Analysis of Ca(2+) signaling mechanisms - our experience on the intercellular communication in muscle remodeling.


Journal

Physiological research
ISSN: 1802-9973
Titre abrégé: Physiol Res
Pays: Czech Republic
ID NLM: 9112413

Informations de publication

Date de publication:
30 04 2019
Historique:
pubmed: 11 1 2019
medline: 26 11 2019
entrez: 11 1 2019
Statut: ppublish

Résumé

The aim of this study was to evaluate cell diversity by considering how Ca(2+) signaling has been adapted in skeletal muscle cell function. We characterized single C2C12 myoblasts through intracellular Ca(2+) 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 Ca(2+)-ATPase pump. These results suggest that C2C12 cells possess functional L- and P/Q-type voltage-operated Ca(2+) channels, ryanodine receptors and functional sarcoplasmic reticulumCa(2+) stores (typical for muscle cells), adenosine and P2 purinergic receptors, as well as ionotropic glutamate receptors. The evaluation of intracellular Ca(2+) 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.

Identifiants

pubmed: 30628838
pii: 934082
doi: 10.33549/physiolres.934082

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

325-328

Auteurs

S Filip (S)

Charles University, Faculty of Medicine, Dept. of Oncology and Radiotherapy, Hradec Králové, Czech Republic. filip@fnhk.cz.

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Classifications MeSH