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  1. Article ; Online: Vitamin B

    Vílchez-Acosta, Alba / Desdín-Micó, Gabriela / Ocampo, Alejandro

    Nature metabolism

    2023  Volume 5, Issue 11, Page(s) 1844–1845

    MeSH term(s) Vitamin B 12 ; Cellular Reprogramming ; Vitamins
    Chemical Substances Vitamin B 12 (P6YC3EG204) ; Vitamins
    Language English
    Publishing date 2023-11-16
    Publishing country Germany
    Document type Journal Article
    ISSN 2522-5812
    ISSN (online) 2522-5812
    DOI 10.1038/s42255-023-00917-5
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  2. Article: Adult-specific Reelin expression alters striatal neuronal organization: implications for neuropsychiatric disorders.

    Pardo, Mònica / Gregorio, Sara / Montalban, Enrica / Pujadas, Lluís / Elias-Tersa, Alba / Masachs, Núria / Vílchez-Acosta, Alba / Parent, Annabelle / Auladell, Carme / Girault, Jean-Antoine / Vila, Miquel / Nairn, Angus C / Manso, Yasmina / Soriano, Eduardo

    Frontiers in cellular neuroscience

    2023  Volume 17, Page(s) 1143319

    Abstract: In addition to neuronal migration, brain development, and adult plasticity, the extracellular matrix protein Reelin has been extensively implicated in human psychiatric disorders such as schizophrenia, bipolar disorder, and autism spectrum disorder. ... ...

    Abstract In addition to neuronal migration, brain development, and adult plasticity, the extracellular matrix protein Reelin has been extensively implicated in human psychiatric disorders such as schizophrenia, bipolar disorder, and autism spectrum disorder. Moreover, heterozygous
    Language English
    Publishing date 2023-04-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2452963-1
    ISSN 1662-5102
    ISSN 1662-5102
    DOI 10.3389/fncel.2023.1143319
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  3. Article ; Online: In vivo reprogramming leads to premature death linked to hepatic and intestinal failure.

    Parras, Alberto / Vílchez-Acosta, Alba / Desdín-Micó, Gabriela / Picó, Sara / Mrabti, Calida / Montenegro-Borbolla, Elena / Maroun, Céline Yacoub / Haghani, Amin / Brooke, Robert / Del Carmen Maza, María / Rechsteiner, Cheyenne / Battiston, Fabrice / Branchina, Clémence / Perez, Kevin / Horvath, Steve / Bertelli, Claire / Sempoux, Christine / Ocampo, Alejandro

    Nature aging

    2023  Volume 3, Issue 12, Page(s) 1509–1520

    Abstract: The induction of cellular reprogramming via expression of the transcription factors Oct4, Sox2, Klf4 and c-Myc (OSKM) can drive dedifferentiation of somatic cells and ameliorate age-associated phenotypes in multiple tissues and organs. However, the ... ...

    Abstract The induction of cellular reprogramming via expression of the transcription factors Oct4, Sox2, Klf4 and c-Myc (OSKM) can drive dedifferentiation of somatic cells and ameliorate age-associated phenotypes in multiple tissues and organs. However, the benefits of long-term in vivo reprogramming are limited by detrimental side-effects. Here, using complementary genetic approaches, we demonstrated that continuous induction of the reprogramming factors in vivo leads to hepatic and intestinal dysfunction resulting in decreased body weight and contributing to premature death (within 1 week). By generating a transgenic reprogrammable mouse strain, avoiding OSKM expression in both liver and intestine, we reduced the early lethality and adverse effects associated with in vivo reprogramming and induced a decrease in organismal biological age. This reprogramming mouse strain, which allows longer-term continuous induction of OSKM with attenuated toxicity, can help better understand rejuvenation, regeneration and toxicity during in vivo reprogramming.
    MeSH term(s) Mice ; Animals ; Intestinal Failure ; Mortality, Premature ; Cellular Reprogramming/genetics ; Transcription Factors/genetics ; Mice, Transgenic ; Liver/metabolism
    Chemical Substances Transcription Factors
    Language English
    Publishing date 2023-11-27
    Publishing country United States
    Document type Journal Article
    ISSN 2662-8465
    ISSN (online) 2662-8465
    DOI 10.1038/s43587-023-00528-5
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  4. Article ; Online: Specific contribution of Reelin expressed by Cajal-Retzius cells or GABAergic interneurons to cortical lamination.

