Redox Regulation of Cardiac Muscle Calcium Signaling

2000 ◽  
Vol 2 (1) ◽  
pp. 65-71 ◽  
Author(s):  
Martin Morad ◽  
Yuichiro J. Suzuki
Keyword(s):  
Calcium Signaling ◽  
Cardiac Muscle ◽  
Redox Regulation ◽  
Muscle Calcium

scholarly journals Calmodulin Binding and Inhibition of Cardiac Muscle Calcium Release Channel (Ryanodine Receptor)

2001 ◽  
Vol 276 (23) ◽  
pp. 20144-20153 ◽  
Author(s):  
David M. Balshaw ◽  
Le Xu ◽  
Naohiro Yamaguchi ◽  
Daniel A. Pasek ◽  
Gerhard Meissner
Keyword(s):  
Cardiac Muscle ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Calmodulin Binding ◽  
Muscle Calcium

scholarly journals Multi-Cellular Functions of MG53 in Muscle Calcium Signaling and Regeneration

2020 ◽  
Vol 11 ◽  
Author(s):  
Dathe Z. Benissan-Messan ◽  
Hua Zhu ◽  
Weina Zhong ◽  
Tao Tan ◽  
Jianjie Ma ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Cellular Functions ◽  
Muscle Calcium

Molecular and Biological Studies on Cardiac Muscle Calcium-Binding Protein (TN-C)

1975 ◽  
Vol 53 (1) ◽  
pp. 15-20 ◽  
Author(s):  
L. D. Burtnick ◽  
W. D. McCubbin ◽  
C. M. Kay
Keyword(s):  
Cardiac Muscle ◽  
Calcium Binding ◽  
Sedimentation Coefficient ◽  
Inhibitory Effect ◽  
Similar Response ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Biological Studies ◽  
Cd Studies ◽  
Muscle Calcium

TN-C was purified from bovine cardiac muscle. In the absence of Ca2+, cardiac TN-C has an intrinsic sedimentation coefficient of 1.93 S and a molecular weight of 18 000 daltons. Cardiac TN-C reverses the inhibitory effect of skeletal TN-I on the Mg2+-activated ATPase of a skeletal synthetic actomyosin preparation in the presence of skeletal tropomyosin. Circular dichroism (CD) studies indicate that cardiac TN-C undergoes a major conformational Change upon binding Ca2+. A similar response is elicited by Sr2+, whereas Mg2+ has a much less pronounced effect. The presence of Mg2+ does not alter the net effects of either Ca2+ or Sr2+. Cardiac TN-C is rich in acidic amino acid residues. UV absorption, near UV CD, and fluorimetric studies show that the protein lacks tryptophan and has a relatively high phenylalanine to tyrosine ratio. The results of this study invite direct comparisons with results reported for the skeletal muscle analogue of cardiac TN-C.

scholarly journals Redox Regulation of Calcium Signaling in Cancer Cells by Ascorbic Acid Involving the Mitochondrial Electron Transport Chain

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Grigory G. Martinovich ◽  
Elena N. Golubeva ◽  
Irina V. Martinovich ◽  
Sergey N. Cherenkevich
Keyword(s):  
Ascorbic Acid ◽  
Electron Transport ◽  
Calcium Signaling ◽  
Electron Transport Chain ◽  
Redox Regulation ◽  
Complex Iii ◽  
Antimycin A ◽  
Ros Production ◽  
Mitochondrial Complex ◽  
Transport Chain

Previously, we have reported that ascorbic acid regulates calcium signaling in human larynx carcinoma HEp-2 cells. To evaluate the precise mechanism of Ca2+ release by ascorbic acid, the effects of specific inhibitors of the electron transport chain components on mitochondrial reactive oxygen species (ROS) production and Ca2+ mobilization in HEp-2 cells were investigated. It was revealed that the mitochondrial complex III inhibitor (antimycin A) amplifies ascorbate-induced Ca2+ release from intracellular stores. The mitochondrial complex I inhibitor (rotenone) decreases Ca2+ release from intracellular stores in HEp-2 cells caused by ascorbic acid and antimycin A. In the presence of rotenone, antimycin A stimulates ROS production by mitochondria. Ascorbate-induced Ca2+ release in HEp-2 cells is shown to be unaffected by catalase. The results obtained suggest that Ca2+ release in HEp-2 cells caused by ascorbic acid is associated with induced mitochondrial ROS production. The data obtained are in line with the concept of redox signaling that explains oxidant action by compartmentalization of ROS production and oxidant targets.

scholarly journals Postsynaptic CaV1.1-driven calcium signaling coordinates presynaptic differentiation at the developing neuromuscular junction

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Mehmet Mahsum Kaplan ◽  
Bernhard E. Flucher
Keyword(s):  
Neuromuscular Junction ◽  
Calcium Signaling ◽  
Motor Neurons ◽  
Motor Nerve ◽  
Neuromuscular Synapse ◽  
Presynaptic Differentiation ◽  
Motor Nerves ◽  
Muscle Calcium ◽  
Activity Dependent ◽  
Postsynaptic Target

AbstractProper formation of neuromuscular synapses requires the reciprocal communication between motor neurons and muscle cells. Several anterograde and retrograde signals involved in neuromuscular junction formation are known. However the postsynaptic mechanisms regulating presynaptic differentiation are still incompletely understood. Here we report that the skeletal muscle calcium channel (CaV1.1) is required for motor nerve differentiation and that the mechanism by which CaV1.1 controls presynaptic differentiation utilizes activity-dependent calcium signaling in muscle. In mice lacking CaV1.1 or CaV1.1-driven calcium signaling motor nerves are ectopically located and aberrantly defasciculated. Axons fail to recognize their postsynaptic target structures and synaptic vesicles and active zones fail to correctly accumulate at the nerve terminals opposite AChR clusters. These presynaptic defects are independent of aberrant AChR patterning and more sensitive to deficient calcium signals. Thus, our results identify CaV1.1-driven calcium signaling in muscle as a major regulator coordinating multiple aspects of presynaptic differentiation at the neuromuscular synapse.

Calcium Signaling in Cardiac Muscle

2010 ◽  
pp. 1027-1030
Author(s):  
K.M. Dibb ◽  
A.W. Trafford ◽  
D.A. Eisner
Keyword(s):  
Calcium Signaling ◽  
Cardiac Muscle
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