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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1982-10-29
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pubmed:abstractText |
Early postnatal changes (4-5 days to 15 days after birth) in the biochemical composition of microsomes were investigated in rabbit skeletal muscles destined to become fast-twitch muscles. During this period, a steady decrease in the microsomal content of cholesterol and of ouabain-sensitive Na + /K + -ATPase activity, as well as a decrease in protein electrophoretic components in the 80 000-70 000 molecular weight range, were observed. These changes are probably due to a diminishing yield of microsomal membranes derived from T-tubules, as the age of the animals increases, and are indicated from a knowledge of the mixed composition of muscle microsomes and previous biochemical data on isolated T-tubules. The content of cytochrome b5, which was found to be high in muscle microsomes of newborn animals, decreased strikingly as the amount of membrane-bound Ca2 + -ATPase protein increased, with a crossing-over point at about 7-10 days after birth. These changes, possibly corresponding to a transition from precursor sarcoplasmic reticulum (SR) to mature SR, were found to be temporally correlated with changes in [3H] alpha-tocopherol binding ability of the microsomes and in the mitochondrial content of glycerol phosphate dehydrogenase. At the same critical periods, coincident with the onset of motile activity, the immunological cross-reactivity of the Ca2 + -ATPase protein of microsomal vesicles, with antibody specific for the Ca2 + -ATPase of adult fast SR, was found to increase markedly, as tested by competitive enzyme-linked immunosorbent assay (ELISA). The immunological data are consistent with data in the literature demonstrating an increase in the concentration of Ca2 + -ATPase molecules in the SR membranes during ontogenic development. Both these data and catalytic data, however, suggest that the Ca2 + -ATPase protein is present in the same form in the SR of immature and of adult fast muscle and, in an antigenically different form, in slow muscle SR.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Calsequestrin,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0142-4319
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
213-30
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:6286721-Animals,
pubmed-meshheading:6286721-Calcium-Transporting ATPases,
pubmed-meshheading:6286721-Calsequestrin,
pubmed-meshheading:6286721-Intracellular Membranes,
pubmed-meshheading:6286721-Membrane Proteins,
pubmed-meshheading:6286721-Microsomes,
pubmed-meshheading:6286721-Mitochondria, Muscle,
pubmed-meshheading:6286721-Muscle Development,
pubmed-meshheading:6286721-Muscle Proteins,
pubmed-meshheading:6286721-Rabbits,
pubmed-meshheading:6286721-Sarcoplasmic Reticulum,
pubmed-meshheading:6286721-Sodium-Potassium-Exchanging ATPase
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pubmed:year |
1982
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pubmed:articleTitle |
Transitions in membrane composition during postnatal development of rabbit fast muscle.
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pubmed:publicationType |
Journal Article
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