Autor según el artículo: Obis T; Besalduch N; Hurtado E; Nadal L; Santafe M; Garcia N; Tomàs M; Priego M; Lanuza M; Tomàs J
Departamento: Ciències Mèdiques Bàsiques
Autor/es de la URV: BESALDUCH CANES, NÚRIA MONTSERRAT / García Gutiérrez, Nerea / Garcia Sancho, Maria de les Neus / Hurtado Caballero, Erica / Lanuza Escolano, María Angel / NADAL MAGRIÑÀ, LAURA / PRIEGO LUQUE, MERCEDES / Santafé Martínez, Manuel / Tomás Ferré, José Maria / Tomas Marginet, Marta / TOMÀS ROIG, JORDI
Palabras clave: Trkb Substrate phosphorylation Rat skeletal-muscle Pkc epsilon Pkc Phorbol esters Neurotrophic factor Neurotransmitter release Neurotransmission Neuromuscular junction Nerve-terminals Muscle contraction Muscarinic autoreceptors Modulate transmitter release Immunofluorescence Electrical stimulation Calcium-channels Anchoring proteins
Resumen: © 2015 Obis et al.; licensee BioMed Central. Background: Protein kinase C (PKC) regulates a variety of neural functions, including neurotransmitter release. Although various PKC isoforms can be expressed at the synaptic sites and specific cell distribution may contribute to their functional diversity, little is known about the isoform-specific functions of PKCs in neuromuscular synapse. The present study is designed to examine the location of the novel isoform nPKCε at the neuromuscular junction (NMJ), their synaptic activity-related expression changes, its regulation by muscle contraction, and their possible involvement in acetylcholine release. Results: We use immunohistochemistry and confocal microscopy to demonstrate that the novel isoform nPKCε is exclusively located in the motor nerve terminals of the adult rat NMJ. We also report that electrical stimulation of synaptic inputs to the skeletal muscle significantly increased the amount of nPKCε isoform as well as its phosphorylated form in the synaptic membrane, and muscle contraction is necessary for these nPKCε expression changes. The results also demonstrate that synaptic activity-induced muscle contraction promotes changes in presynaptic nPKCε through the brain-derived neurotrophic factor (BDNF)-mediated tyrosine kinase receptor B (TrkB) signaling. Moreover, nPKCε activity results in phosphorylation of the substrate MARCKS involved in actin cytoskeleton remodeling and related with neurotransmission. Finally, blocking nPKCε with a nPKCε-specific translocation inhibitor peptide (εV1-2) strongly reduces phorbol ester-induced ACh release potentiation, which further indicates that nPKCε is involved in neurotransmission. Conclusions: Together, these results provide a mechanistic insight into how synaptic activity-induced muscle contraction could regulate the presynaptic action of the nPKCε isoform and suggest that muscle contraction is an important regulatory step in TrkB signaling at the NMJ.
Áreas temáticas: Psicología Neurosciences Molecular biology Interdisciplinar Ciências biológicas ii Cellular and molecular neuroscience
Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/
ISSN: 17566606
Direcció de correo del autor: marta.tomas@urv.cat erica.hurtado@urv.cat nerea.garciagu@estudiants.urv.cat josepmaria.tomas@urv.cat mariaangel.lanuza@urv.cat manuel.santafe@urv.cat
Identificador del autor: 0000-0002-4151-1697 0000-0002-0406-0006 0000-0003-4795-4103 0000-0002-5462-5108
Fecha de alta del registro: 2024-10-05
Versión del articulo depositado: info:eu-repo/semantics/publishedVersion
URL Documento de licencia: https://repositori.urv.cat/ca/proteccio-de-dades/
Referencia al articulo segun fuente origial: Molecular Brain. 8 (1):
Referencia de l'ítem segons les normes APA: Obis T; Besalduch N; Hurtado E; Nadal L; Santafe M; Garcia N; Tomàs M; Priego M; Lanuza M; Tomàs J (2015). The novel protein kinase C epsilon isoform at the adult neuromuscular synapse: Location, regulation by synaptic activity-dependent muscle contraction through TrkB signaling and coupling to ACh release. Molecular Brain, 8(1), -. DOI: 10.1186/s13041-015-0098-x
Entidad: Universitat Rovira i Virgili
Año de publicación de la revista: 2015
Tipo de publicación: Journal Publications
Repositori URV