Mechanical stimulation of C2C12 cells increases m-calpain expression, focal adhesion plaque protein degradation
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Mechanical stimulation of C2C12 cells increases m-calpain expression, focal adhesion plaque protein degradation. / Grossi, Alberto; Karlsson, Anders H; Lawson, Moira Ann.
In: Cell Biology International, Vol. 32, No. 6, 2008, p. 615-622.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Mechanical stimulation of C2C12 cells increases m-calpain expression, focal adhesion plaque protein degradation
AU - Grossi, Alberto
AU - Karlsson, Anders H
AU - Lawson, Moira Ann
N1 - Keywords: Animals; Calpain; Cell Line; Cell Membrane; Focal Adhesions; Mechanotransduction, Cellular; Mice; Myoblasts; Paxillin; Talin
PY - 2008
Y1 - 2008
N2 - Myogenesis is a complex sequence of events, including the irreversible transition from the proliferation-competent myoblast stage into fused, multinucleated myotubes. During embryonic development, myogenic differentiation is regulated by positive and negative signals from surrounding tissues. Stimulation due to stretch- or load-induced signaling is now beginning to be understood as a factor which affects gene sequences, protein synthesis and an increase in Ca2+ influx in myocytes. Evidence of the involvement of Ca2+ -dependent activity in myoblast fusion, cell membrane and cytoskeleton component reorganization due to the activity of the ubiquitous proteolytic enzymes, calpains, has been reported. Whether there is a link between stretch- or load-induced signaling and calpain expression and activation is not known. Using a magnetic bead stimulation assay and C2C12 mouse myoblasts cell population, we have demonstrated that mechanical stimulation via laminin receptors leads to an increase in m-calpain expression, but no increase in the expression of other calpain isoforms. Our study revealed that after a short period of stimulation, m-calpain relocates into focal adhesion complexes and is followed by a breakdown of specific focal adhesion proteins previously identified as substrates for this enzyme. We show that stimulation also leads to an increase in calpain activity in these cells. These data support the pivotal role for m-calpain in the control of muscle precursor cell differentiation and thus strengthen the idea of its implication during the initial events of muscle development.
AB - Myogenesis is a complex sequence of events, including the irreversible transition from the proliferation-competent myoblast stage into fused, multinucleated myotubes. During embryonic development, myogenic differentiation is regulated by positive and negative signals from surrounding tissues. Stimulation due to stretch- or load-induced signaling is now beginning to be understood as a factor which affects gene sequences, protein synthesis and an increase in Ca2+ influx in myocytes. Evidence of the involvement of Ca2+ -dependent activity in myoblast fusion, cell membrane and cytoskeleton component reorganization due to the activity of the ubiquitous proteolytic enzymes, calpains, has been reported. Whether there is a link between stretch- or load-induced signaling and calpain expression and activation is not known. Using a magnetic bead stimulation assay and C2C12 mouse myoblasts cell population, we have demonstrated that mechanical stimulation via laminin receptors leads to an increase in m-calpain expression, but no increase in the expression of other calpain isoforms. Our study revealed that after a short period of stimulation, m-calpain relocates into focal adhesion complexes and is followed by a breakdown of specific focal adhesion proteins previously identified as substrates for this enzyme. We show that stimulation also leads to an increase in calpain activity in these cells. These data support the pivotal role for m-calpain in the control of muscle precursor cell differentiation and thus strengthen the idea of its implication during the initial events of muscle development.
U2 - 10.1016/j.cellbi.2008.01.005
DO - 10.1016/j.cellbi.2008.01.005
M3 - Journal article
C2 - 18299214
VL - 32
SP - 615
EP - 622
JO - Cell Biology International
JF - Cell Biology International
SN - 1065-6995
IS - 6
ER -
ID: 5240945