MgADP Promotes Myosin Head Movement toward Actin at Low [Ca<sup>2+</sup>] to Increase Force Production and Ca<sup>2+</sup>-Sensitivity of Contraction in Permeabilized Porcine Myocardial Strips

MgADP Promotes Myosin Head Movement toward Actin at Low [Ca<sup>2+</sup>] to Increase Force Production and Ca<sup>2+</sup>-Sensitivity of Contraction in Permeabilized Porcine Myocardial Strips

Myosin cross-bridges dissociate from actin following Mg<sup>2+</sup>-adenosine triphosphate (MgATP) binding. Myosin hydrolyses MgATP into inorganic phosphate (P<sub>i</sub>) and Mg<sup>2+</sup>-adenosine diphosphate (ADP), and release of these hydrolysis products...

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Bibliographic Details
Main Authors: Peter O. Awinda, Weikang Ma, Kyrah L. Turner, Jing Zhao, Henry Gong, Mindy S. Thompson, Kenneth S. Campbell, Thomas C. Irving, Bertrand C. W. Tanner
Format: Article
Language:English
Published: MDPI AG 2022-12-01
Series:International Journal of Molecular Sciences
Subjects:
cardiac muscle
X-ray diffraction
thick-filament structure
muscle mechanics
myofilament function
Online Access:https://www.mdpi.com/1422-0067/23/23/15084

Internet

https://www.mdpi.com/1422-0067/23/23/15084

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