    Vílchez-Acosta, Alba / Manso, Yasmina / Cárdenas, Adrián / Elias-Tersa, Alba / Martínez-Losa, Magdalena / Pascual, Marta / Álvarez-Dolado, Manuel / Nairn, Angus C / Borrell, Víctor / Soriano, Eduardo

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 37, Page(s) e2120079119

    Abstract: The extracellular protein Reelin, expressed by Cajal-Retzius (CR) cells at early stages of cortical development and at late stages by GABAergic interneurons, regulates radial migration and the "inside-out" pattern of positioning. Current models of Reelin ...

    Abstract The extracellular protein Reelin, expressed by Cajal-Retzius (CR) cells at early stages of cortical development and at late stages by GABAergic interneurons, regulates radial migration and the "inside-out" pattern of positioning. Current models of Reelin functions in corticogenesis focus on early CR cell-derived Reelin in layer I. However, developmental disorders linked to Reelin deficits, such as schizophrenia and autism, are related to GABAergic interneuron-derived Reelin, although its role in migration has not been established. Here we selectively inactivated the
    MeSH term(s) Animals ; Cell Movement ; Cerebral Cortex/cytology ; Cerebral Cortex/embryology ; GABAergic Neurons/enzymology ; Hippocampus/embryology ; Hippocampus/enzymology ; Interneurons/enzymology ; Mice ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurons/cytology ; Neurons/enzymology ; Reelin Protein/genetics ; Reelin Protein/metabolism
    Chemical Substances Nerve Tissue Proteins ; Reelin Protein ; Reln protein, mouse (EC 3.4.21.-)
    Language English
    Publishing date 2022-09-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2120079119
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    In stock of ZB MED Cologne/Königswinter

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  5. Article ; Online: A conserved role for Syntaxin-1 in pre- and post-commissural midline axonal guidance in fly, chick, and mouse.

    Ros, Oriol / Barrecheguren, Pablo José / Cotrufo, Tiziana / Schaettin, Martina / Roselló-Busquets, Cristina / Vílchez-Acosta, Alba / Hernaiz-Llorens, Marc / Martínez-Marmol, Ramón / Ulloa, Fausto / Stoeckli, Esther T / Araújo, Sofia J / Soriano, Eduardo

    PLoS genetics

    2018  Volume 14, Issue 6, Page(s) e1007432

    Abstract: Axonal growth and guidance rely on correct growth cone responses to guidance cues. Unlike the signaling cascades that link axonal growth to cytoskeletal dynamics, little is known about the crosstalk mechanisms between guidance and membrane dynamics and ... ...

