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  1. AU="Culotta, Lorenza"
  2. AU=Cleaver Ondine
  3. AU="Jordan A. Kreidberg"
  4. AU="Al-Marshoud, Majida"
  5. AU="David S Hui"
  6. AU="Manjappa, Shivaprasad"
  7. AU="Balkan, S"
  8. AU="Chen, Emma"
  9. AU="Delean, Ada"
  10. AU="Gurao, Ankita"
  11. AU="Lang, Zhen"
  12. AU="Mahnaz Mohammadpour"
  13. AU="Britta Grillitsch"
  14. AU=Hoeffner Ellen G
  15. AU="Al Harbi, Shmeylan"
  16. AU=Polevoda Bogdan
  17. AU="Raffaele Galiero"
  18. AU=Hruskova Z
  19. AU="Ayers, J"
  20. AU="Cohen, A D"
  21. AU="Brunetti, Gian Luca"
  22. AU=Andrade Daniel
  23. AU=Hay William W Jr

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  1. Artikel ; Online: Exploring the mechanisms underlying excitation/inhibition imbalance in human iPSC-derived models of ASD.

    Culotta, Lorenza / Penzes, Peter

    Molecular autism

    2020  Band 11, Heft 1, Seite(n) 32

    Abstract: Autism spectrum disorder (ASD) is a range of neurodevelopmental disorders characterized by impaired social interaction and communication, and repetitive or restricted behaviors. ASD subjects exhibit complex genetic and clinical heterogeneity, thus ... ...

    Abstract Autism spectrum disorder (ASD) is a range of neurodevelopmental disorders characterized by impaired social interaction and communication, and repetitive or restricted behaviors. ASD subjects exhibit complex genetic and clinical heterogeneity, thus hindering the discovery of pathophysiological mechanisms. Considering that several ASD-risk genes encode proteins involved in the regulation of synaptic plasticity, neuronal excitability, and neuronal connectivity, one hypothesis that has emerged is that ASD arises from a disruption of the neuronal network activity due to perturbation of the synaptic excitation and inhibition (E/I) balance. The development of induced pluripotent stem cell (iPSC) technology and recent advances in neuronal differentiation techniques provide a unique opportunity to model complex neuronal connectivity and to test the E/I hypothesis of ASD in human-based models. Here, we aim to review the latest advances in studying the different cellular and molecular mechanisms contributing to E/I balance using iPSC-based in vitro models of ASD.
    Mesh-Begriff(e) Autism Spectrum Disorder/diagnosis ; Autism Spectrum Disorder/etiology ; Autism Spectrum Disorder/metabolism ; Biomarkers ; Cell Differentiation ; Disease Susceptibility ; Electrophysiological Phenomena ; Genetic Predisposition to Disease ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Interneurons/metabolism ; Models, Biological ; Multigene Family ; Neuronal Plasticity ; Neurons/metabolism ; Phenotype
    Chemische Substanzen Biomarkers
    Sprache Englisch
    Erscheinungsdatum 2020-05-11
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2540930-X
    ISSN 2040-2392 ; 2040-2392
    ISSN (online) 2040-2392
    ISSN 2040-2392
    DOI 10.1186/s13229-020-00339-0
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: SULT4A1 Modulates Synaptic Development and Function by Promoting the Formation of PSD-95/NMDAR Complex.

    Culotta, Lorenza / Scalmani, Paolo / Vinci, Ersilia / Terragni, Benedetta / Sessa, Alessandro / Broccoli, Vania / Mantegazza, Massimo / Boeckers, Tobias / Verpelli, Chiara

    The Journal of neuroscience : the official journal of the Society for Neuroscience

    2020  Band 40, Heft 37, Seite(n) 7013–7026

    Abstract: Sulfotransferase 4A1 (SULT4A1) is a cytosolic sulfotransferase that is highly conserved across species and extensively expressed in the brain. However, the biological function of SULT4A1 is unclear. SULT4A1 has been implicated in several neuropsychiatric ...

