Store-operated Ca2+ entry in muscle physiology and diseases
Ca2+ release from intracellular stores and influx from extracellular reservoir regulate a wide range of physiological functions including muscle contraction and rhythmic heartbeat. One of the most ubiquitous pathways involved in controlled Ca2+ influx into cells is store-operated Ca2+ entry (SOCE),...
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Korean Society for Biochemistry and Molecular Biology
2014
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pubmed-39674122014-08-01 Store-operated Ca2+ entry in muscle physiology and diseases Pan, Zui Brotto, Marco Ma, Jianjie Review Article Ca2+ release from intracellular stores and influx from extracellular reservoir regulate a wide range of physiological functions including muscle contraction and rhythmic heartbeat. One of the most ubiquitous pathways involved in controlled Ca2+ influx into cells is store-operated Ca2+ entry (SOCE), which is activated by the reduction of Ca2+ concentration in the lumen of endoplasmic or sarcoplasmic reticulum (ER/SR). Although SOCE is pronounced in non-excitable cells, accumulating evidences highlight its presence and important roles in skeletal muscle and heart. Recent discovery of STIM proteins as ER/SR Ca2+ sensors and Orai proteins as Ca2+ channel pore forming unit expedited the mechanistic understanding of this pathway. This review focuses on current advances of SOCE components, regulation and physiologic and pathophysiologic roles in muscles. The specific property and the dysfunction of this pathway in muscle diseases, and new directions for future research in this rapidly growing field are discussed. [BMB Reports 2014; 47(2): 69-79] Korean Society for Biochemistry and Molecular Biology 2014-02 /pmc/articles/PMC3967412/ /pubmed/24411466 http://dx.doi.org/10.5483/BMBRep.2014.47.2.015 Text en Copyright © 2014, Korean Society for Biochemistry and Molecular Biology http://creativecommons.org/licenses/by-nc/3.0 This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Pan, Zui Brotto, Marco Ma, Jianjie |
spellingShingle |
Pan, Zui Brotto, Marco Ma, Jianjie Store-operated Ca2+ entry in muscle physiology and diseases |
author_facet |
Pan, Zui Brotto, Marco Ma, Jianjie |
author_sort |
Pan, Zui |
title |
Store-operated Ca2+ entry in muscle physiology and diseases |
title_short |
Store-operated Ca2+ entry in muscle physiology and diseases |
title_full |
Store-operated Ca2+ entry in muscle physiology and diseases |
title_fullStr |
Store-operated Ca2+ entry in muscle physiology and diseases |
title_full_unstemmed |
Store-operated Ca2+ entry in muscle physiology and diseases |
title_sort |
store-operated ca2+ entry in muscle physiology and diseases |
description |
Ca2+ release from intracellular stores and influx from extracellular reservoir regulate a wide range of physiological functions including muscle contraction and rhythmic heartbeat. One of the most ubiquitous pathways involved in controlled Ca2+ influx into cells is store-operated Ca2+ entry (SOCE), which is activated by the reduction of Ca2+ concentration in the lumen of endoplasmic or sarcoplasmic reticulum (ER/SR). Although SOCE is pronounced in non-excitable cells, accumulating evidences highlight its presence and important roles in skeletal muscle and heart. Recent discovery of STIM proteins as ER/SR Ca2+ sensors and Orai proteins as Ca2+ channel pore forming unit expedited the mechanistic understanding of this pathway. This review focuses on current advances of SOCE components, regulation and physiologic and pathophysiologic roles in muscles. The specific property and the dysfunction of this pathway in muscle diseases, and new directions for future research in this rapidly growing field are discussed. [BMB Reports 2014; 47(2): 69-79] |
publisher |
Korean Society for Biochemistry and Molecular Biology |
publishDate |
2014 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3967412/ |
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1612071722170712064 |