Chapter 4 Calsequestrin
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چکیده
I. Sarcoplasmic Reticulum ............................................................................. 152 II. Isolated Sarcoplasmic Reticulum Vesicles ................................................. 153 III. Isolation of Calsequestrin ........................................................................... 155 IV. Ca Binding by Calsequestrin ................................................................... 155 V. Size and Shape of Calsequestrin................................................................. 157 VI. Amino Acid Sequence ................................................................................ 159 VII. Carbohydrate Content................................................................................. 160 VIII. Stains-All Staining...................................................................................... 160 IX. Properties of Calsequestrin in Other Muscles............................................. 161 X. Phosphorylation of Calsequestrin ............................................................... 162 XI. Localization of Calsequestrin ..................................................................... 163 XII. Biosynthesis................................................................................................ 166 XIII. Calsequestrin in Disease ............................................................................. 168 References .................................................................................................. 168
منابع مشابه
Calsequestrin: more than 'only' a luminal Ca2+ buffer inside the sarcoplasmic reticulum.
In striated muscle, the sarcoplasmic reticulum (SR) Ca2+ release/ryanodine receptor (RyR) channel provides the pathway through which stored Ca2+ is released into the myoplasm during excitation-contraction coupling. Various luminal Ca2+-binding proteins are responsible for maintaining the free [Ca2+] at 10(-3)-10(-4) M in the SR lumen; in skeletal-muscle SR, it is mainly calsequestrin. Here we s...
متن کاملCharacterization of Post-Translational Modifications to Calsequestrins of Cardiac and Skeletal Muscle
Calsequestrin is glycosylated and phosphorylated during its transit to its final destination in the junctional sarcoplasmic reticulum. To determine the significance and universal profile of these post-translational modifications to mammalian calsequestrin, we characterized, via mass spectrometry, the glycosylation and phosphorylation of skeletal muscle calsequestrin from cattle (B. taurus), lab...
متن کاملMass spectrometry of cardiac calsequestrin characterizes microheterogeneity unique to heart and indicative of complex intracellular transit.
Cardiac calsequestrin concentrates in junctional sarcoplasmic reticulum in heart and skeletal muscle cells by an undefined mechanism. During transit through the secretory pathway, it undergoes an as yet uncharacterized glycosylation and acquires phosphate on CK2-sensitive sites. In this study, we have shown that active calsequestrin phosphorylation occurred in nonmuscle cells as well as muscle ...
متن کاملComparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization.
Calsequestrin, the major calcium storage protein of both cardiac and skeletal muscle, binds and releases large numbers of Ca(2+) ions for each contraction and relaxation cycle. Here we show that two crystal structures for skeletal and cardiac calsequestrin are nearly superimposable not only for their subunits but also their front-to-front-type dimers. Ca(2+) binding curves were measured using a...
متن کاملFast kinetics of calcium dissociation from calsequestrin.
We measured the kinetics of calcium dissociation from calsequestrin in solution or forming part of isolated junctional sarcoplasmic reticulum membranes by mixing calsequestrin equilibrated with calcium with calcium-free solutions in a stopped-flow system. In parallel, we measured the kinetics of the intrinsic fluorescence changes that take place following calcium dissociation from calsequestrin...
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