    Abstract Sulfotransferase 4A1 (SULT4A1) is a cytosolic sulfotransferase that is highly conserved across species and extensively expressed in the brain. However, the biological function of SULT4A1 is unclear. SULT4A1 has been implicated in several neuropsychiatric disorders, such as Phelan-McDermid syndrome and schizophrenia. Here, we investigate the role of SULT4A1 within neuron development and function. Our data demonstrate that SULT4A1 modulates neuronal branching complexity and dendritic spines formation. Moreover, we show that SULT4A1, by negatively regulating the catalytic activity of Pin1 toward PSD-95, facilitates NMDAR synaptic expression and function. Finally, we demonstrate that the pharmacological inhibition of Pin1 reverses the pathologic phenotypes of neurons knocked down by SULT4A1 by specifically restoring dendritic spine density and rescuing NMDAR-mediated synaptic transmission. Together, these findings identify SULT4A1 as a novel player in neuron development and function by modulating dendritic morphology and synaptic activity.
    Mesh-Begriff(e) Animals ; Cells, Cultured ; Dendritic Spines/metabolism ; Disks Large Homolog 4 Protein/metabolism ; Female ; HEK293 Cells ; Humans ; Mice ; Mice, Inbred C57BL ; NIMA-Interacting Peptidylprolyl Isomerase/metabolism ; Neurogenesis ; Rats ; Receptors, N-Methyl-D-Aspartate/metabolism ; Sulfotransferases/genetics ; Sulfotransferases/metabolism ; Synapses/metabolism ; Synapses/physiology ; Synaptic Transmission
    Chemische Substanzen Disks Large Homolog 4 Protein ; Dlg4 protein, mouse ; NIMA-Interacting Peptidylprolyl Isomerase ; Receptors, N-Methyl-D-Aspartate ; Sulfotransferases (EC 2.8.2.-) ; Sult4a1 protein, mouse (EC 2.8.2.-) ; Pin1 protein, mouse (EC 5.2.1.8)
    Sprache Englisch
    Erscheinungsdatum 2020-08-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604637-x
    ISSN 1529-2401 ; 0270-6474
    ISSN (online) 1529-2401
    ISSN 0270-6474
    DOI 10.1523/JNEUROSCI.2194-19.2020
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Excitatory Dysfunction Drives Network and Calcium Handling Deficits in 16p11.2 Duplication Schizophrenia Induced Pluripotent Stem Cell-Derived Neurons.

    Parnell, Euan / Culotta, Lorenza / Forrest, Marc P / Jalloul, Hiba A / Eckman, Blair L / Loizzo, Daniel D / Horan, Katherine K E / Dos Santos, Marc / Piguel, Nicolas H / Tai, Derek J C / Zhang, Hanwen / Gertler, Tracy S / Simkin, Dina / Sanders, Alan R / Talkowski, Michael E / Gejman, Pablo V / Kiskinis, Evangelos / Duan, Jubao / Penzes, Peter

    Biological psychiatry

    2022  Band 94, Heft 2, Seite(n) 153–163

    Abstract: Background: Schizophrenia (SCZ) is a debilitating psychiatric disorder with a large genetic contribution; however, its neurodevelopmental substrates remain largely unknown. Modeling pathogenic processes in SCZ using human induced pluripotent stem cell- ... ...

    Abstract Background: Schizophrenia (SCZ) is a debilitating psychiatric disorder with a large genetic contribution; however, its neurodevelopmental substrates remain largely unknown. Modeling pathogenic processes in SCZ using human induced pluripotent stem cell-derived neurons (iNs) has emerged as a promising strategy. Copy number variants confer high genetic risk for SCZ, with duplication of the 16p11.2 locus increasing the risk 14.5-fold.
    Methods: To dissect the contribution of induced excitatory neurons (iENs) versus GABAergic (gamma-aminobutyric acidergic) neurons (iGNs) to SCZ pathophysiology, we induced iNs from CRISPR (clustered regularly interspaced short palindromic repeats)-Cas9 isogenic and SCZ patient-derived induced pluripotent stem cells and analyzed SCZ-related phenotypes in iEN monocultures and iEN/iGN cocultures.
    Results: In iEN/iGN cocultures, neuronal firing and synchrony were reduced at later, but not earlier, stages of in vitro development. These were fully recapitulated in iEN monocultures, indicating a primary role for iENs. Moreover, isogenic iENs showed reduced dendrite length and deficits in calcium handling. iENs from 16p11.2 duplication-carrying patients with SCZ displayed overlapping deficits in network synchrony, dendrite outgrowth, and calcium handling. Transcriptomic analysis of both iEN cohorts revealed molecular markers of disease related to the glutamatergic synapse, neuroarchitecture, and calcium regulation.
    Conclusions: Our results indicate the presence of 16p11.2 duplication-dependent alterations in SCZ patient-derived iENs. Transcriptomics and cellular phenotyping reveal overlap between isogenic and patient-derived iENs, suggesting a central role of glutamatergic, morphological, and calcium dysregulation in 16p11.2 duplication-mediated pathogenesis. Moreover, excitatory dysfunction during early neurodevelopment is implicated as the basis of SCZ pathogenesis in 16p11.2 duplication carriers. Our results support network synchrony and calcium handling as outcomes directly linked to this genetic risk variant.
    Mesh-Begriff(e) Humans ; Schizophrenia/genetics ; Schizophrenia/pathology ; Induced Pluripotent Stem Cells ; Calcium ; Neurons/pathology
    Chemische Substanzen Calcium (SY7Q814VUP)
    Sprache Englisch
    Erscheinungsdatum 2022-11-09
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 209434-4
    ISSN 1873-2402 ; 0006-3223
    ISSN (online) 1873-2402
    ISSN 0006-3223
    DOI 10.1016/j.biopsych.2022.11.005
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: Elongation factor-2 phosphorylation in dendrites and the regulation of dendritic mRNA translation in neurons.

