LIVIVO - Das Suchportal für Lebenswissenschaften

switch to English language
Erweiterte Suche

Ihre letzten Suchen

  1. AU="Carey, Alanna"
  2. AU="Habash, Khader I"
  3. AU="Angela Ribeiro"
  4. AU="Radomir Živadinović"
  5. AU=Shakeri Ahmad

Suchergebnis

Treffer 1 - 3 von insgesamt 3

Suchoptionen

  1. Artikel: PERIRHINAL CORTEX LEARNS A PREDICTIVE MAP (INTERNAL MODEL) OF THE TASK ENVIRONMENT.

    Lee, David G / McLachlan, Caroline A / Nogueira, Ramon / Kwon, Osung / Carey, Alanna E / House, Garrett / Lagani, Gavin D / LaMay, Danielle / Fusi, Stefano / Chen, Jerry L

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Goal-directed tasks involve acquiring an internal model, known as a predictive map, of relevant stimuli and associated outcomes to guide behavior. Here, we identified neural signatures of a predictive map of task behavior in perirhinal cortex (Prh). Mice ...

    Abstract Goal-directed tasks involve acquiring an internal model, known as a predictive map, of relevant stimuli and associated outcomes to guide behavior. Here, we identified neural signatures of a predictive map of task behavior in perirhinal cortex (Prh). Mice learned to perform a tactile working memory task by classifying sequential whisker stimuli over multiple training stages. Chemogenetic inactivation demonstrated that Prh is involved in task learning. Chronic two-photon calcium imaging, population analysis, and computational modeling revealed that Prh encodes stimulus features as sensory prediction errors. Prh forms stable stimulus-outcome associations that expand in a retrospective manner and generalize as animals learn new contingencies. Stimulus-outcome associations are linked to prospective network activity encoding possible expected outcomes. This link is mediated by cholinergic signaling to guide task performance, demonstrated by acetylcholine imaging and perturbation. We propose that Prh combines error-driven and map-like properties to acquire a predictive map of learned task behavior.
    Sprache Englisch
    Erscheinungsdatum 2023-04-10
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.03.17.532214
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  2. Artikel ; Online: CSMD1 regulates brain complement activity and circuit development.

    Baum, Matthew L / Wilton, Daniel K / Fox, Rachel G / Carey, Alanna / Hsu, Yu-Han H / Hu, Ruilong / Jäntti, Henna J / Fahey, Jaclyn B / Muthukumar, Allie K / Salla, Nikkita / Crotty, William / Scott-Hewitt, Nicole / Bien, Elizabeth / Sabatini, David A / Lanser, Toby B / Frouin, Arnaud / Gergits, Frederick / Håvik, Bjarte / Gialeli, Chrysostomi /
    Nacu, Eugene / Lage, Kasper / Blom, Anna M / Eggan, Kevin / McCarroll, Steven A / Johnson, Matthew B / Stevens, Beth

    Brain, behavior, and immunity

    2024  Band 119, Seite(n) 317–332

    Abstract: Complement proteins facilitate synaptic elimination during neurodevelopmental pruning, but neural complement regulation is not well understood. CUB and Sushi Multiple Domains 1 (CSMD1) can regulate complement activity in vitro, is expressed in the brain, ...

