The aim of this study was to evaluate cell diversity by considering
how Ca2+ signaling has been adapted in skeletal muscle cell
function. We characterized single C2C12 myoblasts through
intracellular Ca2+ signaling kinetics after exposure to specific
drugs and calcium blockers using fast fluorescence
microspectrofluorimetry followed by ATP effect analysis, which
confirmed the expression of functional purinergic adenosine and
P2 receptors. Further, we found that glutamate sensitivity of
C2C12 cells was mediated by ionotropic glutamate receptors; on
the other hand, most cells were responsive to cyclopiazonic acid,
which inhibits the sarco-endoplasmic reticulum Ca2+-ATPase
pump. These results suggest that C2C12 cells possess functional
L- and P/Q-type voltage-operated Ca2+ channels, ryanodine
receptors and functional sarcoplasmic reticulum Ca2+ stores
(typical for muscle cells), adenosine and P2 purinergic receptors,
as well as ionotropic glutamate receptors. The evaluation of
intracellular Ca2+ signaling is a promising approach towards
a better understanding and control of the physiopathological
properties of myogenic cells that could be used as a predictive
factor in the selection of optimal cells for scaffold recellularization
or for tissue engineered constructs used in stem cell therapy.