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Synaptic activity‐related classical protein kinase C isoform localization in the adult rat neuromuscular synapse
Author(s) -
Besalduch Núria,
Tomàs Marta,
Santafé Manel M.,
Garcia Neus,
Tomàs Josep,
Lanuza Maria Angel
Publication year - 2009
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/cne.22220
Subject(s) - biology , neuromuscular junction , protein kinase c , postsynaptic potential , microbiology and biotechnology , stimulation , myocyte , neuroscience , synapse , muscle contraction , signal transduction , endocrinology , biochemistry , receptor
Protein kinase C (PKC) is essential for signal transduction in a variety of cells, including neurons and myocytes, and is involved in both acetylcholine release and muscle fiber contraction. Here, we demonstrate that the increases in synaptic activity by nerve stimulation couple PKC to transmitter release in the rat neuromuscular junction and increase the level of α, βI, and βII isoforms in the membrane when muscle contraction follows the stimulation. The phosphorylation activity of these classical PKCs also increases. It seems that the muscle has to contract in order to maintain or increase classical PKCs in the membrane. We use immunohistochemistry to show that PKCα and PKCβI were located in the nerve terminals, whereas PKCα and PKCβII were located in the postsynaptic and the Schwann cells. Stimulation and contraction do not change these cellular distributions, but our results show that the localization of classical PKC isoforms in the membrane is affected by synaptic activity. J. Comp. Neurol. 518:211–228, 2010. © 2009 Wiley‐Liss, Inc.