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  1. Article ; Online: Autocrine activation of P2X7 receptors mediates catecholamine secretion in chromaffin cells.

    Maldifassi, María Constanza / Guerra-Fernández, María José / Ponce, Daniela / Alfonso-Bueno, Samuel / Maripillán, Jaime / Vielma, Alex H / Báez-Matus, Ximena / Marengo, Fernando D / Acuña-Castillo, Claudio / Sáez, Juan C / Martínez, Agustín D / Cárdenas, Ana M

    British journal of pharmacology

    2024  

    Abstract: Background and purpose: ATP is highly accumulated in secretory vesicles and secreted upon exocytosis from neurons and endocrine cells. In adrenal chromaffin granules, intraluminal ATP reaches concentrations over 100 mM. However, how these large amounts ... ...

    Abstract Background and purpose: ATP is highly accumulated in secretory vesicles and secreted upon exocytosis from neurons and endocrine cells. In adrenal chromaffin granules, intraluminal ATP reaches concentrations over 100 mM. However, how these large amounts of ATP contribute to exocytosis has not been investigated.
    Experimental approach: Exocytotic events in bovine and mouse adrenal chromaffin cells were measured with single cell amperometry. Cytosolic Ca
    Key results: ATP induced exocytosis in chromaffin cells, whereas the ectonucleotidase apyrase reduced the release events induced by the nicotinic agonist dimethylphenylpiperazinium (DMPP), high KCl, or ionomycin. The purinergic agonist BzATP also promoted a secretory response that was dependent on extracellular Ca
    Conclusion and implications: Autocrine activation of P2X7 receptors constitutes a crucial feedback system that amplifies the secretion of catecholamines in chromaffin cells by favouring submembrane Ca
    Language English
    Publishing date 2024-04-28
    Publishing country England
    Document type Journal Article
    ZDB-ID 80081-8
    ISSN 1476-5381 ; 0007-1188
    ISSN (online) 1476-5381
    ISSN 0007-1188
    DOI 10.1111/bph.16371
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uf I Zs.146: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: A centronuclear myopathy-causing mutation in dynamin-2 disrupts neuronal morphology and excitatory synaptic transmission in a murine model of the disease.

    Arriagada-Diaz, Jorge / Flores-Muñoz, Carolina / Gómez-Soto, Bárbara / Labraña-Allende, Marjorie / Mattar-Araos, Michelle / Prado-Vega, Lorena / Hinostroza, Fernando / Gajardo, Ivana / Guerra-Fernández, María José / Bevilacqua, Jorge A / Cárdenas, Ana M / Bitoun, Marc / Ardiles, Alvaro O / Gonzalez-Jamett, Arlek M

    Neuropathology and applied neurobiology

    2023  Volume 49, Issue 4, Page(s) e12918

    Abstract: Aims: Dynamin-2 is a large GTPase, a member of the dynamin superfamily that regulates membrane remodelling and cytoskeleton dynamics. Mutations in the dynamin-2 gene (DNM2) cause autosomal dominant centronuclear myopathy (CNM), a congenital ... ...

    Abstract Aims: Dynamin-2 is a large GTPase, a member of the dynamin superfamily that regulates membrane remodelling and cytoskeleton dynamics. Mutations in the dynamin-2 gene (DNM2) cause autosomal dominant centronuclear myopathy (CNM), a congenital neuromuscular disorder characterised by progressive weakness and atrophy of the skeletal muscles. Cognitive defects have been reported in some DNM2-linked CNM patients suggesting that these mutations can also affect the central nervous system (CNS). Here we studied how a dynamin-2 CNM-causing mutation influences the CNS function.
    Methods: Heterozygous mice harbouring the p.R465W mutation in the dynamin-2 gene (HTZ), the most common causing autosomal dominant CNM, were used as disease model. We evaluated dendritic arborisation and spine density in hippocampal cultured neurons, analysed excitatory synaptic transmission by electrophysiological field recordings in hippocampal slices, and evaluated cognitive function by performing behavioural tests.
    Results: HTZ hippocampal neurons exhibited reduced dendritic arborisation and lower spine density than WT neurons, which was reversed by transfecting an interference RNA against the dynamin-2 mutant allele. Additionally, HTZ mice showed defective hippocampal excitatory synaptic transmission and reduced recognition memory compared to the WT condition.
    Conclusion: Our findings suggest that the dynamin-2 p.R465W mutation perturbs the synaptic and cognitive function in a CNM mouse model and support the idea that this GTPase plays a key role in regulating neuronal morphology and excitatory synaptic transmission in the hippocampus.
    MeSH term(s) Animals ; Mice ; Disease Models, Animal ; Dynamin II/genetics ; Dynamin II/metabolism ; Muscle, Skeletal/metabolism ; Mutation ; Myopathies, Structural, Congenital/genetics ; Neurons/metabolism ; Synaptic Transmission
    Chemical Substances Dynamin II (EC 3.6.5.5) ; DNM2 protein, mouse (EC 3.6.5.5)
    Language English
    Publishing date 2023-04-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80371-6
    ISSN 1365-2990 ; 0305-1846
    ISSN (online) 1365-2990
    ISSN 0305-1846
    DOI 10.1111/nan.12918
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1241: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Gain-of-Function Dynamin-2 Mutations Linked to Centronuclear Myopathy Impair Ca

    Bayonés, Lucas / Guerra-Fernández, María José / Hinostroza, Fernando / Báez-Matus, Ximena / Vásquez-Navarrete, Jacqueline / Gallo, Luciana I / Parra, Sergio / Martínez, Agustín D / González-Jamett, Arlek / Marengo, Fernando D / Cárdenas, Ana M

    International journal of molecular sciences

    2022  Volume 23, Issue 18

    Abstract: Gain-of-function mutations of dynamin-2, a mechano-GTPase that remodels membrane and actin filaments, cause centronuclear myopathy (CNM), a congenital disease that mainly affects skeletal muscle tissue. Among these mutations, the variants p.A618T and p ... ...

