Differential Ca2+ sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin

Performed cross-linking experiments that identified both RyR1 and RyR2 as predominant Calmodulin (CaM) binding proteins in skeletal and cardiac sarcoplasmic reticulum, respectively and [35S]CaM binding determination further indicated comparable CaM binding to the two isoforms in the presence of micr...

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Veröffentlicht in:	American Journal of Physiology: Cell Physiology 2000-09, Vol.48 (3), p.C724-C733
Hauptverfasser:	FRUEN, B. R, BARDY, J. M, BYREM, T. M, STRASBURG, G. M, LOUIS, C. F
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Calcium Cell physiology Cellular biology Fundamental and applied biological sciences. Psychology Molecular and cellular biology Muscle contraction Muscular system Skeletal system
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container_title	American Journal of Physiology: Cell Physiology
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creator	FRUEN, B. R BARDY, J. M BYREM, T. M STRASBURG, G. M LOUIS, C. F
description	Performed cross-linking experiments that identified both RyR1 and RyR2 as predominant Calmodulin (CaM) binding proteins in skeletal and cardiac sarcoplasmic reticulum, respectively and [35S]CaM binding determination further indicated comparable CaM binding to the two isoforms in the presence of micromolar Ca2+. CaM activates RyR1 and RyR2 isoforms that may potentially contribute to differences in the Ca2+ dependence of channel activation in skeletal and cardiac muscle.
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R ; BARDY, J. M ; BYREM, T. M ; STRASBURG, G. M ; LOUIS, C. F</creator><creatorcontrib>FRUEN, B. R ; BARDY, J. M ; BYREM, T. M ; STRASBURG, G. M ; LOUIS, C. F</creatorcontrib><description>Performed cross-linking experiments that identified both RyR1 and RyR2 as predominant Calmodulin (CaM) binding proteins in skeletal and cardiac sarcoplasmic reticulum, respectively and [35S]CaM binding determination further indicated comparable CaM binding to the two isoforms in the presence of micromolar Ca2+. 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F</creatorcontrib><title>Differential Ca2+ sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin</title><title>American Journal of Physiology: Cell Physiology</title><description>Performed cross-linking experiments that identified both RyR1 and RyR2 as predominant Calmodulin (CaM) binding proteins in skeletal and cardiac sarcoplasmic reticulum, respectively and [35S]CaM binding determination further indicated comparable CaM binding to the two isoforms in the presence of micromolar Ca2+. CaM activates RyR1 and RyR2 isoforms that may potentially contribute to differences in the Ca2+ dependence of channel activation in skeletal and cardiac muscle.</description><subject>Biological and medical sciences</subject><subject>Calcium</subject><subject>Cell physiology</subject><subject>Cellular biology</subject><subject>Fundamental and applied biological sciences. 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F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential Ca2+ sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><date>2000-09-01</date><risdate>2000</risdate><volume>48</volume><issue>3</issue><spage>C724</spage><epage>C733</epage><pages>C724-C733</pages><issn>0363-6143</issn><eissn>1522-1563</eissn><coden>AJPCDD</coden><abstract>Performed cross-linking experiments that identified both RyR1 and RyR2 as predominant Calmodulin (CaM) binding proteins in skeletal and cardiac sarcoplasmic reticulum, respectively and [35S]CaM binding determination further indicated comparable CaM binding to the two isoforms in the presence of micromolar Ca2+. 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source	American Physiological Society; EZB-FREE-00999 freely available EZB journals
subjects	Biological and medical sciences Calcium Cell physiology Cellular biology Fundamental and applied biological sciences. Psychology Molecular and cellular biology Muscle contraction Muscular system Skeletal system
title	Differential Ca2+ sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin
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