    Abstract Axonal growth and guidance rely on correct growth cone responses to guidance cues. Unlike the signaling cascades that link axonal growth to cytoskeletal dynamics, little is known about the crosstalk mechanisms between guidance and membrane dynamics and turnover. Recent studies indicate that whereas axonal attraction requires exocytosis, chemorepulsion relies on endocytosis. Indeed, our own studies have shown that Netrin-1/Deleted in Colorectal Cancer (DCC) signaling triggers exocytosis through the SNARE Syntaxin-1 (STX1). However, limited in vivo evidence is available about the role of SNARE proteins in axonal guidance. To address this issue, here we systematically deleted SNARE genes in three species. We show that loss-of-function of STX1 results in pre- and post-commissural axonal guidance defects in the midline of fly, chick, and mouse embryos. Inactivation of VAMP2, Ti-VAMP, and SNAP25 led to additional abnormalities in axonal guidance. We also confirmed that STX1 loss-of-function results in reduced sensitivity of commissural axons to Slit-2 and Netrin-1. Finally, genetic interaction studies in Drosophila show that STX1 interacts with both the Netrin-1/DCC and Robo/Slit pathways. Our data provide evidence of an evolutionarily conserved role of STX1 and SNARE proteins in midline axonal guidance in vivo, by regulating both pre- and post-commissural guidance mechanisms.
    MeSH term(s) Animals ; Axons/metabolism ; Chemotaxis/genetics ; Chick Embryo ; Drosophila/genetics ; Drosophila Proteins/genetics ; Exocytosis/genetics ; Gene Expression Regulation, Developmental/genetics ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Mice ; Mice, Knockout ; Nerve Growth Factors/genetics ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nervous System/embryology ; Netrin-1/genetics ; Netrin-1/metabolism ; Neurogenesis/genetics ; Neurogenesis/physiology ; Qa-SNARE Proteins/genetics ; Qa-SNARE Proteins/physiology ; SNARE Proteins/genetics ; SNARE Proteins/metabolism ; Signal Transduction/genetics ; Spinal Cord/embryology ; Spinal Cord/metabolism ; Syntaxin 1/genetics ; Syntaxin 1/physiology
    Chemical Substances Drosophila Proteins ; Glycoproteins ; Nerve Growth Factors ; Nerve Tissue Proteins ; Qa-SNARE Proteins ; SNARE Proteins ; Syntaxin 1 ; slit protein, vertebrate ; Netrin-1 (158651-98-0)
    Language English
    Publishing date 2018-06-18
    Publishing country United States
    Document type Journal Article ; 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.1007432
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  6. Article ; Online: Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.

    Torrent, Joan / Vilchez-Acosta, Alba / Muñoz-Torrero, Diego / Trovaslet, Marie / Nachon, Florian / Chatonnet, Arnaud / Grznarova, Katarina / Acquatella-Tran Van Ba, Isabelle / Le Goffic, Ronan / Herzog, Laetitia / Béringue, Vincent / Rezaei, Human

    Acta neuropathologica communications

    2015  Volume 3, Page(s) 18

    Abstract: Introduction: The prion protein (PrP) binds to various molecular partners, but little is known about their potential impact on the pathogenesis of prion diseases: Results: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), ...

    Abstract Introduction: The prion protein (PrP) binds to various molecular partners, but little is known about their potential impact on the pathogenesis of prion diseases
    Results: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), a key protein of the cholinergic system in neural and non-neural tissues. This heterologous association induced aggregation of monomeric PrP and modified the structural properties of PrP amyloid fibrils. Following its recruitment into PrP fibrils, AChE loses its enzymatic activity and enhances PrP-mediated cytotoxicity. Using several truncated PrP variants and specific tight-binding AChE inhibitors (AChEis), we then demonstrate that the PrP-AChE interaction requires two mutually exclusive sub-sites in PrP N-terminal domain and an aromatic-rich region at the entrance of AChE active center gorge. We show that AChEis that target this site impair PrP-AChE complex formation and also limit the accumulation of pathological prion protein (PrPSc) in prion-infected cell cultures. Furthermore, reduction of AChE levels in prion-infected heterozygous AChE knock-out mice leads to slightly but significantly prolonged incubation time. Finally, we found that AChE levels were altered in prion-infected cells and tissues, suggesting that AChE might be directly associated with abnormal PrP.
    Conclusion: Our results indicate that AChE deserves consideration as a new actor in expanding pathologically relevant PrP morphotypes and as a therapeutic target.
    MeSH term(s) Acetylcholinesterase/deficiency ; Acetylcholinesterase/genetics ; Acetylcholinesterase/metabolism ; Amyloid/metabolism ; Animals ; Cell Culture Techniques ; Humans ; Mice ; Mice, Knockout ; Neurons/metabolism ; PrPSc Proteins/metabolism ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Prions/metabolism ; Prions/pathogenicity
    Chemical Substances Amyloid ; PrPSc Proteins ; Prions ; Acetylcholinesterase (EC 3.1.1.7)
    Language English
    Publishing date 2015-04-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2715589-4
    ISSN 2051-5960 ; 2051-5960
    ISSN (online) 2051-5960
    ISSN 2051-5960
    DOI 10.1186/s40478-015-0188-0
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  7. Article: Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases

