Cala S E, Scott B T, Jones L R
Department of Medicine, Krannert Institute of Cardiology, Indiana University School of Medicine, Indianapolis 46202.
Semin Cell Biol. 1990 Aug;1(4):265-75.
The sarcoplasmic reticulum (SR) controls the level of intracellular Ca2+ in cardiac and skeletal muscle by storing and releasing Ca2+. A set of intralumenal SR Ca(2+)-binding proteins has been identified that may serve important roles in SR Ca2+ storage and mobilization. The most prominent of these SR proteins, calsequestrin, is discretely localized to junctional SR. Other intralumenal proteins are more widely distributed throughout the SR. All of these intralumenal SR Ca(2+)-binding proteins are acidic, stain blue with dye Stains-All, and appear to be substrates for casein kinase II. The biochemistry and cell biology of lumenal SR proteins may conform to a paradigm now emerging from the study of endoplasmic reticulum proteins.
肌浆网（SR）通过储存和释放钙离子来控制心肌和骨骼肌细胞内钙离子的水平。已鉴定出一组腔内肌浆网钙离子结合蛋白，它们可能在肌浆网钙离子储存和动员中发挥重要作用。这些肌浆网蛋白中最突出的是肌集钙蛋白，它离散地定位于连接肌浆网。其他腔内蛋白在整个肌浆网中分布更广泛。所有这些腔内肌浆网钙离子结合蛋白都是酸性的，用全染染料染成蓝色，并且似乎是酪蛋白激酶II的底物。腔内肌浆网蛋白的生物化学和细胞生物学可能符合目前从内质网蛋白研究中出现的一种模式。
