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Animal electricity, Ca2+ and muscle contraction. A brief history of muscle research

100%
Martonosi A. N.
Acta Biochimica Polonica
|
2000
|
vol. 47
|
issue 3
493-516
EN
This brief review attempts to summarize some of the major phases of muscle research from Leeuwenhoek's description of sarcomeres in 1674, through Galvani's observation of "animal electricity" in 1791, to the discovery of Ca2+ as the key messenger in the coupling of nerve excitation to muscle contraction. The emerging molecular mechanism of the contraction process is one of the great achievements of biology, reflecting the intimate links between physics, chemistry and the life Sciences in the solution of biological problems.
2
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The network of calcium regulation in muscle.

63%
Martonosi A. N., Pikula S.
Acta Biochimica Polonica
|
2003
|
vol. 50
|
issue 1
1-30
EN
In this review the molecular characteristics and reaction mechanisms of different Ca2+ transport systems associated with various membranes in muscle cells will be summarized. The following topics will be discussed in detail: a brief history of early observations concerning maintenance and regulation of cellular Ca2+ homeostasis, characterization of the Ca2+ pumps residing in plasma membranes and sarco(endo)plasmic reticulum, mitochondrial Ca2+ transport, Ca2+-binding proteins, coordinated expression of Ca2+ transport systems, a general background of muscle excitation-contraction coupling with emphasis to the calcium release channels of plasma membrane and sarcoplasmic reticulum, the structure and function of dihydropyridine and ryanodine receptors of skeletal and cardiac muscles, and finally their disposition in various types of muscles.
3
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The structure of the Ca2+-ATPase of sarcoplasmic reticulum.

63%
Martonosi A. N., Pikula S.
Acta Biochimica Polonica
|
2003
|
vol. 50
|
issue 2
337-365
EN
In this article the morphology of sarcoplasmic reticulum, classification of Ca2+-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca2+-ATPase determined by electron and X-ray crystallography, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca2+-ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca2+-ATPase to the sarcoplasmic reticulum is discussed.
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