Author, as appears in the article.: Obis T; Hurtado E; Nadal L; Tomàs M; Priego M; Simon A; Garcia N; Santafe M; Lanuza M; Tomàs J

Department: Ciències Mèdiques Bàsiques

URV's Author/s: Garcia Sancho, Maria de les Neus / HURTADO CABALLERO, ERICA / Lanuza Escolano, María Angel / NADAL MAGRIÑÀ, LAURA / Santafé Martínez, Manuel / SIMÓ OLLÉ, ANNA / Tomás Ferré, José Maria / Tomas Marginet, Marta

Keywords: Transmitter release Skeletal-muscle Signal-transduction pathway Protein kinase c Protein kinase a Presynaptic muscarinic autoreceptors Pkc-epsilon Pkc epsilon Pkc Neurotransmitter release Neurotransmission Neuromuscular junction Muscarinic receptors Motor nerve terminal Induced cell-death Electrical stimulation Ca2+ Ca 2+ Anchoring proteins Adult-rat Adenosine receptors Ach release Acetylcholine release

Abstract: © 2015 Obis et al. Background: Various protein kinase C (PKC) isoforms contribute to the phosphorylating activity that modulates neurotransmitter release. In previous studies we showed that nPKCε is confined in the presynaptic site of the neuromuscular junction and its presynaptic function is activity-dependent. Furthermore, nPKCε regulates phorbol ester-induced acetylcholine release potentiation, which further indicates that nPKCε is involved in neurotransmission. The present study is designed to examine the nPKCε involvement in transmitter release at the neuromuscular junction. Results: We use the specific nPKCε translocation inhibitor peptide εV1-2 and electrophysiological experiments to investigate the involvement of this isoform in acetylcholine release. We observed that nPKCε membrane translocation is key to the synaptic potentiation of NMJ, being involved in several conditions that upregulate PKC isoforms coupling to acetylcholine (ACh) release (incubation with high Ca2+, stimulation with phorbol esters and protein kinase A, stimulation with adenosine 3′,5′-cyclic monophosphorothioate, 8-Bromo-, Rp-isomer, sodium salt -Sp-8-BrcAMP-). In all these conditions, preincubation with the nPKCε translocation inhibitor peptide (εV1-2) impairs PKC coupling to acetylcholine release potentiation. In addition, the inhibition of nPKCε translocation and therefore its activity impedes that presynaptic muscarinic autoreceptors and adenosine autoreceptors modulate transmitter secretion. Conclusions: Together, these results point to the importance of nPKCε isoform in the control of acetylcholine release in the neuromuscular junction.

Thematic Areas: Psicología Neurosciences Molecular biology Interdisciplinar Ciências biológicas ii Cellular and molecular neuroscience

licence for use: https://creativecommons.org/licenses/by/3.0/es/

Author's mail: marta.tomas@urv.cat manuel.santafe@urv.cat mariaangel.lanuza@urv.cat josepmaria.tomas@urv.cat

Author identifier: 0000-0002-4151-1697 0000-0002-5462-5108 0000-0003-4795-4103 0000-0002-0406-0006

Record's date: 2023-03-11

Papper version: info:eu-repo/semantics/publishedVersion

Link to the original source: https://molecularbrain.biomedcentral.com/articles/10.1186/s13041-015-0171-5

Licence document URL: http://repositori.urv.cat/ca/proteccio-de-dades/

Papper original source: Molecular Brain. 8 (1):

APA: Obis T; Hurtado E; Nadal L; Tomàs M; Priego M; Simon A; Garcia N; Santafe M; Lanuza M; Tomàs J (2015). The novel protein kinase C epsilon isoform modulates acetylcholine release in the rat neuromuscular junction. Molecular Brain, 8(1), -. DOI: 10.1186/s13041-015-0171-5

Article's DOI: 10.1186/s13041-015-0171-5

Entity: Universitat Rovira i Virgili

Journal publication year: 2015

Publication Type: Journal Publications