Document Detail

Characterization of junctate-SERCA2a interaction in murine cardiomyocyte.
MedLine Citation:
PMID:  19896466     Owner:  NLM     Status:  MEDLINE    
Junctate is a newly identified sarcoplasmic reticulum (SR) Ca(2+) binding protein, but its function in cardiac muscle has remained unclear. Our previous study showed that chronic over-expression of junctate in transgenic mice led to altered SR functions and development of severe hypertrophy. In this study, we identified the interaction of junctate with SERCA2a by co-immunoprecipitation and GST-pull-down assay. This interaction was inhibited by higher Ca(2+) concentration. Immunolocalization assays also showed that junctate and SERCA2a were co-localized in the SR of cardiomyocytes. Direct binding of the C-terminal region of junctate (amino acids 79-270) and luminal domain of SERCA2a (amino acids 70-89) was observed by deletion mutation experiments. Adenovirus-mediated transient over-expression of junctate in cardiomyocytes showed a reduced decay time of Ca(2+) transients and increased oxalate-supported SERCA2 Ca(2+) uptake, suggesting an increased activity of SERCA2a. Taken together, according to our data, junctate may play an important role in the regulation of SR Ca(2+) cycling through the interaction with SERCA2a in the murine heart.
Soon-Jae Kwon; Do Han Kim
Related Documents :
8568846 - Examination of the role of phosphorylation and phospholamban in the regulation of the c...
17159806 - Effect of some antioxidants on sarcoplasmic reticulum ca2+-atpase activity from rabbit ...
16517946 - Regulatory role of ovarian sex hormones in calcium uptake activity of cardiac sarcoplas...
9292226 - Effects of free oxygen radicals on ca2+ release mechanisms in the sarcoplasmic reticulu...
11399906 - Gaba(b) receptors in anterior pituitary cells. mechanism of action coupled to endocrine...
10369756 - Kinetic and thermodynamic stabilization of the betagamma-crystallin homolog spherulin 3...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-11-05
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  390     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-11-30     Completed Date:  2010-01-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1389-94     Citation Subset:  IM    
Department of Life Science and Systems Biology Research Center, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Calcium / metabolism*
Calcium-Binding Proteins / genetics,  metabolism*
Cells, Cultured
Membrane Proteins / genetics,  metabolism*
Mixed Function Oxygenases / genetics,  metabolism*
Muscle Proteins / genetics,  metabolism*
Myocytes, Cardiac / enzymology*
Protein Interaction Domains and Motifs
Rats, Sprague-Dawley
Sarcoplasmic Reticulum / enzymology*
Sarcoplasmic Reticulum Calcium-Transporting ATPases / genetics,  metabolism*
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/Membrane Proteins; 0/Muscle Proteins; 7440-70-2/Calcium; EC 1.-/Asph protein, mouse; EC 1.-/Mixed Function Oxygenases; EC protein, mouse; EC Reticulum Calcium-Transporting ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Circulating microRNA-1 as a potential novel biomarker for acute myocardial infarction.
Next Document:  Functional Links Between Diacylglycerol and Phosphatidylinositol Signaling Systems in Human Leukocyt...