    Abstract Gain-of-function mutations of dynamin-2, a mechano-GTPase that remodels membrane and actin filaments, cause centronuclear myopathy (CNM), a congenital disease that mainly affects skeletal muscle tissue. Among these mutations, the variants p.A618T and p.S619L lead to a gain of function and cause a severe neonatal phenotype. By using total internal reflection fluorescence microscopy (TIRFM) in immortalized human myoblasts expressing the pH-sensitive fluorescent protein (pHluorin) fused to the insulin-responsive aminopeptidase IRAP as a reporter of the GLUT4 vesicle trafficking, we measured single pHluorin signals to investigate how p.A618T and p.S619L mutations influence exocytosis. We show here that both dynamin-2 mutations significantly reduced the number and durations of pHluorin signals induced by 10 μM ionomycin, indicating that in addition to impairing exocytosis, they also affect the fusion pore dynamics. These mutations also disrupt the formation of actin filaments, a process that reportedly favors exocytosis. This altered exocytosis might importantly disturb the plasmalemma expression of functional proteins such as the glucose transporter GLUT4 in skeletal muscle cells, impacting the physiology of the skeletal muscle tissue and contributing to the CNM disease.
    MeSH term(s) Dynamin II/genetics ; Dynamin II/metabolism ; Exocytosis ; Gain of Function Mutation ; Glucose Transport Proteins, Facilitative/metabolism ; Humans ; Ionomycin ; Muscle, Skeletal/metabolism ; Mutation ; Myoblasts/metabolism ; Myopathies, Structural, Congenital/metabolism
    Chemical Substances Glucose Transport Proteins, Facilitative ; Ionomycin (56092-81-0) ; Dynamin II (EC 3.6.5.5)
    Language English
    Publishing date 2022-09-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms231810363
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Dynamin-2 mutations linked to Centronuclear Myopathy impair actin-dependent trafficking in muscle cells.

    González-Jamett, Arlek M / Baez-Matus, Ximena / Olivares, María José / Hinostroza, Fernando / Guerra-Fernández, Maria José / Vasquez-Navarrete, Jacqueline / Bui, Mai Thao / Guicheney, Pascale / Romero, Norma Beatriz / Bevilacqua, Jorge A / Bitoun, Marc / Caviedes, Pablo / Cárdenas, Ana M

    Scientific reports

    2017  Volume 7, Issue 1, Page(s) 4580

    Abstract: Dynamin-2 is a ubiquitously expressed GTP-ase that mediates membrane remodeling. Recent findings indicate that dynamin-2 also regulates actin dynamics. Mutations in dynamin-2 cause dominant centronuclear myopathy (CNM), a congenital myopathy ... ...

    Abstract Dynamin-2 is a ubiquitously expressed GTP-ase that mediates membrane remodeling. Recent findings indicate that dynamin-2 also regulates actin dynamics. Mutations in dynamin-2 cause dominant centronuclear myopathy (CNM), a congenital myopathy characterized by progressive weakness and atrophy of skeletal muscles. However, the muscle-specific roles of dynamin-2 affected by these mutations remain elusive. Here we show that, in muscle cells, the GTP-ase activity of dynamin-2 is involved in de novo actin polymerization as well as in actin-mediated trafficking of the glucose transporter GLUT4. Expression of dynamin-2 constructs carrying CNM-linked mutations disrupted the formation of new actin filaments as well as the stimulus-induced translocation of GLUT4 to the plasma membrane. Similarly, mature muscle fibers isolated from heterozygous knock-in mice that harbor the dynamin-2 mutation p.R465W, an animal model of CNM, exhibited altered actin organization, reduced actin polymerization and impaired insulin-induced translocation of GLUT4 to the sarcolemma. Moreover, GLUT4 displayed aberrant perinuclear accumulation in biopsies from CNM patients carrying dynamin-2 mutations, further suggesting trafficking defects. These results suggest that dynamin-2 is a key regulator of actin dynamics and GLUT4 trafficking in muscle cells. Our findings also support a model in which impairment of actin-dependent trafficking contributes to the pathological mechanism in dynamin-2-associated CNM.
    MeSH term(s) Actins/chemistry ; Actins/metabolism ; Animals ; Disease Models, Animal ; Dynamin II/genetics ; Dynamin II/metabolism ; Enzyme Activation ; Gene Expression ; Genetic Association Studies ; Genetic Predisposition to Disease ; Glucose Transporter Type 4/metabolism ; Humans ; Mice ; Muscle Cells/metabolism ; Mutation ; Myoblasts/metabolism ; Myopathies, Structural, Congenital/genetics ; Myopathies, Structural, Congenital/metabolism ; Myopathies, Structural, Congenital/pathology ; Protein Binding ; Protein Multimerization ; Protein Transport
    Chemical Substances Actins ; Glucose Transporter Type 4 ; Dynamin II (EC 3.6.5.5)
    Language English
    Publishing date 2017-07-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-04418-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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