Browse by author
Lookup NU author(s): Morten Ritso
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Sarcolemma damage and activation of various calcium channels are implicated in altered Ca2+ homeostasis in muscle fibres of both Duchenne muscular dystrophy (DMD) sufferers and in the mdx mouse model of DMD. Previously we have demonstrated that also in mdx myoblasts extracellular nucleotides trigger elevated cytoplasmic Ca2+ concentrations due to alterations of both ionotropic and metabotropic purinergic receptors. Here we extend these findings to show that the mdx mutation is associated with enhanced store-operated calcium entry (SOCE). Substantially increased rate of SOCE in mdx myoblasts in comparison to that in control cells correlated with significantly elevated STIM1 protein levels. These results reveal that mutation in the dystrophin-encoding Dmd gene may significantly impact cellular calcium response to metabotropic stimulation involving depletion of the intracellular calcium stores followed by activation of the store-operated calcium entry, as early as in undifferentiated myoblasts. These data are in agreement with the increasing number of reports showing that the dystrophic pathology resulting from dystrophin mutations may be developmentally regulated. Moreover, our results showing that aberrant responses to extracellular stimuli may contribute to DMD pathogenesis suggest that treatments inhibiting such responses might alter progression of this lethal disease. (C) 2015 Elsevier Inc. All rights reserved.
Author(s): Onopiuk M, Brutkowski W, Young C, Krasowska E, Rog J, Ritso M, Wojciechowska S, Arkle S, Zablocki K, Gorecki DC
Publication type: Article
Publication status: Published
Journal: Archives of Biochemistry and Biophysics
Year: 2015
Volume: 569
Pages: 1-9
Print publication date: 01/03/2015
Online publication date: 04/02/2015
Acceptance date: 01/01/1900
ISSN (print): 0003-9861
ISSN (electronic): 1096-0384
Publisher: Elsevier
URL: http://dx.doi.org/10.1016/j.abb.2015.01.025
DOI: 10.1016/j.abb.2015.01.025
Altmetrics provided by Altmetric
