Premium
NCS‐1 modulates expression of calcium handling proteins
Author(s) -
Telemaque Sabine,
Wang Zhen,
Liu MeeiYueh,
Buzdugan Larisa,
Liu S. Jesse
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.963.7
Subject(s) - phospholamban , contractility , serca , myocyte , microbiology and biotechnology , calcium , regulator , chemistry , sodium calcium exchanger , phosphorylation , calcium binding protein , cardiac function curve , biology , medicine , endocrinology , intracellular , biochemistry , heart failure , atpase , organic chemistry , gene , enzyme
We have previously shown that neuronal‐calcium sensor‐1 (NCS‐1) was present in rat heart and that overexpression of this small binding protein in isolated ventricular myocytes lead to an increase in contractile function. To further elucidate the physiological role of NCS‐1 in the heart, we examine cellular mechanisms by which overexpression of NCS‐1 could augment contractile function. Isolated adult rat ventricular myocytes were infected with adenovirus constructs (MOI: 100) expressing either NCS‐1 or β‐gal (control) for 48 hr. Cells were then washed and collected. Total cardiac lysate proteins were separated on SDS‐PAGE gels and expression levels of major E‐C coupling‐associated proteins were determined. Preliminary results suggest that expression of SERCA‐2a was decreased in the NCS‐1‐infected cells when compared to control cells. Expression of phospholamban (PLB), a negative regulator of SERCA‐2a activity, was unchanged while levels of phosphorylated PLB were significantly increased in NCS‐1‐infected cells, which is consistent with an increase in cardiac contractility. Finally, expression of NCX‐1 was not altered in the NCS‐1‐infected cells. Taken together, our data suggest that in addition to directly interacting with cardiac myofilament proteins, NCS‐1 may also regulate contractile function by modulating expression of key calcium handling proteins. Supported by UAMS Department of Medicine Seed Money Award (ST).