Maile, Tobias M / Wang, Rebecca Y / Ireland, Andrea / O'Brien, Jonathon J / Goudeau, Jérôme / Chan, Leanne J G / Vijay, Twaritha / Freund, Adam / Kenyon, Cynthia / Bennett, Bryson D / McAllister, Fiona E / Kelley, David R / Roy, Margaret / Cohen, Robert L / Levinson, Arthur D / Botstein, David /
    Hendrickson, David G

    eLife

    2022  Volume 11

    Abstract: The process wherein dividing cells exhaust proliferative capacity and enter into replicative senescence has become a prominent model for cellular aging in vitro. Despite decades of study, this cellular state is not fully understood in culture and even ... ...

    Abstract The process wherein dividing cells exhaust proliferative capacity and enter into replicative senescence has become a prominent model for cellular aging in vitro. Despite decades of study, this cellular state is not fully understood in culture and even much less so during aging. Here, we revisit Leonard Hayflick's original observation of replicative senescence in WI-38 human lung fibroblasts equipped with a battery of modern techniques including RNA-seq, single-cell RNA-seq, proteomics, metabolomics, and ATAC-seq. We find evidence that the transition to a senescent state manifests early, increases gradually, and corresponds to a concomitant global increase in DNA accessibility in nucleolar and lamin associated domains. Furthermore, we demonstrate that senescent WI-38 cells acquire a striking resemblance to myofibroblasts in a process similar to the epithelial to mesenchymal transition (EMT) that is regulated by t YAP1/TEAD1 and TGF-β2. Lastly, we show that verteporfin inhibition of YAP1/TEAD1 activity in aged WI-38 cells robustly attenuates this gene expression program.
    MeSH term(s) Aged ; Aging/physiology ; Cell Line ; Cellular Senescence/genetics ; Epithelial-Mesenchymal Transition ; Fibroblasts/metabolism ; Humans
    Language English
    Publishing date 2022-02-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.70283
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  8. Article ; Online: Fatty acid desaturation links germ cell loss to longevity through NHR-80/HNF4 in C. elegans.

    Goudeau, Jérôme / Bellemin, Stéphanie / Toselli-Mollereau, Esther / Shamalnasab, Mehrnaz / Chen, Yiqun / Aguilaniu, Hugo

    PLoS biology

    2011  Volume 9, Issue 3, Page(s) e1000599

    Abstract: Background: Preventing germline stem cell proliferation extends lifespan in nematodes and flies. So far, studies on germline-longevity signaling have focused on daf-16/FOXO and daf-12/VDR. Here, we report on NHR-80/HNF4, a nuclear receptor that ... ...

    Abstract Background: Preventing germline stem cell proliferation extends lifespan in nematodes and flies. So far, studies on germline-longevity signaling have focused on daf-16/FOXO and daf-12/VDR. Here, we report on NHR-80/HNF4, a nuclear receptor that specifically mediates longevity induced by depletion of the germ line through a mechanism that implicates fatty acid monodesaturation.
    Methods and findings: nhr-80/HNF4 is induced in animals lacking a germ line and is specifically required for their extended longevity. Overexpressing nhr-80/HNF4 increases the lifespan of germline-less animals. This lifespan extension can occur in the absence of daf-16/FOXO but requires the presence of the nuclear receptor DAF-12/VDR. We show that the fatty acid desaturase, FAT-6/SCD1, is a key target of NHR-80/HNF4 and promotes germline-longevity by desaturating stearic acid to oleic acid (OA). We find that NHR-80/HNF4 and OA must work in concert to promote longevity.
    Conclusions: Taken together, our data indicate that the NHR-80 pathway participates in the mechanism of longevity extension through depletion of the germ line. We identify fat-6 and OA as essential downstream elements although other targets must also be present. Thus, NHR-80 links fatty acid desaturation to lifespan extension through germline ablation in a daf-16/FOXO independent manner.
    MeSH term(s) Animals ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Fatty Acids/chemistry ; Fatty Acids/metabolism ; Germ Cells/cytology ; Germ Cells/physiology ; Longevity ; Oleic Acid/metabolism ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Stearoyl-CoA Desaturase/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Fatty Acids ; NHR-80 protein, C elegans ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins ; Oleic Acid (2UMI9U37CP) ; Stearoyl-CoA Desaturase (EC 1.14.19.1)
    Language English
    Publishing date 2011-03-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.1000599
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    Zs.A 6193: Show issues Location:
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