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Nitric oxide synthase inhibition prevents activity‐induced calcineurin–NFATc1 signalling and fast‐to‐slow skeletal muscle fibre type conversions
Author(s) -
Martins Karen J. B.,
StLouis Mathieu,
Murdoch Gordon K.,
MacLean Ian M.,
McDonald Pamela,
Dixon Walter T.,
Putman Charles T.,
Michel Robin N.
Publication year - 2012
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.223370
Subject(s) - calcineurin , nitric oxide , nitric oxide synthase , chemistry , skeletal muscle , signalling , microbiology and biotechnology , biophysics , biochemistry , medicine , endocrinology , biology , transplantation , organic chemistry
Key points • Exercise is known to trigger skeletal muscle structural and functional adaptations. • Control of these adaptive alterations is a complex process involving multiple signalling pathways and levels of regulation. • The well‐characterized calcineurin–nuclear factor of activated T‐cells (NFATc1) signalling pathway is involved in the regulation of activity‐dependent alterations in skeletal muscle myosin heavy chain expression. Myosin heavy chain is a contractile protein that largely dictates a muscle's speed of contraction. • We show that a signalling molecule called nitric oxide may be regulating alterations in myosin heavy chain expression via activity‐modulated calcineurin–NFATc1 signalling. • These findings increase our understanding of how skeletal muscle adaptive alterations are regulated.