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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
|
pubmed:dateCreated |
1981-3-24
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pubmed:abstractText |
Polypeptide composition and endogenous phosphorylation were investigated in the subfractions of rat brain myelin isolated by either discontinuous or continuous sucrose density gradient centrifugation of myelin. Similarly, a myelin-like membrane fraction (SN4) was also studied. Observations were made that strongly indicated the presence of a calcium-stimulated protein kinase in a highly purified myelin preparation and which exclusively phosphorylated myelin basic proteins of the membrane preparation. Adenosine cyclic 3',5'-phosphate (cAMP) stimulated kinase on the other hand was found to be considerably enriched in the myelin-like membrane fraction. Although this latter enzyme is also capable of phosphorylating the basic proteins, its effect was at least 5 times weaker compared to the calcium-stimulated myelin protein kinase. Within the gradient subfractions there appeared a close relation between the amount of basic proteins and their calcium-stimulated phosphorylation; a similar relationship, however, was not obtained in the case of cAMP-dependent phosphorylation of myelin basic proteins. The former (i.e., Ca2+-stimulated phosphorylation) was found to require a protein factor that functionally resembled calmodulin. The results thus raises an interesting possibility of the presence of calmodulin-like proteins and a calcium-stimulated protein kinase in adult myelin membrane from mammalian brain, both of which have been hitherto unrecognized constituents of myelin membranes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
|
pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
|
pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
5363-71
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6160873-Animals,
pubmed-meshheading:6160873-Brain,
pubmed-meshheading:6160873-Calcium,
pubmed-meshheading:6160873-Calmodulin,
pubmed-meshheading:6160873-Centrifugation, Density Gradient,
pubmed-meshheading:6160873-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6160873-Male,
pubmed-meshheading:6160873-Myelin Basic Proteins,
pubmed-meshheading:6160873-Myelin Sheath,
pubmed-meshheading:6160873-Phosphorylation,
pubmed-meshheading:6160873-Protein Kinases,
pubmed-meshheading:6160873-Rats
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pubmed:year |
1980
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pubmed:articleTitle |
Calcium ion stimulated endogenous protein kinase catalyzed phosphorylation of basic proteins in myelin subfractions and myelin-like membrane fraction from rat brain.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|