    Abstract Complement proteins facilitate synaptic elimination during neurodevelopmental pruning, but neural complement regulation is not well understood. CUB and Sushi Multiple Domains 1 (CSMD1) can regulate complement activity in vitro, is expressed in the brain, and is associated with increased schizophrenia risk. Beyond this, little is known about CSMD1 including whether it regulates complement activity in the brain or otherwise plays a role in neurodevelopment. We used biochemical, immunohistochemical, and proteomic techniques to examine the regional, cellular, and subcellular distribution as well as protein interactions of CSMD1 in the brain. To evaluate whether CSMD1 is involved in complement-mediated synapse elimination, we examined Csmd1-knockout mice and CSMD1-knockout human stem cell-derived neurons. We interrogated synapse and circuit development of the mouse visual thalamus, a process that involves complement pathway activity. We also quantified complement deposition on synapses in mouse visual thalamus and on cultured human neurons. Finally, we assessed uptake of synaptosomes by cultured microglia. We found that CSMD1 is present at synapses and interacts with complement proteins in the brain. Mice lacking Csmd1 displayed increased levels of complement component C3, an increased colocalization of C3 with presynaptic terminals, fewer retinogeniculate synapses, and aberrant segregation of eye-specific retinal inputs to the visual thalamus during the critical period of complement-dependent refinement of this circuit. Loss of CSMD1 in vivo enhanced synaptosome engulfment by microglia in vitro, and this effect was dependent on activity of the microglial complement receptor, CR3. Finally, human stem cell-derived neurons lacking CSMD1 were more vulnerable to complement deposition. These data suggest that CSMD1 can function as a regulator of complement-mediated synapse elimination in the brain during development.
    Sprache Englisch
    Erscheinungsdatum 2024-03-27
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 639219-2
    ISSN 1090-2139 ; 0889-1591
    ISSN (online) 1090-2139
    ISSN 0889-1591
    DOI 10.1016/j.bbi.2024.03.041
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  3. Artikel ; Online: Local externalization of phosphatidylserine mediates developmental synaptic pruning by microglia.

    Scott-Hewitt, Nicole / Perrucci, Fabio / Morini, Raffaella / Erreni, Marco / Mahoney, Matthew / Witkowska, Agata / Carey, Alanna / Faggiani, Elisa / Schuetz, Lisa Theresia / Mason, Sydney / Tamborini, Matteo / Bizzotto, Matteo / Passoni, Lorena / Filipello, Fabia / Jahn, Reinhard / Stevens, Beth / Matteoli, Michela

    The EMBO journal

    2020  Band 39, Heft 16, Seite(n) e105380

    Abstract: Neuronal circuit assembly requires the fine balance between synapse formation and elimination. Microglia, through the elimination of supernumerary synapses, have an established role in this process. While the microglial receptor TREM2 and the soluble ... ...

    Abstract Neuronal circuit assembly requires the fine balance between synapse formation and elimination. Microglia, through the elimination of supernumerary synapses, have an established role in this process. While the microglial receptor TREM2 and the soluble complement proteins C1q and C3 are recognized as key players, the neuronal molecular components that specify synapses to be eliminated are still undefined. Here, we show that exposed phosphatidylserine (PS) represents a neuronal "eat-me" signal involved in microglial-mediated pruning. In hippocampal neuron and microglia co-cultures, synapse elimination can be partially prevented by blocking accessibility of exposed PS using Annexin V or through microglial loss of TREM2. In vivo, PS exposure at both hippocampal and retinogeniculate synapses and engulfment of PS-labeled material by microglia occurs during established developmental periods of microglial-mediated synapse elimination. Mice deficient in C1q, which fail to properly refine retinogeniculate connections, have elevated presynaptic PS exposure and reduced PS engulfment by microglia. These data provide mechanistic insight into microglial-mediated synapse pruning and identify a novel role of developmentally regulated neuronal PS exposure that is common among developing brain structures.
    Mesh-Begriff(e) Animals ; Coculture Techniques ; Complement C1q/genetics ; Complement C1q/metabolism ; Complement C3/genetics ; Complement C3/metabolism ; Hippocampus/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Knockout ; Microglia/metabolism ; Neurons/metabolism ; Phosphatidylserines/genetics ; Phosphatidylserines/metabolism ; Receptors, Immunologic/genetics ; Receptors, Immunologic/metabolism ; Synapses/genetics ; Synapses/metabolism
    Chemische Substanzen Complement C3 ; Membrane Glycoproteins ; Phosphatidylserines ; Receptors, Immunologic ; Trem2 protein, mouse ; Complement C1q (80295-33-6)
    Sprache Englisch
    Erscheinungsdatum 2020-07-13
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2020105380
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

Zum Seitenanfang