Solubilization and Reaggregation of Sarcoplasmic Reticulum Membranes

Sarzala, M.G.; Zubrzycka, E; Pilarska, Maria; Drabikowski, W.

doi:10.1016/b978-0-08-017822-6.50021-6

Cited by 4 publications

(1 citation statement)

References 23 publications

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“…Although it was evident from earlier studies (12,14,18) that calsequestrin is a glycoprotein, accurate analysis of its sugar content has not yet been reported. The data presented in Table I show that calsequestrin contains only N-acetylglucosamine and mannose in a molar ratio of 1:2:3.…”

Section: Sugar Analysis Of Calsequestrinmentioning

confidence: 99%

Assembly of the sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures: localization by immunofluorescence of sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures

Jorgensen¹,

Kalnins²,

Zubrzyca³

et al. 1977

The Journal of Cell Biology

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Immunofluorescent staining techniques were used to study the distribution of the Ca 2+ + Mg2+-dependent ATPase and calsequestrin in primary cultures of differentiating rat skeletal muscle cells, grown for different periods of time under various culture conditions.In mononucleated myoblasts calsequestrin was detected after 45 h in culture whereas the ATPase was not detected until 60 h. After cell fusion began, both proteins could be identified in all multinucleated cells. Myoblasts grown for longer than 60 h in low Ca z+ medium contained calsequestrin and the ATPase, even though they were unable to fuse. These studies at the cellular level confirm biochemical findings on the biosynthesis of calsequestrin and the ATPase.Immunofluorescent staining of myoblasts showed that calsequestrin first appears in a well-defined region of the cell near one end of the nucleus. At later times, the staining occupied progressively larger regions adjacent to the nucleus and took on a fibrous appearance. This suggests that calsequestrin first accumulates in the Golgi region and then gradually spreads throughout the cell. In contrast, the ATPase appeared to be concentrated in many small patches or foci throughout the cytoplasm and was never confined to one particular region, although some parts of the cell often stained more intensely than others. In multinucleated cells, alternating dark and fluorescent strands parallel to the longitudinal axis of the cells were evident.Fluorescent staining with these antisera was not observed in fibroblasts which were also present in the cultures.Sarcoplasmic reticulum is the intracellular membrane system in muscle cells which regulates contraction by modulating the intracellular concentration of calcium ions (3). The relationship between the individual components of this membrane system and their function at the molecular level has been studied extensively (13). Very little is known, however, about the assembly of this membrane system during the maturation of muscle cells. Examination of the microsomal fractions isolated from embryonic and neonatal muscle, for their ability to transport Ca ++ in an ATP-depen-

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Section: Sugar Analysis Of Calsequestrinmentioning

confidence: 99%

Assembly of the sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures: localization by immunofluorescence of sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures

Jorgensen¹,

Kalnins²,

Zubrzyca³

et al. 1977

The Journal of Cell Biology

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Changes in the Structure, Composition and Function of Sarcoplasmic-Reticulum Membrane during Development

et al. 1975

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The structure, chemical composition and function of the microsomal fraction, isolated by differential centrifugation and purified on sucrose gradients, from muscle of fetal, newborn and young rabbits were characterized and compared with those of sarcoplasmic reticulum vesicles from adult muscle. Negative staining shows that the microsomal vesicles isolated from muscles of embryos and newborn animals are smooth, in contrast to vesicles obtained from adult muscle which contain 4‐nm particles on their surface. The particles appear first in the microsomal vesicles from muscles of 5–8‐day‐old rabbits. Their number increases with the age of the animals. Ca2+‐pump protein, with molecular weight about 100000, accounts for 10% of the total protein content in sarcoplasmic reticulum membrane, isolated at the earliest stages of development analysed. Its amount increases continuously with the rabbit's age to the adult value of about 70% of total sarcoplasmic reticulum protein. The low amount of 100000‐dalton protein and lack of 4‐nm surface particles in sarcoplasmic reticulum vesicles obtained from fetal and newborn rabbits are strictly correlated with the low activity of Ca2+‐dependent ATPase and the ability to take up Ca2+. These activities rise in parallel with the age of the rabbits. On the other hand, Mg2+‐dependent ATPase activity is very high at the early stages of development and declines continuously to a low value in sarcoplasmic reticulum from adult muscle. The sarcoplasmic reticulum membrane from fetal and newborn rabbits contains a higher amount of lipids as compared with the membrane present in the muscle of adult animals. The ratio of both phospholipid to protein and neutral lipid to protein decreases with the age of the rabbits. The composition of sarcoplasmic reticulum phospholipid also changes during development.

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A Study on the Influence of the Treatment by the Cleaned Soluble Proteins to the Fragmented Sarcoplasmic Reticulum

Joswik¹,

Заиков²,

Haghi³

2015

Life Chemistry Research

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Solubilization and Reaggregation of Sarcoplasmic Reticulum Membranes

Cited by 4 publications

References 23 publications

Assembly of the sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures: localization by immunofluorescence of sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures

Assembly of the sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures: localization by immunofluorescence of sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures

Changes in the Structure, Composition and Function of Sarcoplasmic-Reticulum Membrane during Development

A Study on the Influence of the Treatment by the Cleaned Soluble Proteins to the Fragmented Sarcoplasmic Reticulum

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