Source:http://linkedlifedata.com/resource/pubmed/id/10938436
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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001613,
umls-concept:C0007776,
umls-concept:C0021641,
umls-concept:C0022655,
umls-concept:C0027882,
umls-concept:C0031715,
umls-concept:C0086597,
umls-concept:C0202220,
umls-concept:C0205225,
umls-concept:C0205374,
umls-concept:C0442805,
umls-concept:C1720655,
umls-concept:C1947974,
umls-concept:C2700455
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pubmed:issue |
2
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pubmed:dateCreated |
2000-10-19
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pubmed:abstractText |
The modulation of tau phosphorylation and localization in response to insulin-like growth factor-1 or insulin was examined in primary cultures of rat cortical neurons. Insulin and insulin-like growth factor-1 treatment resulted in a rapid and transient increase in tau phosphorylation at specific epitopes. These effects were completely inhibited by lithium, revealing that the insulin and insulin-like growth factor-1 induced changes in tau phosphorylation were mediated by glycogen synthase kinase-3beta. In addition, the increase in tau phosphorylation directly correlated with a transient dissociation of tau from the cytoskeleton, indicating that insulin and insulin-like growth factor-1 treatment resulted in a change in tau localization. Using immunocytochemistry, it was also demonstrated that treatment of neurons with insulin-like growth factor-1 for 3 min resulted in a redistribution of tau to the growth cone and the distal segment of the axons. Further, insulin-like growth factor-1 treatment resulted in an increased immunoreactivity with the phospho-dependent antibody AT8 in the same areas of the axons. Thus, the phosphorylation state and distribution of tau can be modulated by insulin and insulin-like growth factor-1 signaling pathways involving glycogen synthase kinase-3beta. We propose that by transiently increasing tau phosphorylation, insulin and insulin-like growth factor-1 may contribute to the reorganization of the cytoskeleton necessary for the development and growth of the neurites.
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pubmed:grant | |
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:issn |
0306-4522
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
305-16
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10938436-Animals,
pubmed-meshheading:10938436-Cells, Cultured,
pubmed-meshheading:10938436-Cerebral Cortex,
pubmed-meshheading:10938436-Embryo, Mammalian,
pubmed-meshheading:10938436-Growth Cones,
pubmed-meshheading:10938436-Hypoglycemic Agents,
pubmed-meshheading:10938436-Insulin,
pubmed-meshheading:10938436-Insulin-Like Growth Factor I,
pubmed-meshheading:10938436-Neurites,
pubmed-meshheading:10938436-Phosphorylation,
pubmed-meshheading:10938436-Rats,
pubmed-meshheading:10938436-tau Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Insulin-like growth factor-1 and insulin mediate transient site-selective increases in tau phosphorylation in primary cortical neurons.
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pubmed:affiliation |
Department of Psychiatry and Behavioral Neurobiology, University of Alabama at Birmingham, Alabama 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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