| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2190742 | Journal of Molecular and Cellular Cardiology | 2011 | 7 Pages |
In the neonatal mammalian heart, the role of ryanodine receptor (= Ca2+ release channel)-mediated sarcoplasmic reticulum (SR) Ca2+ release for excitation–contraction coupling is still a matter of debate. Using an adenoviral system, we overexpressed separately the junctional SR proteins triadin, junctin, and calsequestrin, which are probably involved in regulation of ryanodine receptor function. Infection of neonatal rat cardiac myocytes with triadin, junctin, or calsequestrin viruses, controlled by green fluorescent protein expression, resulted in an increased protein level of the corresponding transgenes. Measurement of Ca2+ transients of infected cardiac myocytes revealed unchanged peak amplitudes under basal conditions but with overexpression of calsequestrin and triadin caffeine-releasable SR Ca2+ content was increased. Our results demonstrate that an increased expression of triadin or calsequestrin is associated with an increased SR Ca2+ storage but unchanged Ca2+ signaling in neonatal rat cardiac myocytes. This is consistent with an ancillary role of the sarcoplasmic reticulum in excitation–contraction coupling in the developing mammalian heart.
► Overexpression of triadin, junctin and calsequestrin in neonatal rat cardiomyocytes. ► Basal Ca2+ transients were unchanged in infected cardiomyocytes. ► Caffeine-releasable SR Ca2+ content was increased by calsequestrin and triadin. ► The SR is functional but possibly insignificant in neonatal rat cardiomyocytes.
