Document Detail


Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion.
MedLine Citation:
PMID:  18420707     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Myoblast fusion is essential for muscle development, postnatal growth and muscle repair after injury. Recent studies have demonstrated roles for actin polymerization during myoblast fusion. Dynamic cytoskeletal assemblies directing cell-cell contact, membrane coalescence and ultimately fusion require substantial cellular energy demands. Various energy generating systems exist in cells but the partitioning of energy sources during myoblast fusion is unknown. Here, we demonstrate a novel role for phosphocreatine (PCr) as a spatiotemporal energy buffer during primary mouse myoblast fusion with nascent myotubes. Creatine treatment enhanced cell fusion in a creatine kinase (CK)-dependent manner suggesting that ATP-consuming reactions are replenished through the PCr/CK system. Furthermore, selective inhibition of actin polymerization prevented myonuclear addition following creatine treatment. As myotube formation is dependent on cytoskeletal reorganization, our findings suggest that PCr hydrolysis is coupled to actin dynamics during myoblast fusion. We conclude that myoblast fusion is a high-energy process, and can be enhanced by PCr buffering of energy demands during actin cytoskeletal rearrangements in myoblast fusion. These findings implicate roles for PCr as a high-energy phosphate buffer in the fusion of multiple cell types including sperm/oocyte, trophoblasts and macrophages. Furthermore, our results suggest the observed beneficial effects of oral creatine supplementation in humans may result in part from enhanced myoblast fusion.
Authors:
Roddy S O'Connor; Craig M Steeds; Robert W Wiseman; Grace K Pavlath
Related Documents :
565787 - Transfer of human chromosomes via human minisegregant cells into mouse cells and the qu...
15010527 - Characterization of severe acute respiratory syndrome-associated coronavirus (sars-cov)...
9611827 - Biotransformation of digitoxigenin by cultured strophanthus hybrid cells.
1849407 - Regulated expression of cytochrome p-450scc (cholesterol-side-chain cleavage enzyme) in...
17211937 - "the adipocyte: a multifunctional cell".
7777587 - Establishment and characterization of human fetal liver epithelial cell line transfecte...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2008-04-17
Journal Detail:
Title:  The Journal of physiology     Volume:  586     ISSN:  1469-7793     ISO Abbreviation:  J. Physiol. (Lond.)     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-06-16     Completed Date:  2008-08-21     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  0266262     Medline TA:  J Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  2841-53     Citation Subset:  IM    
Affiliation:
Emory University, Department of Pharmacology, 1510 Clifton Rd, Room 5027, Atlanta, GA 30322, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Actins / physiology*,  ultrastructure
Animals
Cell Fusion
Cells, Cultured
Creatine Kinase / metabolism*
Cytoskeleton / physiology*,  ultrastructure*
Humans
Mice
Mice, Inbred BALB C
Myoblasts / cytology*,  physiology*
Phosphocreatine / metabolism*
Signal Transduction / physiology*
Grant Support
ID/Acronym/Agency:
AR047314/AR/NIAMS NIH HHS; AR051372/AR/NIAMS NIH HHS; AR052730/AR/NIAMS NIH HHS; R01 AR047314-10/AR/NIAMS NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 67-07-2/Phosphocreatine; EC 2.7.3.2/Creatine Kinase
Comments/Corrections
Comment In:
J Physiol. 2008 Jun 15;586(Pt 12):2817-8   [PMID:  18556720 ]

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


Previous Document:  How do tonic glutamatergic synapses evade receptor desensitization?
Next Document:  Role of sarcolemmal ATP-sensitive K+ channels in the regulation of sinoatrial node automaticity: an ...