Intralumenal sarcoplasmic reticulum Ca (2+)-binding proteins.
SE Cala, BT Scott, LR Jones - Seminars in cell biology, 1990 - europepmc.org
SE Cala, BT Scott, LR Jones
Seminars in cell biology, 1990•europepmc.orgThe 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 …
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 …
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.
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