2021
DOI: 10.3390/ijms22052624
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Ca2+-ATPase Molecules as a Calcium-Sensitive Membrane-Endoskeleton of Sarcoplasmic Reticulum

Abstract: The Ca2+-transport ATPase of sarcoplasmic reticulum (SR) is an integral, transmembrane protein. It sequesters cytoplasmic calcium ions released from SR during muscle contraction, and causes muscle relaxation. Based on negative staining and transmission electron microscopy of SR vesicles isolated from rabbit skeletal muscle, we propose that the ATPase molecules might also be a calcium-sensitive membrane-endoskeleton. Under conditions when the ATPase molecules scarcely transport Ca2+, i.e., in the presence of AT… Show more

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Cited by 5 publications
(17 citation statements)
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“…They were performed using isolated scallop SR vesicles under the artificial, physiological conditions. The negative staining method employed has limitations because it involves staining with uranyl acetate and drying the sample [ 6 ]; some salt patterns might be formed during drying process and the drying process could itself disturb SR structures. Although these factors might have made the SR classification more complex, we consider the general trends reported to be representative and hope that the theory proposed will stimulate future in vivo study of the SR.…”
Section: Discussionmentioning
confidence: 99%
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“…They were performed using isolated scallop SR vesicles under the artificial, physiological conditions. The negative staining method employed has limitations because it involves staining with uranyl acetate and drying the sample [ 6 ]; some salt patterns might be formed during drying process and the drying process could itself disturb SR structures. Although these factors might have made the SR classification more complex, we consider the general trends reported to be representative and hope that the theory proposed will stimulate future in vivo study of the SR.…”
Section: Discussionmentioning
confidence: 99%
“…They will be the subject of a future study. Stabilization of the crystalline arrays by ATP, can be described based on the biological hydrotrope model of ATP [ 24 ], like rabbit Ca 2+ -ATPase crystals [ 6 ], i.e., ATP may return the structure of the scallop Ca 2+ -ATPase molecules into their intrinsic state to help crystallization. The inhibition of ATPase “two-rail” crystallization by TG alone might be specific to scallop, because the formation of two-rail-crystalline arrays of rabbit Ca 2+ -ATPase promoted by decavanadate [ 25 ] (an inhibitor of Ca 2+ -ATPase [ 26 ]) was further enhanced by TG [ 23 , 27 ].…”
Section: Discussionmentioning
confidence: 99%
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