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J Biol Chem, Vol. 274, Issue 46, 33155-33160, November 12, 1999
From the Department of Physiological Science, University of
California, Los Angeles, California 90095-1527
Mechanical stimuli can cause changes in muscle
mass and structure which indicate that mechanisms exist for transducing
mechanical stimuli into signals that influence gene expression.
Myotendinous junctions show adaptations to modified muscle loading
which suggest that these are transcriptionally distinct domains in
muscle fibers that may experience local regulation of expression of
structural proteins that are concentrated at these sites. Vinculin and
talin are cytoskeletal proteins that are highly enriched at
myotendinous junctions that we hypothesize to be subject to local
transcriptional regulation. Our findings show that mechanical
stimulation of muscle cells in vivo and in
vitro causes an increase in the expression of vinculin and talin
that is mediated by nitric oxide. Furthermore, nitric oxide-stimulated
increases in vinculin and talin expression occur through a protein
kinase G-dependent pathway and therefore differ from other
mechanisms through which nitric oxide has been shown previously to
modulate transcription. Analysis of vinculin mRNA distribution in
mechanically stimulated muscle fibers shows that the mRNA is highly
concentrated at myotendinous junctions, which supports the hypothesis
that myotendinous junctions are distinct domains in which the
expression of cytoskeletal proteins is modulated by mechanical stimuli
through a nitric oxide and protein kinase G-dependent pathway.
Nitric-oxide Synthase Is a Mechanical Signal Transducer That
Modulates Talin and Vinculin Expression
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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