Sarcoplasmic reticulum

Martonosi, Anthony; Donley, J. R.; Pucell, Anthony G.; Halpin, Rita A.

doi:10.1016/0003-9861(71)90358-4

Cited by 104 publications

(25 citation statements)

References 21 publications

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“…Thus the increase of the content of unsaturated fatty acids in the lipid constituent of the sarcoplasmic reticulum membrane and the decrease in cholesterol content during development regulate the fluidity and, consequently, enzymic activity of this membrane. On the other hand, the data available so far concerning specific requirement for phospholipids containing unsaturated fatty acids for the reconstitution of the sarcoplasmic reticulum membrane in vitro are controversial [40,41].…”

Section: Discussionmentioning

confidence: 99%

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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Section: Discussionmentioning

confidence: 99%

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

et al. 1975

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“…Fragmented SRV were prepared from rabbits as in Abbreviations: SRV, sarcoplasmic reticulum vesicles; FITC, fluorescein isothiocyanate; AMP-P(NH)P, adenylyl imidodiphosphate Elsevier/North-Holland Biomedical Press [4]. Incubation of SRV with FITC was done at 20°C by suspending 150-225 pg SRV protein in 100 ~1 containing: 0.25 M sucrose, 25 mM Tris-HCl, 25 mM Na-glycine at the indicated pH and 100 PM EGTA.…”

Section: Methodsmentioning

confidence: 99%

Modification of the ATP binding site of the Ca²⁺‐ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate

1981

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“…The catalytic activity of many membrane-bound enzymes is dependent upon the presence of phospholipids (Martonosi et al, 1968;Strobel et al, 1970;Cater et al, 1975;Gazzotti et al, 1975). Similarly, a phospholipid requirement has been suggested for UDP-glucuronyltransferase (EC 2.4.1.17) activity.…”

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confidence: 98%

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

Tukey¹,

Billings²,

Autor³

et al. 1979

Biochemical Journal

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Hepatic UDP-glucuronyltransferase activity was resolved into two fractions, one exhibiting oestrone glucuronyltransferase activity and the other exhibiting p-nitrophenol glucuronyltransferase activity. Hydroxyapatite-column chromatography removed greater than 95 % of the phospholipids from both preparations. The partially purified delipidated enzymes were essentially devoid of catalytic activity, but activities were restored by the addition of phospholipids or phosphatidylcholine mixtures containing various saturated and unsaturated fatty acids. Both oestrone andp-nitrophenol glucuronyltransferase activities were reconstituted to similar degrees with the phosphatidylcholine mixtures. When purified phospholipids were tested, phosphatidylcholine and lysophosphatidylcholine were most effective in restoring activity, whereas phosphatidylethanolamine was the least effective. These results further suggest that oestrone and p-nitrophenol UDP-glucuronyltransferases are dependent on phospholipids for their activity.

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Sarcoplasmic reticulum

Cited by 104 publications

References 21 publications

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

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

Modification of the ATP binding site of the Ca²⁺‐ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

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Sarcoplasmic reticulum

Cited by 104 publications

References 21 publications

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

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

Modification of the ATP binding site of the Ca2+‐ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

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Modification of the ATP binding site of the Ca²⁺‐ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate