Document Detail


Sorcin modulates mitochondrial Ca(2+) handling and reduces apoptosis in neonatal rat cardiac myocytes.
MedLine Citation:
PMID:  23151801     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sorcin localizes in cellular membranes and has been demonstrated to modulate cytosolic Ca(2+) handling in cardiac myocytes. Sorcin also localizes in mitochondria; however, the effect of sorcin on mitochondrial Ca(2+) handling is unknown. Using mitochondrial pericam, we measured mitochondrial Ca(2+) concentration and fluxes in intact neonatal cardiac myocytes overexpressing sorcin. Our results showed that sorcin increases basal and caffeine-stimulated mitochondrial Ca(2+) concentration. This effect was associated with faster Ca(2+) uptake and release. The effect of sorcin was specific for mitochondria, since similar results were obtained with digitonin-permeabilized cells, where cytosolic Ca(2+) flux was disrupted. Furthermore, mitochondria of cardiac myocytes in which sorcin was overexpressed were more Ca(2+)-tolerant. Experiments analyzing apoptotic signaling demonstrated that sorcin prevented 2-deoxyglucose-induced cytochrome c release. Furthermore, sorcin prevented hyperglycemia-induced cytochrome c release and caspase activation. In contrast, antisense sorcin induced caspase-3 activation. Thus, sorcin antiapoptotic properties may be due to modulation of mitochondrial Ca(2+) handling in cardiac myocytes.
Authors:
Jorge Suarez; Patrick M McDonough; Brian T Scott; Angelica Suarez-Ramirez; Hong Wang; Eduardo S Fricovsky; Wolfgang H Dillmann
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-11-14
Journal Detail:
Title:  American journal of physiology. Cell physiology     Volume:  304     ISSN:  1522-1563     ISO Abbreviation:  Am. J. Physiol., Cell Physiol.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-04     Completed Date:  2013-06-10     Revised Date:  2014-02-04    
Medline Journal Info:
Nlm Unique ID:  100901225     Medline TA:  Am J Physiol Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  C248-56     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Apoptosis / drug effects,  physiology*
Caffeine / pharmacology
Calcium / metabolism*
Calcium-Binding Proteins / metabolism*
Caspase 3 / metabolism
Cytochromes c / metabolism
Mitochondria / drug effects,  metabolism*
Myocytes, Cardiac / cytology,  drug effects,  metabolism*
Rats
Grant Support
ID/Acronym/Agency:
3R01 HL-066917-10S1/HL/NHLBI NIH HHS; HL-52496/HL/NHLBI NIH HHS; HL-66917/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/sorcin protein, rat; 3G6A5W338E/Caffeine; 9007-43-6/Cytochromes c; EC 3.4.22.-/Caspase 3; SY7Q814VUP/Calcium
Comments/Corrections

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


Previous Document:  One hundred years of helicene chemistry. Part 1: non-stereoselective syntheses of carbohelicenes.
Next Document:  Definitive evidence using enucleated cytoplasts for a nongenomic basis for the cystic change in endo...