    Vilchez Acosta, Alba Del Valle / Muñoz-Torrero, Diego / Trovaslet, Marie / Nachon, Florian / Chatonnet, Arnaud / Grznarova, Katarina / Acquatella-Tran Van Ba, Isabelle / Le Goffic, Ronan / Herzog, Laetitia / Beringue, Vincent / Rezaei, Human

    Acta neuropathologica communications 1 (3), 18. (2015)

    Abstract: Introduction: The prion protein (PrP) binds to various molecular partners, but little is known about their potentialimpact on the pathogenesis of prion diseases. Results: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), a ... ...

    Abstract Introduction: The prion protein (PrP) binds to various molecular partners, but little is known about their potentialimpact on the pathogenesis of prion diseases. Results: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), a key protein of the cholinergic system in neural and non-neural tissues. This heterologous association induced aggregation of monomeric PrP and modified the structural properties of PrP amyloid fibrils. Following its recruitment into PrP fibrils, AChE loses its enzymatic activity and enhances PrP-mediated cytotoxicity. Using several truncated PrP variants and specific tight-binding AChE inhibitors (AChEis), we then demonstrate that the PrP-AChE interaction requires two mutually exclusive sub-sites in PrPN-terminal domain and an aromatic-rich region at the entrance of AChE active center gorge. We show that AChEis that target this site impair PrP-AChE complex formation and also limit the accumulation of pathological prion protein (PrPSc) in prion-infected cell cultures. Furthermore, reduction of AChE levels in prion-infected heterozygous AChE knock-out mice leads to slightly but significantly prolonged incubation time. Finally, we found that AChE levels were altered in prioninfected cells and tissues, suggesting that AChE might be directly associated with abnormal PrP. Conclusion: Our results indicate that AChE deserves consideration as a new actor in expanding pathologically relevant PrP morphotypes and as a therapeutic target.
    Language English
    Document type Article
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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  8. Article: Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases

    Vilchez Acosta, Alba Del Valle / Muñoz-Torrero, Diego / Trovaslet, Marie / Nachon, Florian / Chatonnet, Arnaud / Grznarova, Katarina / Acquatella-Tran Van Ba, Isabelle / Le Goffic, Ronan / Herzog, Laetitia / Beringue, Vincent / Rezaei, Human

    Acta neuropathologica communications 1 (3), 18. (2015)

    Abstract: Introduction: The prion protein (PrP) binds to various molecular partners, but little is known about their potentialimpact on the pathogenesis of prion diseases. Results: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), a ... ...

    Abstract Introduction: The prion protein (PrP) binds to various molecular partners, but little is known about their potentialimpact on the pathogenesis of prion diseases. Results: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), a key protein of the cholinergic system in neural and non-neural tissues. This heterologous association induced aggregation of monomeric PrP and modified the structural properties of PrP amyloid fibrils. Following its recruitment into PrP fibrils, AChE loses its enzymatic activity and enhances PrP-mediated cytotoxicity. Using several truncated PrP variants and specific tight-binding AChE inhibitors (AChEis), we then demonstrate that the PrP-AChE interaction requires two mutually exclusive sub-sites in PrPN-terminal domain and an aromatic-rich region at the entrance of AChE active center gorge. We show that AChEis that target this site impair PrP-AChE complex formation and also limit the accumulation of pathological prion protein (PrPSc) in prion-infected cell cultures. Furthermore, reduction of AChE levels in prion-infected heterozygous AChE knock-out mice leads to slightly but significantly prolonged incubation time. Finally, we found that AChE levels were altered in prioninfected cells and tissues, suggesting that AChE might be directly associated with abnormal PrP. Conclusion: Our results indicate that AChE deserves consideration as a new actor in expanding pathologically relevant PrP morphotypes and as a therapeutic target.
    Language English
    Document type Article
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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