    Heise, Christopher / Gardoni, Fabrizio / Culotta, Lorenza / di Luca, Monica / Verpelli, Chiara / Sala, Carlo

    Frontiers in cellular neuroscience

    2014  Band 8, Seite(n) 35

    Abstract: Neuronal activity results in long lasting changes in synaptic structure and function by regulating mRNA translation in dendrites. These activity dependent events yield the synthesis of proteins known to be important for synaptic modifications and diverse ...

    Abstract Neuronal activity results in long lasting changes in synaptic structure and function by regulating mRNA translation in dendrites. These activity dependent events yield the synthesis of proteins known to be important for synaptic modifications and diverse forms of synaptic plasticity. Worthy of note, there is accumulating evidence that the eukaryotic Elongation Factor 2 Kinase (eEF2K)/eukaryotic Elongation Factor 2 (eEF2) pathway may be strongly involved in this process. Upon activation, eEF2K phosphorylates and thereby inhibits eEF2, resulting in a dramatic reduction of mRNA translation. eEF2K is activated by elevated levels of calcium and binding of Calmodulin (CaM), hence its alternative name calcium/CaM-dependent protein kinase III (CaMKIII). In dendrites, this process depends on glutamate signaling and N-methyl-D-aspartate receptor (NMDAR) activation. Interestingly, it has been shown that eEF2K can be activated in dendrites by metabotropic glutamate receptor (mGluR) 1/5 signaling, as well. Therefore, neuronal activity can induce local proteomic changes at the postsynapse by altering eEF2K activity. Well-established targets of eEF2K in dendrites include brain-derived neurotrophic factor (BDNF), activity-regulated cytoskeletal-associated protein (Arc), the alpha subunit of calcium/CaM-dependent protein kinase II (αCaMKII), and microtubule-associated protein 1B (MAP1B), all of which have well-known functions in different forms of synaptic plasticity. In this review we will give an overview of the involvement of the eEF2K/eEF2 pathway at dendrites in regulating the translation of dendritic mRNA in the context of altered NMDAR- and neuronal activity, and diverse forms of synaptic plasticity, such as metabotropic glutamate receptor-dependent-long-term depression (mGluR-LTD). For this, we draw on studies carried out both in vitro and in vivo.
    Sprache Englisch
    Erscheinungsdatum 2014-02-10
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2452963-1
    ISSN 1662-5102
    ISSN 1662-5102
    DOI 10.3389/fncel.2014.00035
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Shed CNTNAP2 ectodomain is detectable in CSF and regulates Ca

    Martín-de-Saavedra, M Dolores / Dos Santos, Marc / Culotta, Lorenza / Varea, Olga / Spielman, Benjamin P / Parnell, Euan / Forrest, Marc P / Gao, Ruoqi / Yoon, Sehyoun / McCoig, Emmarose / Jalloul, Hiba A / Myczek, Kristoffer / Khalatyan, Natalia / Hall, Elizabeth A / Turk, Liam S / Sanz-Clemente, Antonio / Comoletti, Davide / Lichtenthaler, Stefan F / Burgdorf, Jeffrey S /
    Barbolina, Maria V / Savas, Jeffrey N / Penzes, Peter

    Neuron

    2021  Band 110, Heft 4, Seite(n) 627–643.e9

    Abstract: Although many neuronal membrane proteins undergo proteolytic cleavage, little is known about the biological significance of neuronal ectodomain shedding (ES). Here, we show that the neuronal sheddome is detectable in human cerebrospinal fluid (hCSF) and ... ...

    Abstract Although many neuronal membrane proteins undergo proteolytic cleavage, little is known about the biological significance of neuronal ectodomain shedding (ES). Here, we show that the neuronal sheddome is detectable in human cerebrospinal fluid (hCSF) and is enriched in neurodevelopmental disorder (NDD) risk factors. Among shed synaptic proteins is the ectodomain of CNTNAP2 (CNTNAP2-ecto), a prominent NDD risk factor. CNTNAP2 undergoes activity-dependent ES via MMP9 (matrix metalloprotease 9), and CNTNAP2-ecto levels are reduced in the hCSF of individuals with autism spectrum disorder. Using mass spectrometry, we identified the plasma membrane Ca
    Mesh-Begriff(e) Autism Spectrum Disorder/cerebrospinal fluid ; Autism Spectrum Disorder/genetics ; Autism Spectrum Disorder/metabolism ; Cell Membrane/metabolism ; Homeostasis ; Humans ; Membrane Proteins/metabolism ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Plasma Membrane Calcium-Transporting ATPases/cerebrospinal fluid ; Plasma Membrane Calcium-Transporting ATPases/genetics ; Plasma Membrane Calcium-Transporting ATPases/metabolism ; Signal Transduction
    Chemische Substanzen CNTNAP2 protein, human ; Membrane Proteins ; Nerve Tissue Proteins ; Plasma Membrane Calcium-Transporting ATPases (EC 3.6.3.8) ; ATP2B2 protein, human (EC 7.2.2.10)
    Sprache Englisch
    Erscheinungsdatum 2021-12-17
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 808167-0
    ISSN 1097-4199 ; 0896-6273
    ISSN (online) 1097-4199
    ISSN 0896-6273
    DOI 10.1016/j.neuron.2021.11.025
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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